Does anyone have a suggestion for a proper housekeeping protein that IS NOT cleaved in necrotic tissue AND its levels are more or less constant during wound healing/tissue regeneration process?
I noticed that GAPDH and alpha-Tubulin are rapidly degraded in the samples where the caspase activity is high. Beta-Actin is more stable, but it is also a target of caspases, and it is upregulated during wound healing stages. I would appreciate any feedback from those who work with animal tissues.
Could thioredoxin pathways shed any light? also acts as a signalling pathway for ROS levels
Dear Jason, thank you for the suggestion. Although thioredoxin is expressed in a variety of tissues, its levels may be modulated by various stressors, such as viral infection, mitogens, PMA, UV and X-ray radiation, hydrogen peroxide dose and, most importantly, ischemic reperfusion, which I am afraid, is one of the major factors in my experimental model of wound healing. However, a paper by Ueda et al. suggests that thioredoxin is pretty stable upon Caspase-3 activation. I'll give it a try. Thanks!
http://www.jimmunol.org/content/161/12/6689.full
I found an interesting article about the housekeeping genes. It states that the constitutive expressions of ribosomal proteins L37 and L38 are observed in all different animal tissues. In particular, L37 is constitutively expressed during transitions from quiescence to active cell proliferation or terminal differentiation in all tissues in rat and human! Also the authors suggest that PPIase is a better internal control than beta-actin and GAPDH.
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