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In this study, we report quantity, solubility and molecular polymorphism of collagen, proportional relationships between various types of collagen, ultrastructure of collagen fibres, the amounts of various glycosaminoglycans (GAGs) and proportional relationships between them in Wharton’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 features. It is very insoluble in neutral salt and in a slightly acidic solution and appears to be resistant to the action of depolymerizing agent (EDTA-Na₂). Only 50% of total collagen may be solubilized by pepsin digestion and fractionated by differential salt precipitation. Four collagen fractions were obtained. Three of them were identified by polyacrylamide gel electrophoresis as type I, type III, and type V collagen and proportional relationship between them was calculated. Hyaluronic acid is the most abundant component of GAGs contained in Wharton’s jelly. The amounts of sulphated GAGs – keratan sulphate, heparan sulphate, chondroitin-4-sulphate, chondroitin-6-sulphate, dermatan sulphate and heparin – are distinctly lower. Each of them constitutes only a few percent of total GAGs.

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We decided to investigate the EPH-gestosis--connected alterations in collagen of the umbilical cord arteries. The samples of arterial walls were submitted to histological and biochemical studies. It was found that umbilical cord arteries taken from newborns of mothers with EPH-gestosis contain more than twice the amount of collagen in comparison to corresponding arteries of newborns from normal pregnancies. An increase of collagen content in these vessels in accompanied by a slight decrease of its solubility. Types I, III, IV, V and VI collagens were found both in normal umbilical cord arteries and in those of newborns delivered by mothers with EPH-gestosis but their proportional relationships were different. EPH-gestosis is accompanied by an increase of a proportional amount of type III-collagen and a decrease of type I collagen in umbilical cord arteries. It seems that these changes in the umbilical cord arteries may be responsible for the decrease of blood flow in fetus of woman with EPH-gestosis.

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SummaryIt has been found that Hageman factor is adsorbed from normal human plasma by collagen and elastin. The adsorption is dependent upon the concentration of both substances and upon the adsorption time. The adsorption by collagen is almost selective. By the procedure of the repeated adsorption it is possible to obtain plasma containing 3-5% of Hageman factor normal value and normal amount of PTA (factor XI). At pH 9.5-10.0 the Hageman factor can be eluted in part from collagen shaken previously with human or pig plasma, its recovery in the eluates from elastin is poor.Experimental evidence is presented that the Hageman factor is activated following adsorption on collagen. The eluates from collagen have been compared with those prepared in a similar manner from kaolin and celite. All eluates possess clot promoting, TAMe arginine esterase and fibrinolytic activities. They shorten considerably the clotting time of the whole blood in siliconized tubes.It has been suggested that collagen may act as an intrinsic trigger of the blood coagulation in vivo by adsorbing and activating the Hageman factor.