Proteolytic events of wound-healing-coordinated interactions among matrix metalloproteinases (MMPs), integrins, and extracellular matrix molecules

被引:151
作者
Steffensen, B
Häkkinen, L
Larjava, H
机构
[1] Univ Texas, Hlth Sci Ctr, Dept Periodont, San Antonio, TX 78229 USA
[2] Univ British Columbia, Dept Oral Biol & Med Sci, Vancouver, BC V5Z 1M9, Canada
关键词
matrix metalloproteinases; MMP; integrins; extracellular matrix; wound-healing;
D O I
10.1177/10454411010120050201
中图分类号
R78 [口腔科学];
学科分类号
1003 ;
摘要
During wound-healing, cells are required to migrate rapidly into the wound site via a proteolytically generated pathway in the provisional matrix, to produce new extracellular matrix, and, subsequently, to remodel the newly formed tissue matrix during the maturation phase. Two classes of molecules cooperate closely to achieve this goal, namely, the matrix adhesion and signaling receptors, the integrins, and matrix-degrading and -processing enzymes, the matrix metalloproteinases (MMPs). There is now substantial experimental evidence that blocking key molecules of either group will prevent or seriously delay wound-healing. It has been known for some time now that cell adhesion by means of the integrins regulates the expression of MMPs. In addition, certain MMPs can bind to integrins or other receptors on the cell surface involved in enzyme activation, thereby providing a mechanism for localized matrix degradation. By proteolytically modifying the existing matrix molecules, the MMPs can then induce changes in cell behavior and function from a state of rest to migration. During wound repair, the expression of integrins and MMPs is simultaneously up-regulated. This review will focus on those aspects of the extensive knowledge of fibroblast and keratinocyte MMPs and integrins in biological processes that relate to wound-healing.
引用
收藏
页码:373 / 398
页数:26
相关论文
共 345 条
[1]  
Abbey RS, 1997, J DENT RES, V76, P2290
[2]   GELATINASE ACTIVITY DURING WOUND-HEALING [J].
AGREN, MS .
BRITISH JOURNAL OF DERMATOLOGY, 1994, 131 (05) :634-640
[3]   Matrix metalloproteinases (MMPs) are required for re-epithelialization of cutaneous wounds [J].
Ågren, MS .
ARCHIVES OF DERMATOLOGICAL RESEARCH, 1999, 291 (11) :583-590
[4]  
Agrez M, 1999, INT J CANCER, V81, P90, DOI 10.1002/(SICI)1097-0215(19990331)81:1<90::AID-IJC16>3.0.CO
[5]  
2-K
[6]  
AnandApte B, 1997, INVEST OPHTH VIS SCI, V38, P817
[7]  
Aplin AE, 1998, PHARMACOL REV, V50, P197
[8]   Cell adhesion molecules, signal transduction and cell growth [J].
Aplin, AE ;
Howe, AK ;
Juliano, RL .
CURRENT OPINION IN CELL BIOLOGY, 1999, 11 (06) :737-744
[9]   Age-related differences in the temporal and spatial regulation of matrix metalloproteinases (MMPs) in normal skin and acute cutaneous wounds of healthy humans [J].
Ashcroft, GS ;
Horan, MA ;
Herrick, SE ;
Tarnuzzer, RW ;
Schultz, GS ;
Ferguson, MWJ .
CELL AND TISSUE RESEARCH, 1997, 290 (03) :581-591
[10]   Fibrillin degradation by matrix metalloproteinases: implications for connective tissue remodelling [J].
Ashworth, JL ;
Murphy, G ;
Rock, MJ ;
Sherratt, MJ ;
Shapiro, SD ;
Shuttleworth, CA ;
Kielty, CM .
BIOCHEMICAL JOURNAL, 1999, 340 :171-181