Neutrophil proteases in plasminogen activation.

R. Machovich, A. Himer, W. G. Owen

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Leukocyte elastase and leukocyte cathepsin G degrade porcine plasminogen primarily by hydrolysis of the A447-I448 bond between kringle4 and kringle5. The rate of formation of des-kringle1-4-plasminogen is faster with elastase (k"obs greater than 10(5) mol-1 s-1) than with cathepsin G (kobs less than 300 mol-1 s-1). In contrast to elastase, leukocyte cathepsin G does not inactivate alpha 2-antiplasmin. Consequently, plasminogen activation by urokinase in the presence of alpha 2-antiplasmin is elastase-dependent, but cathepsin G does not overcome the action of alpha 2-antiplasmin. The rate-enhancing effect of fibrin(ogen) fragments in plasminogen activation by tissue-type plasminogen activator is also disabled efficiently by these proteases. It is concluded that enhancement of plasmin expression by neutrophil proteases is accounted for primarily by the action of elastase.

Original languageEnglish
Pages (from-to)273-277
Number of pages5
JournalBlood Coagulation and Fibrinolysis
Volume1
Issue number3
Publication statusPublished - Aug 1990

Fingerprint

Cathepsin G
alpha-2-Antiplasmin
Plasminogen
Pancreatic Elastase
Neutrophils
Peptide Hydrolases
Leukocyte Elastase
Fibrinolysin
Urokinase-Type Plasminogen Activator
Tissue Plasminogen Activator
Fibrin
Hydrolysis
Leukocytes
Swine

ASJC Scopus subject areas

  • Hematology

Cite this

Neutrophil proteases in plasminogen activation. / Machovich, R.; Himer, A.; Owen, W. G.

In: Blood Coagulation and Fibrinolysis, Vol. 1, No. 3, 08.1990, p. 273-277.

Research output: Contribution to journalArticle

Machovich, R. ; Himer, A. ; Owen, W. G. / Neutrophil proteases in plasminogen activation. In: Blood Coagulation and Fibrinolysis. 1990 ; Vol. 1, No. 3. pp. 273-277.
@article{8956fe858ddb449b8bb2651a82ba142f,
title = "Neutrophil proteases in plasminogen activation.",
abstract = "Leukocyte elastase and leukocyte cathepsin G degrade porcine plasminogen primarily by hydrolysis of the A447-I448 bond between kringle4 and kringle5. The rate of formation of des-kringle1-4-plasminogen is faster with elastase (k{"}obs greater than 10(5) mol-1 s-1) than with cathepsin G (kobs less than 300 mol-1 s-1). In contrast to elastase, leukocyte cathepsin G does not inactivate alpha 2-antiplasmin. Consequently, plasminogen activation by urokinase in the presence of alpha 2-antiplasmin is elastase-dependent, but cathepsin G does not overcome the action of alpha 2-antiplasmin. The rate-enhancing effect of fibrin(ogen) fragments in plasminogen activation by tissue-type plasminogen activator is also disabled efficiently by these proteases. It is concluded that enhancement of plasmin expression by neutrophil proteases is accounted for primarily by the action of elastase.",
author = "R. Machovich and A. Himer and Owen, {W. G.}",
year = "1990",
month = "8",
language = "English",
volume = "1",
pages = "273--277",
journal = "Blood Coagulation and Fibrinolysis",
issn = "0957-5235",
publisher = "Lippincott Williams and Wilkins",
number = "3",

}

TY - JOUR

T1 - Neutrophil proteases in plasminogen activation.

AU - Machovich, R.

AU - Himer, A.

AU - Owen, W. G.

PY - 1990/8

Y1 - 1990/8

N2 - Leukocyte elastase and leukocyte cathepsin G degrade porcine plasminogen primarily by hydrolysis of the A447-I448 bond between kringle4 and kringle5. The rate of formation of des-kringle1-4-plasminogen is faster with elastase (k"obs greater than 10(5) mol-1 s-1) than with cathepsin G (kobs less than 300 mol-1 s-1). In contrast to elastase, leukocyte cathepsin G does not inactivate alpha 2-antiplasmin. Consequently, plasminogen activation by urokinase in the presence of alpha 2-antiplasmin is elastase-dependent, but cathepsin G does not overcome the action of alpha 2-antiplasmin. The rate-enhancing effect of fibrin(ogen) fragments in plasminogen activation by tissue-type plasminogen activator is also disabled efficiently by these proteases. It is concluded that enhancement of plasmin expression by neutrophil proteases is accounted for primarily by the action of elastase.

AB - Leukocyte elastase and leukocyte cathepsin G degrade porcine plasminogen primarily by hydrolysis of the A447-I448 bond between kringle4 and kringle5. The rate of formation of des-kringle1-4-plasminogen is faster with elastase (k"obs greater than 10(5) mol-1 s-1) than with cathepsin G (kobs less than 300 mol-1 s-1). In contrast to elastase, leukocyte cathepsin G does not inactivate alpha 2-antiplasmin. Consequently, plasminogen activation by urokinase in the presence of alpha 2-antiplasmin is elastase-dependent, but cathepsin G does not overcome the action of alpha 2-antiplasmin. The rate-enhancing effect of fibrin(ogen) fragments in plasminogen activation by tissue-type plasminogen activator is also disabled efficiently by these proteases. It is concluded that enhancement of plasmin expression by neutrophil proteases is accounted for primarily by the action of elastase.

UR - http://www.scopus.com/inward/record.url?scp=0025476769&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025476769&partnerID=8YFLogxK

M3 - Article

C2 - 1715763

AN - SCOPUS:0025476769

VL - 1

SP - 273

EP - 277

JO - Blood Coagulation and Fibrinolysis

JF - Blood Coagulation and Fibrinolysis

SN - 0957-5235

IS - 3

ER -