Amended on 18 October 2017 (I would like to dedicate this answer to 350,000 citizens of Hiroshima (on 6 August 1945; Hiroshima, Japan) and of Nagasaki (on 9 August 1945; Nagasaki, Japan) deceased by atomic bombs) 

I have searched IGF-1 in my HCC specimens in vain by using new proteomics (PDMD method; Protein-Direct-Microsequencing-Deciphering method) based upon the famous Edman degradation method.   Famous Swedish Biochemist Dr. Per Victor Edman (Karolinska Institutet, Solna, Stockholm County, Sweden) has firstly invented the Edman degradation method (please see file; HepG2 Fucoidan). Only,  HCC tissue (with PBC; the aged Japanese woman) has Insulin-like growth factor-binding protein 5/IGFBP-5 at 3.0, and Insulin-like growth factor binding-protein 3/IGFBP-3 at 0.7 μg/mg of tissue protein, respectively.   

Vasoactive intestinal polypeptide receptor 1/VIP-R-1 is only present as a peptide-hormone receptor at 3.8 μg/mg of milk protein in a human milk.   Although peptide hormone is not present in human breast milk, these proteins may be working as protein hormones; i.e., Tetraspanin-14 at 33.8,  Docking protein 1 at 7.7, and Synaptotagmin-1 at 5.8  μg/mg of human milk protein, respectively.   Docking protein 1 is an inhibitor to the insulin receptor. Interestingly, bovine milk of Japan has no these proteins.

I agree with Dr. Ram B Singh (Halberg Hospital and Research Institute, Moradabad, India) that "Yes, milk from animals fed industrial food". If bovine has been fed bovine growth hormone, increase of IGF-1 may occur. Japanese, Austrarian, and New Zealand's bovine may have not given or injected the growth hormone. Steroid hormones as growth factor seem to be not related to cancer, but natural food seems to be better than industrial food.

Therefore, I do not agree that IGF-1 in bovine milk is linked to cancer at all, and IGF-1 protein is not present in Japanese human breast milk and Japanese bovine milk.   IGF-1 has been measured by notorious ELISA method, and usually false results are obtained.   I would like to say that ELISA and PCR methods are not quantitative methods, which do not show the linear calibration-lines at all (Please see file; RIA Yalow (Yalow, RS & Berson, SA (1960). Immunoassay of endogenous plasma insulin in man. J Clin Invest. 39, 1157–75), and Mullis KB & Faloona FA (1985) Specific synthesis of DNA in vitro via a polymerase-catalyzed chain reaction, Methods Enzymol 155, 335-50).   My teacher Late Prof. Dr. Kunio Yamauchi (famous Japanese Milk Scientist of The University of Tokyo, Tokyo, Japan) has said that Methods in Enzymology is not the Journal with reviewer.   The reviewers of Journal of Clinical Investigation have made a mistake at that time.   The importance of linear calibration line in the determination in science has been already indicated by French Astronomer Dr. Pierre Bouguer, Swiss Chemist Dr. Johann Heinrich Lambert, and German Physicist and Chemist Dr. August Beer.    

By the way, human cancer is caused by co-infection of HIV-1 (retrovirus; Gag-Pol polyprotein with reverse transcriptase (RT) and integrase (IN)) and flavivirus (+ssRNA; Genome polyprotein) with Serine protease NS3 and Non-structural proteins NS4A, NS4B (with transcription factor activity) of HCV in the case of HCC.   Then, bovine milk seems to be safe to take adequate volume (please see file; Feed by Measure).

A human breast milk of a healthy Japanese mother has Structural polyprotein (Sindbis virus; SINV; Togavirus) but has no HIV-1 virus, and her child has no risk if the child keep away from HIV-1.   Similarly, a Japanese bovine milk has Genome polyprotein (Dengue virus 3; DENV-3; Flavivus) and Structural polyprotein/p130 (Sagiyama virus; SAGV; Togavirus).   Therefore, children drinking milk should keep away from HIV-1, if these enveloped +ssRNA virus (Flavivirus (Genome polyprotein) and Togavirus (Non-structural polyprotein)) have Serine protease activity and Transcription factor activity.

Thus, only the co-infection of two virus (HIV-1 and Flavivirus or Togavirus) becomes to be the risk factor.   Then, I think that the gene therapy method using iPS and/or STAP is dangerous to increase the risk, since cultured cells already have been invaded by considerable amount of virus (7.2% of cell protein in HepG2 and 5.0% of cell protein in fetal hepatocyte Hc).   Hepatoma HepG2 has both of HCV and HIV-1, on the other hand normal fetal Hc has HCV and DENV and HIV-2 but has not the HIV-1.   It is noteworthy that one liver cancer patient has HCV and SIV, but this patient has been alived; i.e., co-infection of HIV-2 and/or SIV together with HCV does not cause the true cancer.

Do you think this is helpful? https://academic.oup.com/jnci/article/93/17/1330/2519487

"Milk and dietary calcium may have antiproliferative effects against colorectal cancer, but milk intake also raises serum levels of insulin-like growth factor-I (IGF-I). A high ratio of IGF-I to IGF-binding protein-3 (IGFBP-3) has been linked to an increased risk of colorectal cancer."

And this one: https://link.springer.com/article/10.1007/s10552-017-0883-1

"IGF-I is a potential mechanism underlying the observed associations between milk intake and prostate cancer risk."

This issue is still inconclusive. Milk is one of the foods that contains almost all essential nutrients. However, it can also increase the level of IGF-1. The dietary benefits are well known. But the association with cancer risk is still to be proven. It might be a nice issue to think and discuss.....@ Geir Bjorklund 

Does drinking milk increase your IGF levels?

(https://nutritionovereasy.com/2016/03/does-drinking-milk-increase-your-igf-levels/)

Insulin-like growth Factor 1 (IGF-1)

(https://www.whitelies.org.uk/health-nutrition/insulin-growth-factor-1-igf-1)

Milk as a food for growth? The insulin-like growth factors link

(https://www.cambridge.org/core/services/aop-cambridge-core/content/view/323CC71BF88C8C3856B23BD215BF029B/S1368980006000644a.pdf/milk_as_a_food_for_growth_the_insulinlike_growth_factors_link.pdf)

Dear Geir,

There is no believable/hard evidence that the milk or milk products may cause or increase the risk of cancer. Such studies would be very hard to control/monitor and how would the study exclude many many other factors. My ancestors and my entire extended family is dairy farmers for many generations and consume alot of milk and milk products pretty much every day and throughout their lives- And no-one ever in my extended family developed any form of cancer, or died of cancer. Therefore I think the suggested link between milk and cancer is just a speculation.

