Collagens were analyzed in skin and rib cartilage of 9 patients with
Ehlers-Danlos syndrome of the II type. Electrophoresis and CNBr-
peptide mapping showed that extended inserts and deletions as well as rough impairments of post-translation processing were not detected in
collagens of the I, II and III types from these patients. In the patients with
Ehlers-Danlos syndrome of the II type distinct increase was observed both in the total ratio of
collagens III/I (P = 0.95) and in the ratio of intact
collagens III/I free of cross-links. A decrease in content of dimers beta 11 and beta 12 was found in two patients. The data obtained suggest that the
Ehlers-Danlos syndrome of the II type involved deteriorations in the structure of
collagens I responsible for decrease in stability and sometimes for impairments in cross-link formation. Increase in content of
collagen II fraction, predisposed to proteolytic hydrolysis of terminal sites, as well as elevated sensitivity of
collagen II to
pepsin hydrolysis were found in
collagens of rib cartilage from patients with the syndrome and with
funnel chest deformation. This suggests the lowered stability of
collagen II from rib cartilage in
funnel chest deformation.