Antibodies to SPARC inhibit albumin binding to SPARC, gp60, and microvascular endothelium

跨细胞 白蛋白 牛血清白蛋白 化学 生物化学 内皮 血清白蛋白 抗体 血浆蛋白结合 分子生物学 生物 免疫学 内吞作用 受体 内分泌学
作者
Jan E. Schnitzer,Philmo Oh
出处
期刊:American Journal of Physiology-heart and Circulatory Physiology [American Physiological Society]
卷期号:263 (6): H1872-H1879 被引量:99
标识
DOI:10.1152/ajpheart.1992.263.6.h1872
摘要

Albumin, through its binding to the endothelial glycocalyx, functions as a major determinant of capillary permeability and as a carrier for various small molecules in its transcytosis across continuous endothelium via plasma-lemmal vesicles. Several albumin-binding proteins (ABP) have been identified: three membrane-associated ABP, which we call gp60, gp30, and gp18, and one secreted protein, acidic and rich in cysteine (SPARC). In this study, we used antiserum raised against bovine SPARC (BON) to investigate the possible interrelationships among ABP to better understand their role in binding and transcytosis. BON not only interacted with SPARC secreted by cultured endothelium but also recognized gp60 in lysates of cultured rat, human, and bovine endothelial cells. Purified SPARC inhibited BON interaction with gp60. BON immunoglobulin (Ig)G specifically inhibited albumin binding to both SPARC and gp60 extracts. This effect was eliminated by preabsorption of BON to immobilized SPARC. BON also significantly inhibited albumin binding to cultured microvascular endothelial cells via its interaction with gp60. Anti-SPARC peptide sera were also tested, and one serum raised against a peptide encompassing an NH2-terminal region of SPARC recognized both SPARC and gp60 but did not inhibit albumin binding; gp30 and gp18 were not recognized by any of these anti-SPARC antibodies. These results suggest that SPARC and gp60 are functionally and immunologically related ABP that may share a common albumin-binding domain. gp60 appears to be the major mediator of albumin binding to microvascular endothelium.
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