Atlas of Genetics and Cytogenetics in Oncology and Haematology


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MMP11 (matrix metalloproteinase 11 (stromelysin 3))

Identity

Other namesST3 (stromelysin-3)
MMP-11 (matrix metalloproteinase 11)
HGNC MMP11
Location 22q11.2

DNA/RNA

Description 8 exons and 7 introns spanning 11.5 kb; cDNA: 2247 bp, coding sequence 1464 bp
Transcription expression is induced by retinoic acid and TPA through a DR1-type responsive element and a C/EBP binding site, respectively, expression is induced by epithelial cells in a paracrin manner

Protein

Description 488 amino-acids; 51 kDa; functional domains: signal peptide, targeting the protein to the secretory pathway, prodomain containing a furin-type cleavage site responsible for the intracellular activation, catalytic domain containing a zinc binding site, hemopexin-like domain
Expression cells of mesenchymal origin, notably fibroblastic cells, macrophages, osteoclasts
Function extracellular zinc-dependent proteinase expressed during tissu remodelling processes (development, wound healing) and whose specific substrate is unknown
Homology member of the matrix metalloproteinases (MMP) subfamily of matrixins

Implicated in

Entity various cancer:
Disease expression of ST3 in 80 to 100% invasive carcinomas of the breast, colon, head and neck, lung, ovary, pancreas, prostate, skin (basal cell carcinoma), uterus (cervix carcinoma and endometrial carcinoma) and in some non-invasive carcinomas that have a high risk of evolving towards invasion; also expression in: fibroblastic stromal cells in the close vicinity of cancerous epithelial cells
Prognosis prognostic factor of invasion and aggressiveness of the tumors
  

External links

Nomenclature
HGNCMMP11   7157
Entrez_GeneMMP11  4320  matrix metallopeptidase 11 (stromelysin 3)
Cards
AtlasST3ID200
GeneCardsMMP11
EnsemblMMP11 [Search_View]   ENSG00000099953 [Gene_View]
GenatlasMMP11
GeneLynxMMP11
eGenomeMMP11
euGene4320
Genomic and cartography
GoldenPathMMP11  -  22q11.2   chr22:22445036-22456503 +  22q11.23   [Description]    (hg18-Mar_2006)
EnsemblMMP11 - 22q11.23 [CytoView]
NCBIMapview
OMIMDisease map [OMIM]
HomoloGeneMMP11
Gene and transcription
GenbankAK075448 [ ENTREZ ]
GenbankAK125911 [ ENTREZ ]
GenbankAK129792 [ ENTREZ ]
GenbankBC057788 [ ENTREZ ]
GenbankCR602252 [ ENTREZ ]
RefSeqNM_005940 [ SRS ]    NM_005940 [ ENTREZ ]
RefSeqAC_000065 [ SRS ]    AC_000065 [ ENTREZ ]
RefSeqAC_000154 [ SRS ]    AC_000154 [ ENTREZ ]
RefSeqNC_000022 [ SRS ]    NC_000022 [ ENTREZ ]
RefSeqNT_011520 [ SRS ]    NT_011520 [ ENTREZ ]
RefSeqNW_001838745 [ SRS ]    NW_001838745 [ ENTREZ ]
RefSeqNW_927628 [ SRS ]    NW_927628 [ ENTREZ ]
AceViewMMP11 AceView - NCBI
UnigeneHs.143751 [ SRS ]    Hs.143751 [ NCBI ]     HS143751 [ spliceNest ]
Fast-db2592 (alternative variants)
Protein : pattern, domain, 3D structure
SwissProtP24347 [ SRS]    P24347 [ EXPASY ]     P24347 [ INTERPRO ]     P24347 [ UNIPROT ]
PrositePS00546 CYSTEINE_SWITCH [ SRS ]    PS00546 CYSTEINE_SWITCH [ Expasy ]
PrositePS00024 HEMOPEXIN [ SRS ]    PS00024 HEMOPEXIN [ Expasy ]
PrositePS00142 ZINC_PROTEASE [ SRS ]    PS00142 ZINC_PROTEASE [ Expasy ]
InterproIPR000585 Hemopexin [ SRS ]    IPR000585 Hemopexin [ EBI ]
InterproIPR001818 Pept_M10A_M12B [ SRS ]    IPR001818 Pept_M10A_M12B [ EBI ]
InterproIPR016293 Pept_M10A_matrix [ SRS ]    IPR016293 Pept_M10A_matrix [ EBI ]
InterproIPR006025 Pept_M_Zn_BS [ SRS ]    IPR006025 Pept_M_Zn_BS [ EBI ]
InterproIPR006026 Peptidase_M [ SRS ]    IPR006026 Peptidase_M [ EBI ]
CluSTrP24347
PfamPF00045 Hemopexin [ SRS ]    PF00045 Hemopexin [ Sanger ]    pfam00045 [ NCBI-CDD ]
PfamPF00413 Peptidase_M10 [ SRS ]    PF00413 Peptidase_M10 [ Sanger ]    pfam00413 [ NCBI-CDD ]
SmartSM00120 HX [EMBL]
SmartSM00235 ZnMc [EMBL]
BlocksP24347
HPRD01705
Protein Interaction databases
DIPP24347
IntActP24347
Polymorphism : SNP, mutations, diseases
OMIM185261    [ map ]   
GENECLINICS185261
SNPMMP11 [dbSNP-NCBI]  
SNPNM_005940 [SNP-NCI]  
SNPMMP11 [GeneSNPs - Utah]  MMP11] [HGBASE - SRS]
HAPMAPMMP11 [HAPMAP]  
COSMICMMP11 [Somatic mutation (COSMIC-CGP-Sanger)]  
HGMDMMP11
General knowledge
Family BrowserMMP11 [UCSC Family Browser]
SOURCENM_005940
SMDHs.143751
SAGEHs.143751
Enzyme3.4.24.- [ Enzyme-Expasy ]   3.4.24.- [ Enzyme-SRS ]   3.4.24.- [ IntEnz-EBI ]   3.4.24.- [ BRENDA ]   3.4.24.- [ KEGG ]   3.4.24.- [ WIT ]
GOstromelysin 3 activity [Amigo]  stromelysin 3 activity
GOcalcium ion binding [Amigo]  calcium ion binding
GOextracellular region [Amigo]  extracellular region
GOproteinaceous extracellular matrix [Amigo]  proteinaceous extracellular matrix
GOproteolysis [Amigo]  proteolysis
GOmulticellular organismal development [Amigo]  multicellular organismal development
GOzinc ion binding [Amigo]  zinc ion binding
GOcollagen catabolic process [Amigo]  collagen catabolic process
PubGeneMMP11
TreeFamMMP11
CTD4320 [Comparative ToxicoGenomics Database]
Other databases
Probes
ProbeMMP11 Related clones (RZPD - Berlin)
PubMed
PubMed27 Pubmed reference(s) in LocusLink