Best wishes,

Refik

Yes, milk from animals fed industrial food

Amended on 18 October 2017 (I would like to dedicate this answer to 350,000 citizens of Hiroshima (on 6 August 1945; Hiroshima, Japan) and of Nagasaki (on 9 August 1945; Nagasaki, Japan) deceased by atomic bombs) 

I have searched IGF-1 in my HCC specimens in vain by using new proteomics (PDMD method; Protein-Direct-Microsequencing-Deciphering method) based upon the famous Edman degradation method.   Famous Swedish Biochemist Dr. Per Victor Edman (Karolinska Institutet, Solna, Stockholm County, Sweden) has firstly invented the Edman degradation method (please see file; HepG2 Fucoidan). Only,  HCC tissue (with PBC; the aged Japanese woman) has Insulin-like growth factor-binding protein 5/IGFBP-5 at 3.0, and Insulin-like growth factor binding-protein 3/IGFBP-3 at 0.7 μg/mg of tissue protein, respectively.   

Vasoactive intestinal polypeptide receptor 1/VIP-R-1 is only present as a peptide-hormone receptor at 3.8 μg/mg of milk protein in a human milk.   Although peptide hormone is not present in human breast milk, these proteins may be working as protein hormones; i.e., Tetraspanin-14 at 33.8,  Docking protein 1 at 7.7, and Synaptotagmin-1 at 5.8  μg/mg of human milk protein, respectively.   Docking protein 1 is an inhibitor to the insulin receptor. Interestingly, bovine milk of Japan has no these proteins.

I agree with Dr. Ram B Singh (Halberg Hospital and Research Institute, Moradabad, India) that "Yes, milk from animals fed industrial food". If bovine has been fed bovine growth hormone, increase of IGF-1 may occur. Japanese, Austrarian, and New Zealand's bovine may have not given or injected the growth hormone. Steroid hormones as growth factor seem to be not related to cancer, but natural food seems to be better than industrial food.

Therefore, I do not agree that IGF-1 in bovine milk is linked to cancer at all, and IGF-1 protein is not present in Japanese human breast milk and Japanese bovine milk.   IGF-1 has been measured by notorious ELISA method, and usually false results are obtained.   I would like to say that ELISA and PCR methods are not quantitative methods, which do not show the linear calibration-lines at all (Please see file; RIA Yalow (Yalow, RS & Berson, SA (1960). Immunoassay of endogenous plasma insulin in man. J Clin Invest. 39, 1157–75), and Mullis KB & Faloona FA (1985) Specific synthesis of DNA in vitro via a polymerase-catalyzed chain reaction, Methods Enzymol 155, 335-50).   My teacher Late Prof. Dr. Kunio Yamauchi (famous Japanese Milk Scientist of The University of Tokyo, Tokyo, Japan) has said that Methods in Enzymology is not the Journal with reviewer.   The reviewers of Journal of Clinical Investigation have made a mistake at that time.   The importance of linear calibration line in the determination in science has been already indicated by French Astronomer Dr. Pierre Bouguer, Swiss Chemist Dr. Johann Heinrich Lambert, and German Physicist and Chemist Dr. August Beer.    

By the way, human cancer is caused by co-infection of HIV-1 (retrovirus; Gag-Pol polyprotein with reverse transcriptase (RT) and integrase (IN)) and flavivirus (+ssRNA; Genome polyprotein) with Serine protease NS3 and Non-structural proteins NS4A, NS4B (with transcription factor activity) of HCV in the case of HCC.   Then, bovine milk seems to be safe to take adequate volume (please see file; Feed by Measure).

A human breast milk of a healthy Japanese mother has Structural polyprotein (Sindbis virus; SINV; Togavirus) but has no HIV-1 virus, and her child has no risk if the child keep away from HIV-1.   Similarly, a Japanese bovine milk has Genome polyprotein (Dengue virus 3; DENV-3; Flavivus) and Structural polyprotein/p130 (Sagiyama virus; SAGV; Togavirus).   Therefore, children drinking milk should keep away from HIV-1, if these enveloped +ssRNA virus (Flavivirus (Genome polyprotein) and Togavirus (Non-structural polyprotein)) have Serine protease activity and Transcription factor activity.

Thus, only the co-infection of two virus (HIV-1 and Flavivirus or Togavirus) becomes to be the risk factor.   Then, I think that the gene therapy method using iPS and/or STAP is dangerous to increase the risk, since cultured cells already have been invaded by considerable amount of virus (7.2% of cell protein in HepG2 and 5.0% of cell protein in fetal hepatocyte Hc).   Hepatoma HepG2 has both of HCV and HIV-1, on the other hand normal fetal Hc has HCV and DENV and HIV-2 but has not the HIV-1.   It is noteworthy that one liver cancer patient has HCV and SIV, but this patient has been alived; i.e., co-infection of HIV-2 and/or SIV together with HCV does not cause the true cancer.

According to Dr. Viji Viji (Chaoyang University of Technology, Department of Applied Chemistry, Taiwan), I have searched the PDMD data of milks.   Although research of lactoferrin seems difficult (please see file; LF Dr. Kawakami (in Japanese)), I think that Fe is an important growth factor like vitamin H for cultured cells and bacteria (our unpublished observation at Gunma University (Maebashi, Gunma, Japan)).

Cow's milk has major secreted proteins of (1) α-Lactalbumin (20- of precursor, 1- of mature) at 110.0, (2) α s1 Casein (16- of precursor, 1- of mature) at 101.1, (3) β- Casein (16- of precursor, 1- of mature)  at 78.8, and (4) κ- Casein (22- of precursor, 1- of mature) at 74.3 μg/mg of milk protein, respectively.

Human breast milk has major secreted proteins of (1) α-Lactalbumin (20- of precursor, 1- of mature)　at 156.0, (2) β-Casein　（16- of precursor; １－of mature） at 127.5, (3) Lactoferrin (LF; 20- of precursor; 1- of mature) at 83.0, and (4) Lysozyme (human sequence; 19- of precursor; 1- of mature)  at 30.9 μg/mg of milk protein, respectively.

Therefore, human breast milk has a higher antibacterial and antiviral activity as compared to cow's milk.

But cow's milk also has Lysozyme (Bovine sequence; 19- of precursor; 1- of mature) at 11.2 μg/mg of milk protein and Lactoferrin (LF; 20- of precursor; 1- of mature)  at 3.0 μg/mg of milk protein.

Therefore, the risk to become cancers via co-infection of two virus (HIV-1 and Flavivirus or Togavirus) becomes to be very low in milk drinking. 

Amended on 24 August 2017

Antimicrobe activity in the foodstuffs is very important issue.   Hen's egg-white protects egg-yolk, which is rich in various nutritions such as biotin (vitamin H) and lipoic acid (thioctic acid), by using Ovotransferrin/Conalbumin (Fe binding protein), Avidin (biotin/lipoic acid binding protein), and Lysozyme (hydrolase to the bacterial cell-wall).

