Preferential interaction of albumin-binding proteins, gp30 and gp18, with conformationally modified albumins. Presence in many cells and tissues with a possible role in catabolism.

@article{Schnitzer1992PreferentialIO,
  title={Preferential interaction of albumin-binding proteins, gp30 and gp18, with conformationally modified albumins. Presence in many cells and tissues with a possible role in catabolism.},
  author={Jan E. Schnitzer and Arthur Sung and Reinhard Horvat and Julisa Bravo},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 34},
  pages={24544-53}
}
Albumin binding to the endothelial surface apparently initiates its transcytosis via plasmalemmal vesicles and also increases capillary permselectivity. Several albumin-binding proteins, which, we call gp60, gp30, and gp18, have been identified; however, their functional relationship to each other is unclear. In this study, we show that gp30 and gp18 are both variably expressed by cultured rat fibroblasts, smooth muscle cells, and endothelial cells and are present in all tissues examined (heart… CONTINUE READING

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