Proteases associated with invadopodia, and their role in degradation of extracellular matrix

被引：105

作者：

Chen, WT ^{[1
]}

机构：

[1] GEORGETOWN UNIV, DEPT CELL BIOL, SCH MED, WASHINGTON, DC 20007 USA

来源：

ENZYME & PROTEIN | 1996年 / 49卷 / 1-3期

关键词：

dipeptidyl peptidase IV; fibroblast activation protein; gelatinase; membrane-type matrix metalloprotease; meprin; guanidinobenzoatase; seprase;

D O I：

10.1159/000468616

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Metastasizing cancer cells invade the extracellular matrix using plasma membrane protrusions (invadopodia) that contact and dissolve the matrix. Evidence suggests that membrane-associated proteases, 170-kD gelatinase (seprase) and Gelatinase A, exert their mechanisms of action on invadopodia. Potential roles that other metallo- and serine-types of membrane proteases, including membrane-type matrix metalloprotease, meprin, dipeptidyl peptidase IV, fibroblast activation protein a and guanidinobenzoatase, play in the cell surface proteolysis are also discussed. It is proposed that formation of a structurally and functionally linked protease complex on invadopodia allows the invasion of cancer cells into the extracellular matrix.

引用

页码：59 / 71

页数：13

共 84 条

[1] MATRIX METALLOPROTEINASE-2 IS AN INTERSTITIAL COLLAGENASE - INHIBITOR-FREE ENZYME CATALYZES THE CLEAVAGE OF COLLAGEN FIBRILS AND SOLUBLE NATIVE TYPE-I COLLAGEN GENERATING THE SPECIFIC 3/4-LENGTH AND 1/4-LENGTH FRAGMENTS [J].

AIMES, RT ;

QUIGLEY, JP .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (11) :5872-5876

[2] A 170-KDA MEMBRANE-BOUND PROTEASE IS ASSOCIATED WITH THE EXPRESSION OF INVASIVENESS BY HUMAN-MALIGNANT MELANOMA-CELLS [J].

AOYAMA, A ;

CHEN, WT .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1990, 87 (21) :8296-8300

[3]

AZZAM HS, 1992, CANCER RES, V52, P4540

[4] ASSOCIATION OF MMP-2 ACTIVATION POTENTIAL WITH METASTATIC PROGRESSION IN HUMAN BREAST-CANCER CELL-LINES INDEPENDENT OF MMP-2 PRODUCTION [J].

AZZAM, HS ;

ARAND, G ;

LIPPMAN, ME ;

THOMPSON, EW .

JOURNAL OF THE NATIONAL CANCER INSTITUTE, 1993, 85 (21) :1758-1764

[5] A COLLAGEN-BINDING GLYCOPROTEIN ON THE SURFACE OF MOUSE FIBROBLASTS IS IDENTIFIED AS DIPEPTIDYL PEPTIDASE-IV [J].

BAUVOIS, B .

BIOCHEMICAL JOURNAL, 1988, 252 (03) :723-731

[6] ASTACINS, SERRALYSINS, SNAKE-VENOM AND MATRIX METALLOPROTEINASES EXHIBIT IDENTICAL ZINC-BINDING ENVIRONMENTS (HEXXHXXGXXH AND MET-TURN) AND TOPOLOGIES AND SHOULD BE GROUPED INTO A COMMON FAMILY, THE METZINCINS [J].

BODE, W ;

GOMISRUTH, FX ;

STOCKLER, W .

FEBS LETTERS, 1993, 331 (1-2) :134-140

[7]

BOND JS, 1991, BIOMED BIOCHIM ACTA, V50, P775

[8] FOCAL ADHESIONS - TRANSMEMBRANE JUNCTIONS BETWEEN THE EXTRACELLULAR-MATRIX AND THE CYTOSKELETON [J].

BURRIDGE, K ;

FATH, K ;

KELLY, T ;

NUCKOLLS, G ;

TURNER, C .

ANNUAL REVIEW OF CELL BIOLOGY, 1988, 4 :487-525

[9] T-CELL ACTIVATION ANTIGEN, CD26, AS A COFACTOR FOR ENTRY OF HIV IN CD4+ CELLS [J].

CALLEBAUT, C ;

KRUST, B ;

JACOTOT, E ;

HOVANESSIAN, AG .

SCIENCE, 1993, 262 (5142) :2045-2050

[10] THE C-TERMINAL REGION OF MEMBRANE TYPE MATRIX METALLOPROTEINASE IS A FUNCTIONAL TRANSMEMBRANE DOMAIN REQUIRED FOR PRO-GELATINASE-C ACTIVATION [J].

CAO, J ;

SATO, H ;

TAKINO, T ;

SEIKI, M .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (02) :801-805

← 1 2 3 4 5 6 7 8 9 →