Human breast milk has α-Lactalbumin (Ca-Zn-binder; 156.0 μg/mg of milk protein), Lactoferrin (LF; Fe-binder; 83.0 μg/mg of milk protein), Lysozyme (30.9 μg/mg of milk protein), MARCKS-related protein/Macrophage myristoylated alanine-rich C kinase substrate (25.8 μg/mg of milk protein), Macrophage mannose receptor 1 (Acts as phagocytic receptor for bacteria and fungi; 11.3 μg/mg of milk protein), IgD (7.0 μg/mg of milk protein), Olfactorin/Uromodulin-like 1; 4.5 μg/mg of milk protein),  α-Fetoprotein (Cu-, Ni-binder; 2.9 μg/mg of milk protein),  26S Protease regulatory subunit 6A (Suppresses Tat-mediated transactivation in case of HIV-1 infection; 2.8 μg/mg of milk protein),  Chondroitin sulfate synthase 1 (Co-, Mn-, Cd-binder; 2.5 μg/mg of milk protein), N-Heparan sulfate sulphotransferase 1/Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1 (1.9 μg/mg of milk protein), Bcl-2/adenovirus E1B 19kDa-interacting protein 2-like protein (1.9 μg/mg of milk protein), Sterile alpha motif domain-containing protein 4B (0.7 μg/mg of milk protein), and Influenza virus NS1A-binding protein (mediate the inhibition of splicing by NS/influenza virus NS1A protein; 0.6 μg/mg of milk protein).    Total defence protein becomes to be 44.6% in human breast milk proteins.

Cow's milk has α-Lactalbumin (Ca-Zn-binder; 110.0 μg/mg of milk protein), V-type proton ATPase 116 kDa subunit a isoform 1 (transferrin transport; 126.4  μg/mg of milk protein), Solute carrier family 43 member 3 (124.9 μg/mg of milk protein), Leucine-rich repeat-containing protein 33 (104.3 μg/mg of milk protein), Aldehyde oxidase (Mo-binder; 81.9 μg/mg of milk protein), Lysozyme (11.2 μg/mg of milk protein), Lactoferrin (Fe-binder; 3.0 μg/mg of milk protein), and Guanylate cyclase soluble subunit alpha-1 (defense-related host nitric oxide production; 2.1 μg/mg of milk protein).   Total defence protein becomes to be 57.8% in cow's milk proteins, which is mainly against bacteria.

It is noteworthy that cow's milk has α-S2 Casein (16- of precursor, 1- of mature) at 50.3 μg/mg of milk protein and β-Lactoglobulin (17- of precursor, 1- of mature) at 27.5 μg/mg of milk protein, but human breast milk has no these proteins, which suggests that these two genes are not present in humans.   On the other hand, human breast-milk biotinidase (1-; our unpublished sequence of humans) is present in human breast milk at 5.8 μg/mg of milk protein, but cow's milk has not it.   Antimicrobe activity in human breast-milk biotinidase has not been tested yet (please see file; Compa BINs). 

Human breast milk seems to have a higher power against virus than Cow's milk, and the drinking of mother's breast milk is strongly recommended for the human baby.    

IGF1 is no more a cause of cancer than Insulin.   The Int. Olympic Committee commissioned an extensive study on this, to assure that it is not a performance enhancer.  The study concluded that oral IGF1 does not raise serum levels..

It is not valid to translate in vitro studies with tissue culture and IGF1 to any conclusions about carcinogenesis in humans

Geir:

Here are my thoughts on this excellent question, based on critical appraisal and review of the aggregate data, to date:

*****

THE MILK IGF-1 ASSOCIATION

Of the studies investigating the association between milk, dairy protein, and dairy products and IGF-I, four are RCTs [Ben-Shlomo 2005] [Cadogan 1997] [Heaney 1999] [Zhu 2005], but one RCT found a negative milk/IGF-1 association, but I note that this study exhibits the strong methodological limitation that the association was assessed between exposure in childhood and - far removed in time - outcome in adulthood. In the remaining 3 RCTs all finding for positive association, follow-up was more relevant within the near term, out to no more than 18 - 24 months. Using this RCT base, if we then also synthesize the quality-assessed non-randomized data, we find a moderate level of evidence supporting the contention that milk intake is indeed positively associated with increased levels of both IGF-I and IGFBP-3 [Harrison 2017a].

*****

THE IGF-1 CANCER ASSOCIATION

That's what the best critically appraised, systematically reviewed and meta-analyzed evidence concludes about the positive milk/IGF-1 association. The next question that was posed - implicit in Geir's challenge - is whether in turn such triggered elevation in IGF-1 levels is in turn associated with risk of cancer development. This is of course, given the radically different pathodynamics of cancer, is  malignancy-specific. We have the strongest data as to the IGF-1/Prostate Cancer association: the latest meta-analytic data, adjusted by albatross plots which circumvents the problem of highly diverse reporting of individual studies which often lacked sufficient information for calculation of comparable effect sizes and standard errors, and allows an approximate examination of underlying effect sizes and the potential to identify sources of heterogeneity [Harrison 2017b] across 18 prospective and 41 retrospective studies being meta-analyzed [Harrison 2017], finds that there is moderate evidence that increased IGF-1 increases prostate cancer risk  (and decreases with  IGFBP-3), in essential agreement with previous meta-analysis [Rowlands 2009]. 

*****

BEYOND PROSTATE CANCER

But that is for prostate cancer, and associations vary by malignancy type, so critical reviews - with methodological quality assessment metrics - need be undertaken for the different cancer types, but in general the evidence supports that negative impact on carcinogenesis - that is, elevated risk of development - is largely consequential to elevated IGF-1 levels, while positive (cancer risk reduction) effects may be related to the content of milk's bioactive components, especially calcium, lactoferrin, and fermentation products, and likely also anticancer peptides [Sah 2015]. So, for instance, given the exquisite sensitivity of colon and colorectal cancers to calcium intake and calcium levels, meta-analytic  data shows a consistent association between dairy intake and decreased risk of colon/colorectal cancer [Thorning 2016]. As to several other malignancy types, dairy intake appears not to be associated with risk of pancreatic cancer, ovarian cancer, or lung cancer, but for other cancers we require more robust prospective data to draw more decisive conclusions, given the presence of several methodological limitations, conjoined with potential confounders, and I await the maturing of the data to more comprehensively review cross-malignancy milk/IGF dependencies.

*****

THE ONCOVIRUS ISSUE

Kou Hawakawa has introduced the issue of the potential oncoviral impact on oncogenesis (both carcinogenesis and tumorigenesis), a complex but highly important domain of inquiry, given that we now have sufficient evidence of the carcinogenicity in humans for:

-  HIV (human immunodeficiency virus),

-  HPV (human papillomavirus),

-  HBV (hepatitis B virus),

-  HCV (hepatitis C virus),

-  EBV (Epstein-Barr virus),

-  HTLC (human T-cell lymphotrophic virus), and

-  HHV-8 (human herpes virus 8)

[IARC 2012] [Blackadar 2016] [Chang 2014].

