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

@article{Schnitzer1992AntibodiesTS,
  title={Antibodies to SPARC inhibit albumin binding to SPARC, gp60, and microvascular endothelium.},
  author={Jan E. Schnitzer and Philmo Y Oh},
  journal={The American journal of physiology},
  year={1992},
  volume={263 6 Pt 2},
  pages={H1872-9}
}
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… CONTINUE READING