Nd. Rosenblum et al., ALPHA-1-VIII COLLAGEN IS EXPRESSED IN THE RAT GLOMERULUS AND IN RESIDENT GLOMERULAR CELLS, The American journal of physiology, 264(6), 1993, pp. 1003-1010
Current knowledge regarding the molecular composition of extracellular
matrices in the glomerulus does not explain how these components inte
ract to form stable three-dimensional structures. The recent recogniti
on that short-chain collagens such as type VIII collagen function as m
olecular bridges in some nonrenal tissues has raised the possibility t
hat such molecules may serve a similar function in the glomerulus. We
have recently shown that cultured rat mesangial cells synthesize and s
ecrete several short-chain collagenous proteins, one of which has prop
erties similar to alpha1-VIII collagen. In the present study we have i
solated a rat mesangial cell alpha1-VIII collagen cDNA clone, the sequ
ence of which is 81% homologous to mouse alpha1-VIII collagen. We used
this cDNA to determine that alpha1-VIII collagen mRNA is expressed in
rat renal cortex and in cultured glomerular mesangial, epithelial, an
d endothelial cells. Additionally, we demonstrated that alpha1-VIII co
llagen is secreted by cultured mesangial cells as an 80-kDa translatio
n product. By immunocytochemistry, alpha1-VIII collagen localized to t
he media of large intrarenal arteries and to the capillary loops and t
he mesangium of normal rat kidney. These results indicate that type VI
II collagen is a normal constituent of the rat glomerulus as well as l
arge intrarenal arteries. We speculate that type VIII collagen may fun
ction in part to determine the three-dimensional organization of the s
ubendothelial and mesangial matrices.