PMID- 15166260
OWN - NLM
STAT- MEDLINE
DCOM- 20040621
LR  - 20190501
IS  - 0021-9746 (Print)
IS  - 1472-4146 (Electronic)
IS  - 0021-9746 (Linking)
VI  - 57
IP  - 6
DP  - 2004 Jun
TI  - Membrane associated proteases and their inhibitors in tumour angiogenesis.
PG  - 577-84
AB  - Cell surface proteolysis is an important mechanism for generating biologically 
      active proteins that mediate a range of cellular functions and contribute to 
      biological processes such as angiogenesis. Although most studies have focused on 
      the plasminogen system and matrix metalloproteinases (MMPs), recently there has 
      been an increase in the identification of membrane associated proteases, 
      including serine proteases, ADAMs, and membrane-type MMPs (MT-MMPs). Normally, 
      protease activity is tightly controlled by tissue inhibitors of MMPs (TIMPs) and 
      plasminogen activator inhibitors (PAIs). The balance between active proteases and 
      inhibitors is thought to determine the occurrence of proteolysis in vivo. High 
      concentrations of proteolytic system components correlate with poor prognosis in 
      many cancers. Paradoxically, high (not low) PAI-1 or TIMP concentrations predict 
      poor survival in patients with various cancers. Recent observations indicate a 
      much more complex role for protease inhibitors in tumour progression and 
      angiogenesis than initially expected. As knowledge in the field of protease 
      biology has improved, the unforeseen complexities of cell associated enzymes and 
      their interaction with physiological inhibitors have emerged, often revealing 
      unexpected mechanisms of action.
FAU - Noel, A
AU  - Noel A
AD  - Laboratory of Tumour and Development Biology, University of Liege, Sart Tilman, 
      B-4000 Liege, Belgium. noel@ulg.ac.be
FAU - Maillard, C
AU  - Maillard C
FAU - Rocks, N
AU  - Rocks N
FAU - Jost, M
AU  - Jost M
FAU - Chabottaux, V
AU  - Chabottaux V
FAU - Sounni, N E
AU  - Sounni NE
FAU - Maquoi, E
AU  - Maquoi E
FAU - Cataldo, D
AU  - Cataldo D
FAU - Foidart, J M
AU  - Foidart JM
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - England
TA  - J Clin Pathol
JT  - Journal of clinical pathology
JID - 0376601
RN  - 0 (Protease Inhibitors)
RN  - 0 (Tissue Inhibitor of Metalloproteinases)
RN  - EC 3.4.- (Endopeptidases)
RN  - EC 3.4.21.- (Serine Endopeptidases)
RN  - EC 3.4.24.- (Matrix Metalloproteinases)
SB  - IM
MH  - Cell Membrane/physiology
MH  - Endopeptidases/*physiology
MH  - Humans
MH  - Matrix Metalloproteinases/physiology
MH  - Neoplasms/*blood supply
MH  - Neovascularization, Pathologic/*physiopathology
MH  - Protease Inhibitors/*metabolism
MH  - Serine Endopeptidases/physiology
MH  - Tissue Inhibitor of Metalloproteinases/physiology
PMC - PMC1770325
EDAT- 2004/05/29 05:00
MHDA- 2004/06/24 05:00
PMCR- 2007/06/01
CRDT- 2004/05/29 05:00
PHST- 2004/05/29 05:00 [pubmed]
PHST- 2004/06/24 05:00 [medline]
PHST- 2004/05/29 05:00 [entrez]
PHST- 2007/06/01 00:00 [pmc-release]
AID - 0570577 [pii]
AID - 10.1136/jcp.2003.014472 [doi]
PST - ppublish
SO  - J Clin Pathol. 2004 Jun;57(6):577-84. doi: 10.1136/jcp.2003.014472.