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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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The amounts and activities of matrix metalloproteinases (MMPs) were studied in human myometrium and uterine leiomyomas in various stages of growth. It was found that both myometrium and the investigated tumors contain collagenolytic enzymes. MMP-1, MMP-2, MMP-3 and MMP-9 were found. Gelatinase A (MMP-2) is the most abundant. In control myometrium only 10% of this enzyme exists in an active form, whereas in tumors, especially in large ones, the values reach 30%. It is suggested that the high activity of MMP-2 is responsible for remodelling of extracellular matrix in the growing tumors.

The high activity of MMP-9 in preeclamptic plasma suggests its participation in the proteolytic release of peptide growth factors from their complexes with other matrix components, with subsequent stimulation of cell division and matrix biosynthesis. We suggest this might represent one of the mechanisms for matrix remodeling in the umbilical cord of preeclamptic newborns.