Bibliography

A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas.
Basset P, Bellocq JP, Wolf C, Stoll I, Hutin P, Limacher JM, Podhajcer OL, Chenard MP, Rio MC, Chambon P
Nature. 1990 ; 348 (6303) : 699-704.
PMID 1701851
 
Stromelysin-3 gene expression in human cancer: an overview.
Rouyer N, Wolf C, Chenard MP, Rio MC, Chambon P, Bellocq JP, Basset P
Invasion & metastasis. 1994 19 95 ; 14 (1-6) : 269-275.
PMID 7657519
 
Structure and promoter characterization of the human stromelysin-3 gene.
Anglard P, Melot T, Guˆ©rin E, Thomas G, Basset P
The Journal of biological chemistry. 1995 ; 270 (35) : 20337-20344.
PMID 7657606
 
High levels of stromelysin-3 correlate with poor prognosis in patients with breast carcinoma.
Chenard MP, O'Siorain L, Shering S, Rouyer N, Lutz Y, Wolf C, Basset P, Bellocq JP, Duffy MJ
International journal of cancer. Journal international du cancer. 1996 ; 69 (6) : 448-451.
PMID 8980245
 
Stromelysin-3 is induced in tumor/stroma cocultures and inactivated via a tumor-specific and basic fibroblast growth factor-dependent mechanism.
Mari BP, Anderson IC, Mari SE, Ning Y, Lutz Y, Kobzik L, Shipp MA
The Journal of biological chemistry. 1998 ; 273 (1) : 618-626.
PMID 9417124
 
Stromelysin 3: an independent prognostic factor for relapse-free survival in node-positive breast cancer and demonstration of novel breast carcinoma cell expression.
Ahmad A, Hanby A, Dublin E, Poulsom R, Smith P, Barnes D, Rubens R, Anglard P, Hart I
The American journal of pathology. 1998 ; 152 (3) : 721-728.
PMID 9502414
 
In vivo evidence that the stromelysin-3 metalloproteinase contributes in a paracrine manner to epithelial cell malignancy.
Masson R, Lefebvre O, Noˆ´l A, Fahime ME, Chenard MP, Wendling C, Kebers F, LeMeur M, Dierich A, Foidart JM, Basset P, Rio MC
The Journal of cell biology. 1998 ; 140 (6) : 1535-1541.
PMID 9508784
 
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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Contributor(s)

Written03-2000Paul Basset, Marie-Christine Rio
Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS/INSERM U184/ULP BP 163, Illkirch, CU de Strasbourg, France

Citation

This paper should be referenced as such :
Basset P and Rio MC . MMP11 (matrix metalloproteinase 11 (stromelysin 3)). Atlas Genet Cytogenet Oncol Haematol. March 2000 .
URL : http://AtlasGeneticsOncology.org/Genes/ST3ID200.html

© Atlas of Genetics and Cytogenetics in Oncology and Haematology
indexed on : Mon Aug 11 21:17:42 2008


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