Studies on the underhydroxylated basement membrane procollagen synthesized by rat parietal yolk sacs in the presence of alpha,alpha'-dipydridyl.
Rat embryo parietal yolk sacs synthesized and secreted underhydroxylated [14C]proline-labeled basement membrane procollagen when incubated in the presence of the iron chelator alpha,alpha'-dipyridyl and [14C]proline. Upon reduction and sodium dodecyl sulfate-agarose gel filtration, this procollagen eluted as a discrete peak of labeled material close to the position of the beta components of type I collagen. Secreted underhydroxylated procollagen contained interchain disulfide bonds and was completely degraded by a 6 hr treatment with alpha-chymotrypsin at 4 degrees C. Results from 4 hr incubations indicated that the distribution of 14C-procollagen between tissue and medium was unaffected by the presence of alpha,alpha'-dipyridyl, but analysis of results from pulse-label and chase experiments revealed that underhydroxylated procollagen was secreted at less than half the rate of control procollagen.
D015082:2,2'-Dipyridyl / Q000494:pharmacology*; D000818:Animals; D001485:Basement Membrane / Q000378:metabolism; D002850:Chromatography, Gel; D002918:Chymotrypsin; D046508:Culture Techniques; D004220:Disulfides / Q000378:metabolism; D006900:Hydroxylation; D011347:Procollagen / Q000096:biosynthesis* / Q000378:metabolism; D011392:Proline / Q000378:metabolism; D011725:Pyridines / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains; D015017:Yolk Sac / Q000187:drug effects / Q000378:metabolism*
D004220:Disulfides; D011347:Procollagen; D011725:Pyridines; D015082:2,2'-Dipyridyl; D011392:Proline; D002918:Chymotrypsin