Presence of plasma proteins facilitates the uptake of /sup 125/I-thrombin by the rabbit thoracic aorta endothelium in vitro
Various purified proteins, protein derivatives and two polysaccharides were added individually to a physiological medium in order to effect uptake of /sup 125/I-thrombin by the rabbit aorta endothelium. Over a wide range of concentration (0.004-40 mg/ml), the presence of either purified rabbit or bovine albumin during thrombin uptake encouraged an increase (70-110%) in /sup 125/I-thrombin binding by the endothelium and subendothelium compared to uptake by aorta segments in the absence of added protein. Pretreatment of aorta segments with albumin before incubation with /sup 125/I-thrombin in the absence of albumin did not encourage thrombin uptake to the same extent as having /sup 125/I-thrombin and albumin together. Purified human transferrin, rabbit IgG, chicken ovalbumin or denatured bovine casein could replace albumin to produce a similar enhancement of thrombin uptake. Replacing active concentrations of albumin by either reduced-carboxymethylated albumin, defatted albumin, plasmin-treated or thermolysin-treated albumin also caused an increase (50-130%) in thrombin binding, whereas replacement by acid-hydrolysed albumin or with polyglutamic acid was either ineffective or even inhibitory. Lysine-modified or arginine-modified albumins caused a small enhancement (14-32%) and no enhancement of thrombin uptake, respectively. Dextran, at low concentration (0.04-0.4 mg/ml) did not influence thrombin uptake, and at higher concentration (4-40 mg/ml) caused a decrease in uptake by both the endothelium and subendothelial layers. Low concentration of dextran sulphate inhibited thrombin uptake to 20-30% of control values. These data express the importance of accompanying protein in the response of the vascular endothelium during binding of thrombin. The possibility that other protein-cell interactions may be similarly influenced by macromolecular solutes is also discussed.
- OSTI ID:
- 5013215
- Journal Information:
- Thromb. Res.; (United States), Journal Name: Thromb. Res.; (United States) Vol. 1; ISSN THBRA
- Country of Publication:
- United States
- Language:
- English
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59 BASIC BIOLOGICAL SCIENCES
ALBUMINS
ANIMAL TISSUES
ANIMALS
AORTA
ARTERIES
BETA DECAY RADIOISOTOPES
BIRDS
BLOOD VESSELS
BODY
CARBOHYDRATES
CARDIOVASCULAR SYSTEM
CHICKENS
COAGULANTS
DAYS LIVING RADIOISOTOPES
DRUGS
ELECTRON CAPTURE RADIOISOTOPES
ENDOTHELIUM
ENZYMES
FOWL
GLOBULINS
GLOBULINS-BETA
GLUCOPROTEINS
HEMATOLOGIC AGENTS
HEMOSTATICS
HYDROLASES
IN VITRO
INTERMEDIATE MASS NUCLEI
IODINE 125
IODINE ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
LABELLED COMPOUNDS
MAMMALS
METALLOPROTEINS
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
ORGANS
OVALBUMIN
PEPTIDE HYDROLASES
PROTEINS
RABBITS
RADIOISOTOPES
SACCHARIDES
SERINE PROTEINASES
THROMBIN
TISSUES
TRACER TECHNIQUES
TRANSFERRIN
UPTAKE
VERTEBRATES