Specific albumin binding to microvascular endothelium in culture
Abstract
The specific binding of rat serum albumin (RSA) to confluent microvascular endothelial cells in culture derived from the vasculature of the rat epididymal fat pad was studied at 4{degree}C by radioassay and immunocytochemistry. Radioiodinated RSA ({sup 125}I-RSA) binding to the cells reached equilibrium at {approximately} 20 min incubation. Albumin binding was a slowly saturating function over concentrations ranging from 0.01 to 50 mg/ml. Specific RSA binding with a moderate apparent affinity constant of 1.0 mg/ml and with a maximum binding concentration of 90 ng/cm{sup 2} was immunolocalized with anti-RSA antibody to the outer (free) side of the enothelium. Scatchard analysis of the binding yielded a nonlinear binding curve with a concave-upward shape. Dissociation rate analysis supports negative cooperativity of albumin binding, but multiple binding sites may also be present. Albumin binding fulfilled many requirements for ligand specificity including saturability, reversibility, competibility, and dependence on both cell type and cell number. The results are discussed in terms of past in situ investigations on the localization of albumin binding to vascular endothelium and its effect on transendothelial molecular transport.
- Authors:
-
- Yale Univ. School of Medicine, New Haven, CT (USA)
- Publication Date:
- OSTI Identifier:
- 7101032
- Resource Type:
- Journal Article
- Journal Name:
- American Journal of Physiology; (USA)
- Additional Journal Information:
- Journal Volume: 254:3; Journal ID: ISSN 0002-9513
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; ALBUMINS; RADIOASSAY; ENDOTHELIUM; CYTOCHEMISTRY; ANGIOTENSIN; BLOOD SERUM; CAPILLARIES; CELL CULTURES; CROSS-LINKING; FIBROBLASTS; IODINATION; IODINE 125; RATS; SODIUM IODIDES; ALKALI METAL COMPOUNDS; ANIMAL CELLS; ANIMAL TISSUES; ANIMALS; BETA DECAY RADIOISOTOPES; BIOCHEMISTRY; BLOOD VESSELS; BODY; CARDIOVASCULAR AGENTS; CARDIOVASCULAR SYSTEM; CHEMICAL REACTIONS; CHEMISTRY; CONNECTIVE TISSUE CELLS; DAYS LIVING RADIOISOTOPES; DRUGS; ELECTRON CAPTURE RADIOISOTOPES; GLOBULINS; HALIDES; HALOGEN COMPOUNDS; HALOGENATION; INORGANIC PHOSPHORS; INTERMEDIATE MASS NUCLEI; IODIDES; IODINE COMPOUNDS; IODINE ISOTOPES; ISOTOPES; MAMMALS; NUCLEI; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; ORGANS; PHOSPHORS; POLYMERIZATION; PROTEINS; RADIOISOTOPES; RODENTS; SODIUM COMPOUNDS; SOMATIC CELLS; TISSUES; VASOCONSTRICTORS; VERTEBRATES; 550201* - Biochemistry- Tracer Techniques
Citation Formats
Schnitzer, J E, Carley, W W, and Palade, G E. Specific albumin binding to microvascular endothelium in culture. United States: N. p., 1988.
Web.
Schnitzer, J E, Carley, W W, & Palade, G E. Specific albumin binding to microvascular endothelium in culture. United States.
Schnitzer, J E, Carley, W W, and Palade, G E. 1988.
"Specific albumin binding to microvascular endothelium in culture". United States.
@article{osti_7101032,
title = {Specific albumin binding to microvascular endothelium in culture},
author = {Schnitzer, J E and Carley, W W and Palade, G E},
abstractNote = {The specific binding of rat serum albumin (RSA) to confluent microvascular endothelial cells in culture derived from the vasculature of the rat epididymal fat pad was studied at 4{degree}C by radioassay and immunocytochemistry. Radioiodinated RSA ({sup 125}I-RSA) binding to the cells reached equilibrium at {approximately} 20 min incubation. Albumin binding was a slowly saturating function over concentrations ranging from 0.01 to 50 mg/ml. Specific RSA binding with a moderate apparent affinity constant of 1.0 mg/ml and with a maximum binding concentration of 90 ng/cm{sup 2} was immunolocalized with anti-RSA antibody to the outer (free) side of the enothelium. Scatchard analysis of the binding yielded a nonlinear binding curve with a concave-upward shape. Dissociation rate analysis supports negative cooperativity of albumin binding, but multiple binding sites may also be present. Albumin binding fulfilled many requirements for ligand specificity including saturability, reversibility, competibility, and dependence on both cell type and cell number. The results are discussed in terms of past in situ investigations on the localization of albumin binding to vascular endothelium and its effect on transendothelial molecular transport.},
doi = {},
url = {https://www.osti.gov/biblio/7101032},
journal = {American Journal of Physiology; (USA)},
issn = {0002-9513},
number = ,
volume = 254:3,
place = {United States},
year = {Tue Mar 01 00:00:00 EST 1988},
month = {Tue Mar 01 00:00:00 EST 1988}
}