But this topic is beyond the borders of the present discussion, and requires a wholly separate topic to do justice to the theme.

*****

REFERENCES

[Ben-Shlomo 2005] Ben-Shlomo Y, Holly J, McCarthy A et al. Prenatal and postnatal milk supplementation and adult insulin-like growth factor I: long-term follow-up of a randomized controlled trial. Cancer Epidemiol Biomark Prev 2005; 14(5):1336–1339.

[Blackadar 2016] Blackadar CB. Historical review of the causes of cancer. World J Clin Oncol 2016 Feb 10; 7(1):54-86.

[Cadogan 1997] Cadogan J, Eastell R, Jones N et al. Milk intake and bone mineral acquisition in adolescent girls: randomised, controlled intervention trial. BMJ 1997; 315(7118):1255–1260.

[Chang 2014] Viruses and Human Cancer: From Basic Science to Clinical Prevention. Editors: Chang, Mei Hwei, Jeang, Kuan-Teh (Eds.). Recent Results in Cancer Research 193. Springer-Verlag Berlin Heidelberg. 2014.

[Harrison 2017a] Harrison S, Lennon R, Holly J, et al. Does milk intake promote prostate cancer initiation or progression via effects on insulin-like growth factors (IGFs)? A systematic review and meta-analysis. Cancer Causes Control. 2017 Jun; 28(6):497-528.

[Harrison 2017b] Harrison S, Jones HE, Martin RM, Lewis SJ, Higgins JPT. The albatross plot: A novel graphical tool for presenting results of diversely reported studies in a systematic review. Res Synth Methods. 2017 Apr 28.

[Heaney 1999] Heaney RP, McCarron DA, Dawson-Hughes B et al. Dietary changes favorably affect bone remodeling in older adults. J Am Diet Assoc 1999; 99(10):1228–1233.

[IARC 2012] IARC (2012) IARC Monographs on the Evaluation of Carcinogenic Risks to Humans: A Review of Human Carcinogens: Biological Agents Vol. 100B. International Agency for Cancer Research: Lyon, France.

[Rowlands 2009] Rowlands MA, Gunnell D, Harris R, et al. Circulating insulin-like growth factor peptides and prostate cancer risk: a systematic review and meta-analysis. Int J Cancer 2009; 124(10):2416–2429.

[Sah 2015] Sah BNP, Vasiljevic T, McKechnie S, Donkor ON. Identification of anticancer peptides from bovine milk proteins and their potential roles in management of cancer: A critical review. Rev. Food Sci. Food Safety. 2015; 14: 123–138.

[Thorning 2016] Thorning TK, Raben A, Tholstrup T, Soedamah-Muthu SS, Givens, Astrup A. Milk and dairy products: good or bad for human health? An assessment of the totality of scientific evidence. Food Nutr Res 2016; 60:32527.

[Zhu 2005] Zhu K, Du XQ, Cowell CT et al. Effects of school milk intervention on cortical bone accretion and indicators relevant to bone metabolism in Chinese girls aged 10–12 years in Beijing. Am J Clin Nutr 2005; 81(5):1168–1175.

*****

Kind regards

Constantine

*****

Constantine Kaniklidis

Director, Medical Research, No Surrender Breast Cancer Foundation (NSBCF)

Oncology Reviewer, Current Oncology [journal]

Society for Integrative Oncology (SIO)

Member, European Association for Cancer Research (EACR) 

Amended on 12 September 2017

Although Japanese mother and Japanese bovine milk seem to have no prion, bovine milk of USA (Lactoferrin from bovine milk, Sigma (L 9507; ≥85% by SDS-PAGE)) has prion (my unpublished observation by using sensitive and reliable proteomics of PDMD method).   Bovine milk of Australia and New Zealand have not yet been researched.   It is noteworthy that detection of prion is only able to be performed by using new proteomics PDMD method since notorious PCR and ELISA methods (IgG1 to prion has surely been sold elsewhere) is not applicable to milk and serum samples.   Notorious PCR method has been surely not applicable to blood of neonates (personal communication from Dr. Makoto Iwaya, Ph.D., who studied genetics at Harvard University (Cambridge, Massachusetts, USA; Prof. Jack L. Strominger)).   Further, one serum from gait disorder with contraction patient's (32y, female) has Putative testis-specific prion protein/Protein M8 (34-94) at 5.0 μg/mg of serum protein.   Although this protein and gait disorder has not been clarified yet, prion from American beef may be evidently present already in Japan.   Psychiatrist Dr. Kenro Muraki (M.D., JR Tokyo General Hospital, Yoyogi, Shibuya-Ku, Tokyo, Japan) has once personally informed me that CJD patient is already present in Japan.      

Human breast milk of a Japanese mother (n=1) may have Protein smp (Escherichia coli O157) at 40.3 μg/mg of milk protein.   Bovine milk of Japan (n=1) has Bifunctional purine biosynthesis protein purH (Escherichia coli  O5) at 3.2 μg/mg of milk protein.

Human breast milk of a Japanese mother (n=1) has Protein Bel-2 (Macaque simian foamy virus; SFV) at 21.9 μg/mg of milk protein, but has no BLV.   My research suggests that only HIV-1 and HCV (both human specific virus) is important, and presence of SFV in breast milk does not increase the risk for human health.

Further, Lactobacillus casei (Shirota) of beverage Yakult (fermented product from Japanese bovine milk) has Lethal factor (Bacillus anthracis) at 9.5 μg/mg of cell protein.   I only can recommend to the maker to eliminate the plasmid or bacteriophage at this time. 

These findings may be more important for human health especially in Japan.

By the way,  I must sadly repeat about the differences in determination value between HPLC-photometric method and notorious ELISA method (please see files in order to compare the results; SEC fucoidan determination and ELISA fucoidan).The determined value of fucoidan (Okinawa-fucan) is c.a. 2,000-fold higher in the HPLC-photometric analysis as compared to notorious ELISA method (our experience together with Dr. Takeaki Nagamine, M.D., Graduate School of Health Sciences, Gunma University, Showa-machi, Maebashi, Gunma, Japan).   Dr. Nagamine has sadly thrown away the fucoidan-assay kit of ELISA when he is retiring from the University (my unpublished observation or experience).(1) Direct photometric assay without purification gives only 50% value as compared to HPLC-photometric assay due to violence to Lambert-Beer's law (please see Fig. 10 of file "SEC fucoidan determination" again).  (2) Further, binding protein is not so specific; i.e., avidin binds biotin (vitamin H), lipoic acid (thioctic acid), and amino acids, and binding is stronger to lipoic acid than biotin (please see file; Thioctic acid determination) .   Then, biotin assay by using avidin is very difficult since serum has 10-fold higher concentration of lipoic acid than biotin; i.e., lipoic acid may interfere the biotin binding reaction of avidin.  (3) Furthermore, specificity of binding protein increases 10-fold by homo-dimerization(please see file; The Fascio Effect).   The specificity of IgG seems to be 100-fold lower than pentamer IgM due to the Fascio effect.Then, 2 (1) x 10 (2) x 100 (3) = 2000-fold difference seems to be occurred between HPLC-photometric method and ELISA method.  

