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Am J Physiol Heart Circ Physiol 277: H1985-H1996, 1999;
0363-6135/99 $5.00
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Vol. 277, Issue 5, H1985-H1996, November 1999

Cablin: a novel protein of the capillary basal lamina

Audra J. Charron1, Weimin Xu2, Robert L. Bacallao2, and Angela Wandinger-Ness3

1 Integrated Graduate Program in the Life Sciences, Northwestern University Medical School, Chicago, Illinois 60611; 2 Department of Medicine, Indiana University Medical Center, Indianapolis, Indiana 46202; and 3 Department of Pathology, University of New Mexico Health Sciences Center, Albuquerque, New Mexico 87131

The microvascular wall is remarkably simple, consisting only of the endothelial lining, subjacent basal lamina, and underlying periendothelial cells. This study describes the characterization of a novel microvascular protein. This 80,000-molecular weight protein was predominantly associated with electron-lucent amorphous material in capillary basal laminae and therefore termed cablin (protein of the capillary basal lamina). Consistent with its immunolocalization to the microvasculature, cablin was synthesized and secreted by cultured endothelial cells and vascular smooth muscle cells. Furthermore, cablin expression was induced during neovascularization. The predicted amino acid sequence of cablin revealed a prevalence of polar amino acids. Accounting for the low yet significant homology to several alpha -helical proteins, these residues were best accommodated by secondary structure predictions that aligned the molecule into two large alpha -helical domains. The presence of the integrin-binding RGD tripeptide and a putative elastin-binding sequence suggest that this rodlike molecule is suited to cross-link cells and matrix constituents. In this capacity it could contribute to the mechanical strength or the angiogenic potential of the microvasculature.

vascular smooth muscle; endothelial cell; microvascular; extracellular matrix


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