The role of intracellular lysosomal enzymes in the autocellular-surveillance of unhydroxylated collagens in dermal and gingival fibroblasts.
The turnover of unhydroxylated collagen was investigated in dermal and gingival fibroblasts derived from C57Bl/6J mice. Unhydroxylated collagen molecules were fostered by the inhibition of prolyl- and lysyl-hydroxylase by the addition of alpha, alpha' dipyridyl. Turnover of collagens was determined by single isotope continuous labeling, double-isotopic labeling, the use of lysosomal pH modulators, and proteinase inhibitors. These studies reveal that the turnover of unhydroxylated collagen is an extracellular event, in spite of the susceptibility of these abnormal structural and conformational proteins to proteolysis; the synthesizing cell does not utilize intracellular lysosomal enzymes as a means of modulating the quantities of non-helical unhydroxylated collagen as an intolerable post-translational error of protein processing.
D000818:Animals; D002478:Cells, Cultured; D003094:Collagen / Q000378:metabolism*; D010450:Endopeptidases / Q000378:metabolism; D005347:Fibroblasts / Q000201:enzymology*; D005881:Gingiva / Q000166:cytology*; D008247:Lysosomes / Q000201:enzymology*; D051379:Mice; D008810:Mice, Inbred C57BL; D008815:Mice, Inbred Strains; D003012:Microbial Collagenase / Q000378:metabolism; D012867:Skin / Q000166:cytology*
D003094:Collagen; D010450:Endopeptidases; D003012:Microbial Collagenase