Therefore, ELISA method is neither sensitive nor quantitative at all; i.e., only giving the false values at ng/mL of serum or milk.   Thus, ELISA can not specifically detect prion proteins in the milk. 

Further, I must sadly repeat about the differences in determination value of biotin between HPLC-photometric method and binding assay method; i.e., such a biotin assay as

"Anal Biochem. 1986 Apr;154(1):367-70.

A sensitive enzyme assay for biotin, avidin, and streptavidin

Edward A. Bayer, Haya Ben-Hur, Meir Wilchek

Department of Biophysics, The Weizmann Institute of Science, Rehovot 76100, Israel

Reciprocal enzyme assays are described for the vitamin biotin and for the biotin-binding proteins avidin and streptavidin. The assays are based on the following steps: (a) biotinylated bovine serum albumin is adsorbed onto microtiter plates; (b) streptavidin (or avidin) is bound to the biotincoated plates: (c) biotinylated enzyme (in this case alkaline phosphatase) is then interacted with the free biotin-binding sites on the immobilized protein. For biotin assay, competition between the free vitamin and the biotinylated enzyme is carried out between steps (b) and (c). The method takes advantage of the four biotin-binding sites which characterize both avidin and streptavidin. The method is extremely versatile and accurate over a concentration range exceeding three orders of magnitude. The lower limits of detection are approximately 2 pg/ml (0.2 pg/sample) for biotin and less than 100 ng/ml (10 ng/sample) for either avidin or streptavidin."

gives only a false value with detection limit as 0.2 pg of biotin.   This detection limit is false since linear regression line or linear calibration line is not possible to get in usual binding-protein assay (such as Immuno Sorbent Assay (ISA) or Immunoassay (IA)).

True HPLC-biotin determination method is presented in the file (Netherlands biotin).   HPLC-method gives a true value with detection limit 17 pg of biotin.  

There is NO data supporting CJD prions in the milk of any species.  It is found primarily in the nerve tissues of infected sheep.

Related question:

How effective are modern cancer drugs? https://www.researchgate.net/post/How_effective_are_modern_cancer_drugs

Further, added on 10 October 2017 It may be important that growth factors may be related to cancer, and I have searched the expression of growth-factor related proteins in liver tissues. Fetal normal hepatocyte Hc and pseudo-liver cancer (normal) has no such growth factor related proteins as expected. LC tissue of patient’s No.6 has Growth hormone-releasing hormone receptor/GRFR/GHRH receptor at 3.3 μg/mg of tissue protein, but this protein is a GPCR. LC tissue with leprosy has Kallman syndrome protein/KAL1/Anosmin-1 at 3.9 μg/mg of tissue protein, and this protein uses a fibroblast growth factor receptor signaling pathway through the JAK-STAT signaling pathway or the Receptor tyrosine kinase (RTK) pathway. It may have been difficult to distinguish between LC and HCC tissues, since this liver with leprosy has turned into a running sore. Hepatoma HepG2 has Insulin receptor substrate 2/IRS-2 at 15.0 μg/mg of cell protein and SH2 (Src homology 2) domain-containing protein 4A at 0.9 μg/mg of cell protein (total 15.9 μg/mg of cell protein). On the other hand, healed HepG2 (cultured for 3 days with fucoidan at 0.102 mg/mL) has EGF-like module-containing, mucin-like, hormone receptor-like 2 at 0.85, Fibroblast growth factor 23 at 0.32, and Keratinocyte growth factor/Fibroblast growth factor 7 at 0.24 μg/mg of cell protein, respectively (total 1.41 μg/mg of cell protein). Therefore, fucoidan has reduced the expression of the growth factor related proteins for 11.3-fold during three days. HCC tissue of patient’s No.6 has Prolactin receptor type 2 at 6.4, Fibroblast growth factor receptor 1/BFGF-R at 1.0, Fibroblast growth factor receptor 2 at 1.0 μg/mg of tissue protein, respectively (total 8.4 μg/mg of tissue protein). HCC tissue wit PBC has Growth hormone receptor/GH receptor at 12.4, Insulin-like growth factor-binding protein 5/IBP-5 at 3.0, and Insulin-like growth factor binding-protein 3/IBP-3 at 0.7 μg/mg of tissue protein, respectively (total 16.1 μg/mg of tissue protein). Therefore, the growth factor related proteins with the JAK/STAT pathway increase in the cancer. Thus, therapies using excess amount of insulin, prolactin and growth hormone are very dangerous.

Furthermore, I would like to add more findings on 23 October 2017. Interestingly, growth-factor related proteins are important for the cell growth.

Therefore, I have searched for the growth-factor related protein tyrosine kinase (PYK).

Hepatoma HepG2 (without fucoidan) has Breast cancer anti-estrogen resistance 2/Transcriptional-regulating factor 1 at 4.8 μg/mg of cell protein (total 4.8 μg/mg of cell protein). Hepatoma HepG2 cell has no Tyrosine-protein phosphatases.

However, healed HepG2 (by fucoidan) has no PYK proteins and Tyrosine-protein phosphatases.

LC tissue (named No.6) has Tyrosine protein kinase receptor EPH/Ephrin type-A receptor 1 at 9.4 μg/mg tissue protein. But, this tissue has Prostatic acid phosphatase/5'-Nucleotidase at 0.64, Protein-tyrosine phosphatase 1C/PTP-1C/Tyrosine-protein phosphatase non-receptor type 6 at 0.15, Receptor-type tyrosine-protein phosphatase epsilon/R-PTP-epsilon at 0.15, and Receptor-type tyrosine-protein phosphatase gamma/R-PTP-gamma at 6.9 μg/mg tissue protein, respectively (total Tyrosine-protein phosphatases is 7.8 μg/mg tissue protein). Therefore, Tyrosine protein kinase receptor EPH/Ephrin type-A receptor 1 in this LC tissue is adequately controlled by tyrosine-protein phosphatases. Interestingly, HCC tissue (No.6) has no Tyrosine-protein phosphatases.

On the other hand, HCC tissue (No.6) has Tyrosine-protein kinase BTK at 0.35 μg/mg of tissue protein and Tyrosine-protein kinase ITK/TSK/Tyrosine protein kinase LYK at 10.6 μg/mg of tissue protein, and Tyrosine-protein kinase LYN at 1.3 μg/mg of tissue protein (Total 12.3 μg/mg of tissue protein). This HCC tissue has no Tyrosine-protein phosphatases.

