How matrix metalloproteinases regulate cell behavior

Citation
Md. Sternlicht et Z. Werb, How matrix metalloproteinases regulate cell behavior, ANN R C DEV, 17, 2001, pp. 463-516
Citations number
230
Language
INGLESE
art.tipo
Review
Categorie Soggetti
Cell & Developmental Biology
Journal title
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY
ISSN journal
1081-0706 → ACNP
Volume
17
Year of publication
2001
Pages
463 - 516
Database
ISI
SICI code
1081-0706(2001)17:<463:HMMRCB>2.0.ZU;2-9
Abstract
The matrix metalloproteinases (MMPs) constitute a multigene family of over 25 secreted and cell surface enzymes that process or degrade numerous peric ellular substrates. Their targets include other proteinases, proteinase inh ibitors, clotting factors, chemotactic molecules, latent growth factors, gr owth factor-binding proteins, cell surface receptors, cell-cell adhesion mo lecules, and virtually all structural extracellular matrix proteins. Thus M MPs are able to regulate many biologic processes and are closely regulated themselves. We review recent advances that help to explain how MMPs work, h ow they are controlled, and how they influence biologic behavior. These adv ances shed light on how the structure and function of the MMPs are related and on how their transcription, secretion, activation, inhibition, localiza tion, and clearance are controlled. MMPs participate in numerous normal and abnormal processes, and there are new insights into the key substrates and mechanisms responsible for regulating some of these processes in vivo. Our knowledge in the field of MMP biology is rapidly expanding, yet we still d o not fully understand how these enzymes regulate most processes of develop ment, homeostasis, and disease.