PMID- 10625689
OWN - NLM
STAT- MEDLINE
DCOM- 20000218
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 2
DP  - 2000 Jan 14
TI  - Post-translational proteolytic processing of procollagen C-terminal proteinase
      enhancer releases a metalloproteinase inhibitor.
PG  - 1384-90
AB  - Activity of matrix metalloproteinases (MMP) is regulated by a family of proteins 
      called tissue inhibitors of metalloproteinases (TIMP). Four TIMPs have been
      cloned, and their molecular weights range from 29,000 to 20,000. By reverse
      zymography, we have observed a metalloproteinase inhibitor with an apparent
      molecular weight of 16, 500 from medium conditioned by human brain tumor cells.
      Antibodies directed against TIMPs failed to react with the 16,500 molecular
      weight inhibitor, indicating that it was not a truncated form of a known TIMP.
      The inhibitor was isolated from conditioned medium using affinity and ion
      exchange chromatography. N-terminal sequences of the inhibitor matched amino acid
      sequences within the C-terminal domain of a protein known as procollagen
      C-terminal proteinase enhancer (PCPE). Thus, the inhibitor was named CT-PCPE.
      Comparison of the N-terminal domain of TIMP with CT-PCPE revealed that both
      contained six cysteine residues. As in the case of TIMP, reduction and alkylation
      abolished the inhibitory activity of CT-PCPE. Purified CT-PCPE inhibited MMP-2
      with an IC(50) value much greater than that of TIMP-2. This implies that MMPs may
      not be the physiologic targets for CT-PCPE inhibition. However, these results
      suggest that CT-PCPE may constitute a new class of metalloproteinase inhibitor.
FAU - Mott, J D
AU  - Mott JD
AD  - Department of Radiology, University of California, San Francisco, California
      94143-0750, USA. JDMott@lbl.gov
FAU - Thomas, C L
AU  - Thomas CL
FAU - Rosenbach, M T
AU  - Rosenbach MT
FAU - Takahara, K
AU  - Takahara K
FAU - Greenspan, D S
AU  - Greenspan DS
FAU - Banda, M J
AU  - Banda MJ
LA  - eng
GR  - AR43621/AR/NIAMS NIH HHS/United States
GR  - GM46846/GM/NIGMS NIH HHS/United States
GR  - T32-ES07106/ES/NIEHS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Extracellular Matrix Proteins)
RN  - 0 (Glycoproteins)
RN  - 0 (PCOLCE protein, human)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Tissue Inhibitor of Metalloproteinases)
RN  - EC 3.4.21.7 (Fibrinolysin)
SB  - IM
MH  - Amino Acid Sequence
MH  - Brain Neoplasms
MH  - Chromatography, Affinity
MH  - Chromatography, Ion Exchange
MH  - Extracellular Matrix Proteins
MH  - Fibrinolysin/metabolism
MH  - Glycoproteins/*chemistry/genetics/isolation & purification/*metabolism
MH  - Humans
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - *Protein Processing, Post-Translational
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Tissue Inhibitor of Metalloproteinases/*chemistry/isolation &
      purification/*metabolism
MH  - Tumor Cells, Cultured
EDAT- 2000/01/08 09:00
MHDA- 2000/02/26 09:00
CRDT- 2000/01/08 09:00
PHST- 2000/01/08 09:00 [pubmed]
PHST- 2000/02/26 09:00 [medline]
PHST- 2000/01/08 09:00 [entrez]
AID - 10.1074/jbc.275.2.1384 [doi]
AID - S0021-9258(18)31261-4 [pii]
PST - ppublish
SO  - J Biol Chem. 2000 Jan 14;275(2):1384-90. doi: 10.1074/jbc.275.2.1384.