COLLAGEN AND GLYCOSAMINOGLYCANS OF WHARTONS JELLY

In this study, we report quantity, solubility and molecular polymorphi sm of collagen, proportional relationships between various types of co llagen, ultrastructure of collagen fibres, the amounts of various glyc osaminoglycans (GAGs) and proportional relationships between them in W harton's jelly of normal umbilical cords. We compare the extracellular matrix components in Wharton's jelly with those in the umbilical cord artery. Collagen of the Wharton's jelly demonstrates some specific fe atures. It is very insoluble in neutral salt and in a slightly acidic solution and appears to be resistant to the action of depolymerizing a gent (EDTA-Na-2). Only 50% of total collagen may be solubilized by pep sin digestion and fractionated by differential salt precipitation. Fou r collagen fractions were obtained. Three of them were identified by p olyacrylamide gel electrophoresis as type I, type III, and type V coll agen and proportional relationship between them was calculated. Hyalur onic acid is the most abundant component of GAGs contained in Wharton' s jelly. The amounts of sulphated GAGs - keratan sulphate, heparan sul phate, chondroitin-4-sulphate, chondroitin-6-sulphate, dermatan sulpha te and heparin - are distinctly lower. Each of them constitutes only a few percent of total GAGs.