HCC tissue (with PBC) has Receptor tyrosine-protein kinase erbB-2/Erb b-2 receptor protein-tyrosine kinase at 5.7 μg/mg of tissue protein, Proto-oncogene tyrosine-protein kinase Abl/C-Abl/Abelson murine leukemia viral oncogene homolog 1 at 7.2 , Mast/stem cell growth factor receptor Kit/STAT Non-receptor tyrosine kinase at 3.0 μg/mg of tissue protein, respectively (Total 15.9 μg/mg of tissue protein). This HCC tissue has no Tyrosine-protein phosphatases.

LC tissue (with leprosy) has no such PYK proteins. But, this tissue has Protein-tyrosine phosphatase gamma/R-PTP-gamma at 1.2 μg/mg of tissue protein and Tyrosine-protein phosphatase non-receptor type 3/PTP-H1 at 7.4 μg/mg of tissue protein.

Pseudo cancer (normal liver) has Granulocyte-macrophage colony-stimulating factor receptor alpha chain/GM-CSF-R at 3.0 and Tyrosine-protein kinase receptor TIE at 8.2 μg/mg of tissue protein (Total 11.2 μg/mg of tissue protein). However, this tissue has Receptor of activated protein C kinase 1/Guanine nucleotide-binding protein beta subunit-like protein 12.3 at 0.74, Prostatic acid phosphatase, Isoform 2 at 0.49, and Receptor-type tyrosine-protein phosphatase zeta/R-PTP-zeta at 43.9 μg/mg of tissue protein, respectively. Therefore, GM-CSF-R and Tyrosine-protein kinase receptor TIE are adequately repressed by these PYK inhibitors and Tyrosine-protein phsphatase.

Normal fetal hepatocye Hc cells have Tyrosine-protein kinase ITK/TSK at 9.7 μg/mg of cell protein, but this cells also have Protein janus-A homolog/Phosphohistidine phosphatase 1 at 12.1 μg/mg of cell protein. Thus, Tyrosine-protein kinase ITK/TSK in Hc seems to be adequately controlled by this PYK inhibitor. This cell has no Tyrosine-protein phosphatases.

It is interesting that Hc has 1st major protein of Histone H 3.1. at 55.2 μg/mg cell protein, and 2nd major protein of Protein kinase C eta type at 47.5 μg/mg cell protein. Protein kinase C is a protein serine/threonine kinase (PSTK), and normal developing fetal cells may use mainly PSTK as a tool for the normal growth.

Therefore, the growth-factor related protein tyrosine kinase (PYK)seems to be linked to cancer. Normal cells can adequately control the protein tyrosine kinase (PYK) via the protein tyrosine kinase (PYK) inhibitor activity.

Conclusion; Fucoidan seems to strongly reduce the Growth hormone related receptors and Growth-factor related protein tyrosine kinase (PYK).

Further amended on 26 October 2017, and I wish to dedicate this important answer to the 15,894 people died by "The 2011 earthquake off the Pacific coast of Tōhoku" or "Tōhoku-chihō Taiheiyō Oki Jishin".

I must further add about the mechanism of fucoidan to reduce the expression of Insulin (INS), Insulin-like growth factor I (IGF-I), Prolactin (PRL), and Growth hormone (GH) related proteins. Due thanks to Dr. Joel Subach (Rutgers, The State University of New Jersey, New Brunswick, NJ, USA), I have understood the role of infected virus on to the gene expression of host cell.

Interestingly, GPCR-type receptors seem to be up-regulated by Herpes vira in the adult, but fetal Hc cells seems to induce GPCRs by their own development proteins (does not obey the infected virus).

Hepatoma HepG2 (without fucoidan; who has died) has Insulin receptor substrate 2/IRS-2 at 15.0 μg/mg of cell protein. This hepatoma also has HIV-1 proteins at 15.8 μg/mg of cell protein. Thus, HIV-1 have upregulated IRS-2 gene expression.

On the other hand, healed HepG2 by fucoidan (at 0.102 mg/mL for three days) has no IRS-2 and has Hepatocyte growth factor-regulated tyrosine kinase substrate (negative regulator of JAK-STAT cascade) at 1.9 μg/mg of cell protein. Influenza A virus/FluA and Influenza C virus/FluC at 1.4 μg/mg of cell protein may induced the Hepatocyte growth factor-regulated tyrosine kinase substrate. But this healed cells still has HIV-1 protein (Protein Nef at 0.8 μg/mg of cell protein), and has induced Fibroblast growth factor 23 at 0.32 μg/mg of cell protein. Then, effect of dangerous Fibroblast growth factor 23 may be inhibited by Hepatocyte growth factor-regulated tyrosine kinase substrate. Proteins of HIV-1 have been reduced for 20-fold by fucoidan. Therefore, fucoidan effect has mainly been occurred via reduction of HIV-1 virus. Occurrence and effect of dangerous Fibroblast growth factor 23 by remained HIV-1 may be inhibited by the Hepatocyte growth factor-regulated tyrosine kinase substrate, and fucoidan effect has been achieved within 3 days of therapy.

HCC tissue (with PBC; who has died) has Growth hormone receptor/GH receptor at 12.4, Insulin-like growth factor-binding protein 5/IBP-5 at 3.0, and Insulin-like growth factor binding-protein 3/IBP-3 at 0.7 μg/mg of tissue protein, respectively (total 16.1 μg/mg of tissue protein). This HCC tissue has HIV-1 proteins at 12.9 μg/mg of tissue protein and SIV protein (Gag-Pol polyprotein) at 8.6 μg/mg of tissue protein.

HCC tissue (numbered No.6) has Prolactin receptor type 2 at 6.4 μg/mg of tissue protein. This HCC tissue has SIV at 15.8 μg/mg of tissue protein, and he has survived.

LC tissue (numbered No.6) has no Growth hormone related protein. But, dangerous Tyrosine protein kinase receptor EPH/Ephrin type-A receptor 1 is present at 9.4 μg/mg of tissue protein, and this gene seems to be upregulated by SIV protein (Pol polyprotein) at 7.5, Corticotropin-lipotropin/Pro-opiomelanocortin/POMC at 0.94, and Interleukin-1 alpha/IL-1 alpha at 2.1μg/mg of tissue protein, respectively (total 10.5 μg/mg of tissue protein). However, Prostatic acid phosphatase/5'-nucleotidase at 0.64, Protein-tyrosine phosphatase 1C/PTP-1C/Tyrosine-protein phosphatase non-receptor type 6 at 0.15, Receptor-type tyrosine-protein phosphatase epsilon/R-PTP-epsilon at 0.15, and Receptor-type tyrosine-protein phosphatase gamma/R-PTP-gamma at 6.9 μg/mg of tissue protein, respectively (total 7.8 μg/mg of tissue protein), are present in this tissue to inhibit the Ephrin type-A receptor 1. These protein tyrosine phosphatase seems to be induced by Bovine respiratory syncytial virus/BRSV at 5.2 μg/mg of tissue protein and by Influenza A virus/FluA at 1.7 μg/mg of tissue protein (total 6.9 μg/mg of tissue protein). Thus, this tissue has been remained as LC (non-cancer) state.

