MMP3: Polycystic Ovarian Syndrome Database

MMP3

Gene Information
 
Gene Symbol
MMP3
 
Aliases
CHDS6, MMP-3, SL-1, STMY, STMY1, STR1
 
Entrez Gene ID
 
Gene Name
Matrix metallopeptidase 3
 
Chromosomal Location
11q22.2
 
HGNC ID
 
Summary
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene encodes an enzyme which degrades fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq, Jul 2008]
 
RefSeq DNA
 
RefSeq mRNA
  e!Ensembl
Gene
Transcript  
Protein

Gene Ontology (GO)

GO ID Ontology Function Evidence Reference
GO:0006508 Biological process Proteolysis IDA 12867428, 15863497, 19022250, 20969476
GO:0010727 Biological process Negative regulation of hydrogen peroxide metabolic process IDA 20969476
GO:0030198 Biological process Extracellular matrix organization IBA 21873635
GO:0030574 Biological process Collagen catabolic process IBA 21873635
GO:0032461 Biological process Positive regulation of protein oligomerization IDA 19022250
Protein Information
 
Protein Name
Stromelysin-1, matrix metalloproteinase 3 (stromelysin 1, progelatinase), proteoglycanase, transin-1
 
Function
Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase
 
Refseq Proteins
 
UniProt
 
PDB
 
Pfam
Pfam Accession Pfam ID
PF00045 Hemopexin
PF00413 Peptidase_M10
PF01471 PG_binding_1
Pathways
 
KEGG
 
Reactome
 

IL-17 signaling pathway
TNF signaling pathway
Transcriptional misregulation in cancer
Prostate cancer
Rheumatoid arthritis

  

Collagen degradation
Degradation of the extracellular matrix
Activation of Matrix Metalloproteinases
Assembly of collagen fibrils and other multimeric structures
EGFR Transactivation by Gastrin
Interleukin-4 and Interleukin-13 signaling
Extra-nuclear estrogen signaling
     

Associated Diseases

Disease groupDisease NameReferences
Cardiovascular Diseases
Arteriosclerosis
Coronary Restenosis
Endocrine System Diseases
PCOS
Neoplasms
Astrocytoma
Breast Cancer
References
 
 
PubMed ID Associated gene/s Associated condition Genetic Mutation Diagnostic Criteria Association with PCOS Ethnicity Conclusion
 
Pre-eclampsia and implantation abnormalities 
 
 Rotterdam criteria and NIH 
Related 
12 PCOS subjects and 6 Control 
 In conclusion, the study provides novel in vitro data showing that a subset of women with PCOS have an aberrant decidualization response of their eSF to E2 and P4, with concomitant increased pro-inflammatory cytokine, chemokine and MMP release—creating a microenvironment conducive to recruiting migratory immune cells. These data support the idea that the endometrium of women with PCOS may present a compromised endometrial environment for implantation and also abnormal endometrial function, resulting in sub-optimal implantation, and predisposition to endometrial cancer. 
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