Distribution of CL Glycoprotein in Tissues: An Immunohistochemical Study

Abstract

CL glycoprotein is a collagen-like glycoprotein which we have recently isolated from rapidly growing fetal bovine, elastin-rich tissues. This protein has a molecular weight of approximately 140,000 daltons, contains hydroxyproline and hydroxylysine and is digested by highly purified collagenase to yield three large polypeptides. A specific antibody has been developed against this protein and has been used for immunofluorescence microscopy to study the distribution of CL glycoprotein in a range of tissues. It has been shown that the antibody localized in the intercellular matrix of nuchal ligament and aorta, of the non-elastic Achilles tendon and in complex tissues such as kidney, lung, skin and spleen. The antibody also localized to the surface of aortic smooth muscle cells-presumably to the basement membrane, but did not bind to other basement membranes, including the vascular subendothelial basement membrane. The pattern of distribution was similar in adult bovine tissues. As this antibody showed no avidity for elastic tissue elements, it is most unlikely that CL glycoprotein is a constituent of elastin-associated microfibrils. When the pattern of the CL glycoprotein distribution within the tissues was studied, it was found that, apart from its concentration around vascular smooth muscle cells, CL glycoprotein exhibited considerable overlap in distribution with the interstitial collagens. On the basis of these observations and having regard to its biochemical characteristics, it is proposed that CL glycoprotein has a structural role inter-linking interstitial components to one another and to vascular smooth muscle cells.