MINIREVIEWS
Cell Research (1998)8:171-177
© 1998 SIBS, CAS All rights reserved 1001-0602/98
Complex role of matrix metalloproteinases in angiogenesis.
Sang QX.
Department of Chemistry, Florida State University, Tallahassee 32306-4390,
USA.
Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases
(TIMPs) play a significant role in regulating angiogenesis, the process
of new blood vessel formation. Interstitial collagenase (MMP-1), 72 kDa
gelatinase A/type IV collagenase (MMP-2), and 92 kDa gelatinase B/type IV
collagenase (MMP-9) dissolve extracellular matrix (ECM) and may initiate
and promote angiogenesis. TIMP-1, TIMP-2, TIMP-3, and possibly, TIMP-4 inhibit
neovascularization. A new paradigm is emerging that matrilysin (MMP-7),
MMP-9, and metalloelastase (MMP-12) may block angiogenesis by converting
plasminogen to angiostatin, which is one of the most potent angiogenesis
antagonists. MMPs and TIMPs play a complex role in regulating angiogenesis.
An understanding of the biochemical and cellular pathways and mechanisms
of angiogenesis will provide important information to allow the control
of angiogenesis, e.g. the stimulation of angiogenesis for coronary collateral
circulation formation; while the inhibition for treating arthritis and cancer.
Keywords : Collagenases,
tissue inhibitors of metalloproteinases, neovascularization, plasminogen
angiostatin converting enzymes, extracellular matrix. |
