Biochemical characterization of collagens synthesized by intestinal epithelial cell cultures.

摘要: Abstract Rat intestinal epithelial cells in culture synthesize and secrete several different collagens as identified by biochemical ultrastructural criteria. These were labeled with [U-14C]proline, separated DEAE- CM-cellulose chromatography, at least four collagen chains identified. Two of them, present almost exclusively fully processed collagens, alpha 1(I) 2 chains. The presence a large excess 1 (I) over the normal ratio for type I indicated that both [alpha 1(I)]2 1(I)]3 or trimer medium extracellular matrix. chain had CNBr peptide pattern superimposable on standard from rat skin, but intact radiolabeled differed its migration sodium dodecyl sulfate gels elution position column much higher hydroxylysine content. other two partially procollagens. They constituted 60 to 70% collagenous proteins features corresponding none known types. chromatography further characterized. Both contained interchain disulfide bonds pepsin-resistant portion molecule and, after pepsin digestion, eluted lower salt concentrations than chain. One them was characterized low hydroxyproline content high content, all glycosylgalactosyl derivative. patterns these unknown each other, did not correspond those any examined. may represent new types specifically basement membrane.