LC tissue (with leprosy) has no Growth hormone related proteins, and has no HIV-1and SIV.

Liver tissue of Pseudo liver cancer has no Growth hormone related proteins but has Granulocyte-macrophage colony-stimulating factor receptor alpha chain/GM-CSF-R at 3.0 μg/mg of tissue protein. This normal tissue has HIV-1 protein (Gag-Pol polyprotein) at 3.9 μg/mg of tissue protein, but has no SIV.

But, this GM-CSF-R's protein tyrosine kinase (PYK) activity seems to be completely inhibited by Receptor of activated protein C kinase 1/Guanine nucleotide-binding protein beta subunit-like protein 12.3 (with protein tyrosine kinase inhibitor activity) at 0.74 μg/mg of tissue protein, and Receptor-type tyrosine-protein phosphatase/R-PYP zeta/R-PTP-zeta at 43.9 μg/mg of tissue protein. Receptor of activated protein C kinase 1 seems to be induced by Matrix (M) protein (Influenza C virus/FluC) at 0.52 μg/mg of tissue protein. R-PYP zeta seems to be induced by ORF1a (Avian infectious bronchitis virus/IBV/ACoV) at 46.0 μg/mg of tissue protein. Thus, the liver of pseudo liver-cancer has not become to the true cancer due to presence of FluC and IBV.

Normal fetal hepatocyte Hc has no Growth hormone related proteins, and has no HIV-1 and SIV.

This is an important issue that the gene expression of adult human cells are under the control of virus. Therefore, rare infection of Zika virus to fetal baby sometimes induce morphological microcephaly.

General conclusion: As has Dr. Ram B Singh (Halberg Hospital and Research Institute, Moradabad, India) said that "Yes, milk and meat from animals fed industrial food", it is essential not to take dangerous industrial animals. Therefore, natural protein (and milk) derived from such as bird, whale and fish seems to be most safe to humans nowadays.

Amended on 28 October 2017

I wish to dedicate this important answer to Late Hon. Prof. Dr. Kunio Yamauchi, Ph.D. (The University of Tokyo, Yayoi, Bunkyou-ku, Tokyo, Japan), who kindly introduced milk-protein analysis for me.

Further, I would like to inform about the milk proteins for the sake of milk researchers. Milk proteins have been determined by the reliable PDMD method (please see file to application on serum; JMBT Alopecia).

Lactobacillus casei (Shirota) (isolated from beverage Yakult (Yakult Honsha Co. Tokyo, Japan)) has c.a. 12% of cellular proteins of bacteriophages (bacterial virus) (c.a. 120 μg/mg of bacterial cell protein).

Bovine milk has 17% of proteins of invading microbes, 1.6 % of proteins of virus, 15% of proteins of bacteria and yeast.

α-Lactalbumin (20- of precursor) 110.0 μg/mg of milk protein

α s1 Casein (16- of precursor, 1- of mature) 101.1

β- Casein (16- of precursor, 1- of mature) 78.8

κ- Casein (1- of Q was pyroGlu and N-terminal blocked) 74.3

α- S2 Casein (present only in cow's milk) 50.3

β- Lactoglobulin (present only in cow's milk) 27.5

Lysozyme (Bovine sequence; 19- of precursor) 11.2

Lactoferrin (20- of precursor; 1- of mature) 3.0

Bovine serum albumin (25- of precursor; 1- of mature) 2.0

Milk biotinidase 0.0

V-type proton ATPase 116 kDa subunit a isoform 1/Vacuolar proton pump subunit 1 (transferrin transport) 126.4

Solute carrier family 43 member 3 (Highly expressed in macrophages) 124.9

Leucine-rich repeat-containing protein 33 (phagocyte; control of ROS production) 104.3

Aldehyde oxidase 3L1 (ROS homeostasis) 81.9

Fibrillin-1 (fetal development of the cardiovascular system) 15.3

Guanylate cyclase soluble subunit alpha-1 (only known receptor for nitric oxide, NO; powerful vasodilator) 2.1

Human breast milk has 16% of proteins of invading microbes, 11 % of proteins of virus, 4% of proteins of bacteria and yeast.

α-Lactalbumin (1- of mature) 156.0 μg/mg of milk protein

β-Casein　（16- of precursor; 1- of mature） 127.5

β- Lactoglobulin (present only in cow's milk) 0.0

Lactoferrin (20- of precursor; 1- of mature) 83.0

Lysozyme (human sequence; 19- of precursor; 1-) 30.9

α s1 casein (16- of precursor, 1- of mature) 30.0

α - S2 Casein (present only in cow's milk) 0.0

κ-Casein (22- of precursor; 1-of mature) 11.8

Milk biotinidase (1-; our unpublished sequence of humans) 5.8

Milk lipoamidase (our unpublished sequence of humans) (23.0)

Kidney-type urine biotinidase (1-; our unpublished sequence) 4.2

Human serum albumin (25- of precursor; 1- of mature) 4.1

RING finger protein 86/Tripartite motif-containing protein 2 (neuroprotective function) 55.0

Vacuolar protein sorting-associated protein 13B (post Golgi membrane traffic) 55.0

Tetraspanin-14 (neurogenesis) 33.8

MARCKS-related protein/Macrophage myristoylated alanine-rich C kinase substrate 25.8

Zinc finger protein 610 (Transcription regulation) 19.6 Coprogen oxidase (Heme biosynthesis) 15.0

Plexin-D1/ Cell surface receptor for SEMA4A (cell-cell signaling) 13.2 Dardarin/Leucine-rich repeat serine/threonine-protein kinase 2 (Differentiation) 12.8

Macrophage mannose receptor 1 (receptor for bacteria, fungi and other pathogens) 11.3

Laminin subunit alpha-5 (embryonic development) 10.1 RING finger protein 123/E3 ubiquitin-protein ligase RNF123 9.8 Transmembrane protein 49/Vacuole membrane protein 1 (neurogenesis) 8.5

Secreted modular calcium-binding protein 2 (endothelial cell proliferation) 8.3

Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1/Centaurin-gamma-2 (trafficking of proteins) 7.9

Transmembrane and TPR repeat-containing porotein 1

(cell cycle regulation) 7.7

Docking protein 1 (axon guidance, insulin receptor binding) 7.7

Carbonic anhydrase 12 (respiration, calcification) 7.5 Protein FAM46B (tyrosine-specific phosphatase) 7.2

IgD (defence to fungus and yeast) 7.0

Delangin/Nipped-B-like protein (developing limbs) 6.9 Synaptotagmin-1 (Differentiation) 5.8

