Presence of plasma proteins facilitates the uptake of /sup 125/I-thrombin by the rabbit thoracic aorta endothelium in vitro

Journal Article · Tue Jul 01 00:00:00 EDT 1986 · Thromb. Res.; (United States)

DOI:https://doi.org/10.1016/0049-3848(86)90045-9· OSTI ID:5013215

Hatton, M W; Moar, S L

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), Vol. 1
• Country of Publication: United States
• Language: English

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59 BASIC BIOLOGICAL SCIENCES
THROMBIN
UPTAKE
ALBUMINS
AORTA
CHICKENS
ENDOTHELIUM
IN VITRO
IODINE 125
LABELLED COMPOUNDS
OVALBUMIN
PROTEINS
RABBITS
TRACER TECHNIQUES
TRANSFERRIN
ANIMAL TISSUES
ANIMALS
ARTERIES
BETA DECAY RADIOISOTOPES
BIRDS
BLOOD VESSELS
BODY
CARBOHYDRATES
CARDIOVASCULAR SYSTEM
COAGULANTS
DAYS LIVING RADIOISOTOPES
DRUGS
ELECTRON CAPTURE RADIOISOTOPES
ENZYMES
FOWL
GLOBULINS
GLOBULINS-BETA
GLUCOPROTEINS
HEMATOLOGIC AGENTS
HEMOSTATICS
HYDROLASES
INTERMEDIATE MASS NUCLEI
IODINE ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
MAMMALS
METALLOPROTEINS
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
ORGANS
PEPTIDE HYDROLASES
RADIOISOTOPES
SACCHARIDES
SERINE PROTEINASES
TISSUES
VERTEBRATES
551001* - Physiological Systems- Tracer Techniques