Interaction of Blood Coagulation and Fibrinolytic Factors with Intact Erythrocytes and Erythrocyte Membranes

Bibliographic Details
Main Author: Burkholder, David E.
Language:English
Published: Bowling Green State University / OhioLINK 1975
Subjects:
Online Access:http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1566297702068354
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spelling ndltd-OhioLink-oai-etd.ohiolink.edu-bgsu15662977020683542021-08-03T07:12:35Z Interaction of Blood Coagulation and Fibrinolytic Factors with Intact Erythrocytes and Erythrocyte Membranes Burkholder, David E. Biology It has recently been suggested that red blood cell membranes may serve a regulatory role in the blood by selective binding and inhibition of proteolytic enzymes, particularly those of the clotting mechanism (Burkholder and Brecher, 1972; Burkholder, 1973; Burkholder and Brecher, 1974). The studies reported herein indicate that bovine erythrocyte ghosts bind plasminogen and plasmin but do not inhibit the caseinolytic activity of plasmin. Urokinase is not bound to bovine erythrocyte membranes and readily activates plas-minogen in the presence of ghosts without an apparent loss in efficiency in contrast to trypsin which binds to membranes and activates plasminogen at a reduced rate in 3he presence of membranes. Increased binding of trypsin-H to ghosts was seen in the presence of plasminogen suggesting that there are separate binding sites on the surface of the membranes for trypsin and plasminogen, and that trypsin may bind directly to ghosts and to plasminogen which is bound to ghosts. A potential role for the possible transport of zymogens and enzymes involved in fibrinolysis in the blood was suggested on the basis of these results. Confirmation of the binding of trypsin-H and chymotrypsin-H was obtained with human erythrocyte membranes thereby minimizing species variability. However no binding of trypsin-H or chymotrypsin-H to intact erythro-cytes was observed, suggesting that binding of trypsin and chymotrypsin must be to membrane components exposed upon hemolysis of the intact cells, or that binding is transient and unstable in a centrifugal field. Tissue factor apoprotein purified from bovine lung, as well as C -relipidated tissue factor, thrombin and pro-thrombin (at the highest membrane level) were not adsorbed to intact erythrocytes nor to membranes to a considerable extent. Increased clotting activity was observed upon exposure of and subsequent separation of relipidated tissue factor from intact human cells or membranes. Thus, intact erythrocytes may play a relatively minor role in the regulation and/or transport of clotting factors although ruptured erythrocytes may have much more reactive surface membrane properties which have the capacity to influence enzymic activity. 1975 English text Bowling Green State University / OhioLINK http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1566297702068354 http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1566297702068354 unrestricted This thesis or dissertation is protected by copyright: all rights reserved. It may not be copied or redistributed beyond the terms of applicable copyright laws.
collection NDLTD
language English
sources NDLTD
topic Biology
spellingShingle Biology
Burkholder, David E.
Interaction of Blood Coagulation and Fibrinolytic Factors with Intact Erythrocytes and Erythrocyte Membranes
author Burkholder, David E.
author_facet Burkholder, David E.
author_sort Burkholder, David E.
title Interaction of Blood Coagulation and Fibrinolytic Factors with Intact Erythrocytes and Erythrocyte Membranes
title_short Interaction of Blood Coagulation and Fibrinolytic Factors with Intact Erythrocytes and Erythrocyte Membranes
title_full Interaction of Blood Coagulation and Fibrinolytic Factors with Intact Erythrocytes and Erythrocyte Membranes
title_fullStr Interaction of Blood Coagulation and Fibrinolytic Factors with Intact Erythrocytes and Erythrocyte Membranes
title_full_unstemmed Interaction of Blood Coagulation and Fibrinolytic Factors with Intact Erythrocytes and Erythrocyte Membranes
title_sort interaction of blood coagulation and fibrinolytic factors with intact erythrocytes and erythrocyte membranes
publisher Bowling Green State University / OhioLINK
publishDate 1975
url http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1566297702068354
work_keys_str_mv AT burkholderdavide interactionofbloodcoagulationandfibrinolyticfactorswithintacterythrocytesanderythrocytemembranes
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