Role of Annexin II tetramer in plasminogen activation

Hyoung Min Kang; Kyu Sil Choi; Geetha Kassam; Sandra L. Fitzpatrick; Mijung Kwon; David M. Waisman

doi:10.1016/S1050-1738(99)00012-2

Role of Annexin II tetramer in plasminogen activation

Hyoung Min Kang, Kyu Sil Choi, Geetha Kassam, Sandra L. Fitzpatrick, Mijung Kwon, David M. Waisman

Research output: Contribution to journal › Review article › peer-review

54 Citations (Scopus)

Abstract

The enzymatic cascade triggered by activation of plasminogen has been implicated in a variety of normal and pathologic events, such as fibrinolysis, wound healing, tissue remodeling, embryogenesis, and the invasion and spread of transformed tumor cells. Recent data established that the Ca²⁺- and phospholipid-binding protein, annexin II heterotetramer (AIIt) binds tissue-type plasminogen activator (tPA), plasminogen, and plasmin, and dramatically stimulates the tPA-dependent conversion of plasminogen to plasmin in vitro. Interestingly, the binding of plasmin to AIIt can inhibit the activity of the enzyme, suggesting that plasmin bound to the cell surface is regulated by AIIt. The existing experimental evidence suggests that AIIt is the key physiological receptor for plasminogen on the extracellular surface of endothelial cells. Copyright (C) 1999 Elsevier Science Inc.

Original language	English
Pages (from-to)	92-102
Number of pages	11
Journal	Trends in Cardiovascular Medicine
Volume	9
Issue number	3-4
DOIs	https://doi.org/10.1016/S1050-1738(99)00012-2
Publication status	Published - Apr 1999
Externally published	Yes

Bibliographical note

Funding Information:
Supported by a grant from the Medical Research Council (MT 13343), the Al berta Heart and Stroke Foundation, and the National Institutes of Health (1RO1CA78639-01).

ASJC Scopus Subject Areas

Cardiology and Cardiovascular Medicine

PubMed: MeSH publication types

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

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10.1016/S1050-1738(99)00012-2

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title = "Role of Annexin II tetramer in plasminogen activation",

abstract = "The enzymatic cascade triggered by activation of plasminogen has been implicated in a variety of normal and pathologic events, such as fibrinolysis, wound healing, tissue remodeling, embryogenesis, and the invasion and spread of transformed tumor cells. Recent data established that the Ca2+- and phospholipid-binding protein, annexin II heterotetramer (AIIt) binds tissue-type plasminogen activator (tPA), plasminogen, and plasmin, and dramatically stimulates the tPA-dependent conversion of plasminogen to plasmin in vitro. Interestingly, the binding of plasmin to AIIt can inhibit the activity of the enzyme, suggesting that plasmin bound to the cell surface is regulated by AIIt. The existing experimental evidence suggests that AIIt is the key physiological receptor for plasminogen on the extracellular surface of endothelial cells. Copyright (C) 1999 Elsevier Science Inc.",

author = "Kang, {Hyoung Min} and Choi, {Kyu Sil} and Geetha Kassam and Fitzpatrick, {Sandra L.} and Mijung Kwon and Waisman, {David M.}",

note = "Funding Information: Supported by a grant from the Medical Research Council (MT 13343), the Al berta Heart and Stroke Foundation, and the National Institutes of Health (1RO1CA78639-01).",

year = "1999",

month = apr,

doi = "10.1016/S1050-1738(99)00012-2",

language = "English",

volume = "9",

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journal = "Trends in Cardiovascular Medicine",

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T1 - Role of Annexin II tetramer in plasminogen activation

AU - Kang, Hyoung Min

AU - Choi, Kyu Sil

AU - Kassam, Geetha

AU - Fitzpatrick, Sandra L.

AU - Kwon, Mijung

AU - Waisman, David M.

N1 - Funding Information: Supported by a grant from the Medical Research Council (MT 13343), the Al berta Heart and Stroke Foundation, and the National Institutes of Health (1RO1CA78639-01).

PY - 1999/4

Y1 - 1999/4

N2 - The enzymatic cascade triggered by activation of plasminogen has been implicated in a variety of normal and pathologic events, such as fibrinolysis, wound healing, tissue remodeling, embryogenesis, and the invasion and spread of transformed tumor cells. Recent data established that the Ca2+- and phospholipid-binding protein, annexin II heterotetramer (AIIt) binds tissue-type plasminogen activator (tPA), plasminogen, and plasmin, and dramatically stimulates the tPA-dependent conversion of plasminogen to plasmin in vitro. Interestingly, the binding of plasmin to AIIt can inhibit the activity of the enzyme, suggesting that plasmin bound to the cell surface is regulated by AIIt. The existing experimental evidence suggests that AIIt is the key physiological receptor for plasminogen on the extracellular surface of endothelial cells. Copyright (C) 1999 Elsevier Science Inc.

AB - The enzymatic cascade triggered by activation of plasminogen has been implicated in a variety of normal and pathologic events, such as fibrinolysis, wound healing, tissue remodeling, embryogenesis, and the invasion and spread of transformed tumor cells. Recent data established that the Ca2+- and phospholipid-binding protein, annexin II heterotetramer (AIIt) binds tissue-type plasminogen activator (tPA), plasminogen, and plasmin, and dramatically stimulates the tPA-dependent conversion of plasminogen to plasmin in vitro. Interestingly, the binding of plasmin to AIIt can inhibit the activity of the enzyme, suggesting that plasmin bound to the cell surface is regulated by AIIt. The existing experimental evidence suggests that AIIt is the key physiological receptor for plasminogen on the extracellular surface of endothelial cells. Copyright (C) 1999 Elsevier Science Inc.

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AN - SCOPUS:0033117168

SN - 1050-1738

VL - 9

SP - 92

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JO - Trends in Cardiovascular Medicine

JF - Trends in Cardiovascular Medicine

IS - 3-4

ER -

Role of Annexin II tetramer in plasminogen activation

Abstract

Bibliographical note

ASJC Scopus Subject Areas

PubMed: MeSH publication types

Access to Document

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