Synopsis
Although normally, dermal collagen fails to retain the Ponceau 2R/Acid Fuchsin component of the Masson trichrome procedure and is stained green by the counterstain, the collagen of sections of human dermis which have been heated above its denaturation temperature (T s) in moist conditions will retain the initial red stain. This difference in dye retention appears to be related to conformational changes of the collagen molecule which are associated with denaturation, for the change in staining is directly related to the shrinkage temperature, is reversed by rapid cooling after heating, is profoundly affected by differences in environmental conditions during heating which affect molecular rearrangement, and is age-dependent.
Analogous changes in staining propensity have been observed in heated keratin and epidermis. However, whereas the retention of the initial red dye mixture is increased in denatured dermis, it is diminished in heated epidermis. It is suggested that the subtle dye substrate interaction of the Masson trichrome staining procedure can be utilized to demonstrate changes in molecular configuration which are associated with thermal, as well as other forms of denaturation of collagen and other proteins.
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Flint, M.H., Lyons, M.F. The effect of heating and denaturation on the staining of collagen by the Masson trichrome procedure. Histochem J 7, 547–555 (1975). https://doi.org/10.1007/BF01003792
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DOI: https://doi.org/10.1007/BF01003792