Glycogen phosphorylase, liver form 5.5

Putative uncharacterized protein C14orf165 5.2

Lactase-like protein (beta-glucosidase activity) 4.9

DNA helicase V /Far upstream element-binding protein 1 4.9

Olfactorin/Uromodulin-like 1 (anti microbes; peptidase inhibitor) 4.5

Glutathione S-transferase theta-2/GSTT2 (detoxification) 4.4 Serine/threonine-protein kinase Nek1 (axonogenesis) 4.2 Ankyrin-3 (up-regulated during muscle cell differentiation) 3.9

Vasoactive intestinal polypeptide receptor 1 (GPCR for VIP) 3.8

N-Glycanase 1 3.5

Calcyphosin-2 (calcium:sodium antiporter) 3.5

Protein KIAA0100/Antigen MLAA-22 (membrane trafficking) 3.2

α-Fetoprotein 2.9

26S Protease regulatory subunit 6A 2.8

Mucin-5AC (mucus hypersecretion in the pulmonary tracts) 2.7 Chondroitin sulfate synthas 1 (modulation of NOTCH signaling) 2.5 Nuclear receptor corepressor 2 2.5

Protein naked cuticle homolog 1 (eye cell differentiation) 2.5

Actin-like protein 7A (acrosome biogenesis ) 2.2

DNA topoisomerase 3-alpha 2.0

Transmembrane and coiled-coil domain-containing protein 1.9

N-Heparan sulfate sulphotransferase 1 (aorta development) 1.9

Bcl-2/adenovirus E1B 19kDa-interacting protein 2-like protein (regulation of growth rate) 1.9

RING finger protein 173/E3 ubiquitin-protein ligase MARCH3 1.7

Formin homolog overexpressed in spleen 1 (F-actin structure) 1.6

Transcription factor IIIA 1.5

Potassium voltage-gated channel subfamily F member 1 (protein homooligomerization) 1.5

Serine palmitoyltransferase 2 (sphingolipid metabolism ) 1.2

Meltrin-alpha (skeletal muscle regeneration) 1.0

Sterile alpha motif domain-containing protein 4B (response to tissue injury) 0.7

Zinc finger protein 610 0.7

Transcription regulator protein BACH2 0.7

Influenza virus NS1A-binding protein (cell division) 0.6

It is interesting that bovine milk has anti-bacterial proteins Lysozyme and Lactoferrin at 14.2 μg/mg of milk protein, but human breast milk has anti-bacterial proteins at 113.9 μg/mg of milk protein (8-fold higher in human milk). This may be related to the rumination in bovine.

Further, it is noteworthy that bovine milk has high level of Yeast (Candida albicans, Schizosaccharomyces pombe, and Saccharomyces cerevisiae) at 2.9% of milk protein.

On the other hand, human breast milk has low level of Yeast (Schizosaccharomyces pombe and Saccharomyces cerevisiae) at 0.6% of milk protein. Therefore, IgD in human milk may be specifically protest against Yeast.

Related question:

Is sugar a carcinogen?

https://www.researchgate.net/post/Is_sugar_a_carcinogen?

Amemded on 7 November 2017

Surely, oligosaccharides seem to be growth accelerators. Oligo-Okinawa-fucan (Okinawa-SMW-fucan; Okinawa-Small-Molecular-Weight-fucan) has a growth accelerator activity at 0.1 mg/mL, but large-molecular-weight native Okinawa-fucan shows no such growth accelerator activity (please see page 26 of the file; Rat DEN Np-Fuco). However, L-Fucose (mono-saccharide; 0.1 mg/mL) has no growth accelerator activity. This growth accelerator activity has been demonstrated on both normal and cancer cells.

Nigero-oligosaccharide (small polymer of D-glucose) also shows growth accelerator activity (our unpublished observation).

This growth accelerator activity in oligo-saccharides is not linked to cancer at all. Then, oligo-saccharide seems to be an important nutrition both to healthy persons and cancer patients to be fed by measure (please see file; Feed by Measure).

I am now considering that oligo-sugars is the direct material for the biosynthesis of various polysaccharides.

By the way, biotin (20 μM) and lipoic acid (240 μM) have the growth accelerator activity onto human cells, but lipoic acid is toxic to rat cells (our unpublished observation). Effect of biotin has been described in the file "JCB Fucoidan transport".

Effect of optimum concentration of Hg and other metals onto the growth accelerator activity has not yet been tested.

Furthermore, it is noteworthy that Nicotine, Caffeine, and Acetaldehyde have unexpectedly shown no growth accelerator and/or retardation activity, but only Fucoidan (derived from Japanese edible Mozuku; natural high-molecular-weight (HMW) Fucoidan) has shown a remarkable growth retardation activity on the adult cancer cells (HepG2 and HuH-7). However, Fucoidan has shown no growth accelerator and/or retardation activity onto fetal normal Hc cells and hepatoblastoma HuH-6 (my unpublished observation).

yes definatelly

Cow’s milk allergy is an immunologically mediated response to one or more of cow’s milk proteins. Lactose intolerance, a no immunological reaction, is the occurrence of symptoms after persons with low levels of the enzyme lactase (lactose maldigesters) consume lactose (milk sugar) in amounts exceeding lactase’s ability to digest it. Cow’s milk protein allergy occurs primarily in infancy and early childhood. Moreover, the condition tends to be outgrown by 5 years of age. In contrast to cow’s milk allergy, which occurs primarily in infancy and young childhood, lactose intolerance (symptoms) seldom occurs prior to preadolescence. Although lactase activity begins to decline after weaning in genetically predisposed individuals, whether or not the condition becomes symptomatic depends on a variety of biological, psychological, and dietary factors.

Lactose is a sugar found in milk. It cannot become absorbed by the body unless is gets changed into more simple sugars called glucose and galactose. This change happens when the lactose passes through the stomach into the upper part of the gut (small intestine) and comes into contact with a chemical called lactase. Lactase is made by cells that line the upper part of the small intestine. If there is not enough lactase in the small intestine, lactose cannot be broken down and cannot get absorbed. This leads to lactose intolerance. Some people confuse lactose intolerance with allergy to cow's milk. With milk allergy, your immune system reacts to proteins found in milk which can cause symptoms. Lactose intolerance is not an allergy. Symptoms are caused by the undigested lactose in the gut

IgF1 does not promote cancer in vivo!!!

I agree with @ Kou Hayakawa. I hope this link will help you

Article Acne, dairy and cancer: The 5alpha-P link

Kind regards

Various meta-analytical studies are available supporting association between IGF-1 (from food) and cancer, on the other hand many contradicting studies are also available. I would raise a question over most of the meta-analysis study supporting association between IGF-1 and cancer as they did not consider the Natural variation in Individual human's capability to produce IGF-1, As individual with abnormally higher capabilities to product IGF-1 are at higher risk of getting cancer even though they do not consume any dairy product. In summary no study has provided conclusive solid evidence so far to prove association between IGF-1 (from food) and cancer.