MMP26

Matrix metallopeptidase 26

Identifiers

MMP26; MGC126590; MGC126592

External IDs

OMIM: 605470 HomoloGene: 49684 ChEMBL: 4707 GeneCards: MMP26 Gene

3.4.24.1

Gene Ontology
Molecular function	• metalloendopeptidase activity • zinc ion binding
Cellular component	• proteinaceous extracellular matrix
Biological process	• proteolysis • collagen catabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

n/a

n/a

RefSeq (mRNA)

NM_021801

n/a

RefSeq (protein)

NP_068573

n/a

Location (UCSC)

Chr 11:
4.73 – 5.01 Mb

n/a

PubMed search

[1]

n/a

Matrix metalloproteinase-26 also known as matrilysin-2 and endometase is an enzyme that in humans is encoded by the MMP26 gene.^[1]^[2]^[3]

Function

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. The encoded protein degrades type IV collagen, fibronectin, fibrinogen, casein, vitronectin, alpha 1-antitrypsin (A1AT), alpha 2-macroglobulin (A2M), and insulin-like growth factor-binding protein 1 (IGFBP), and activates MMP9 by cleavage. The protein differs from most MMP family members in that it lacks a conserved C-terminal protein domain.^[3]

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References

^ Park HI, Ni J, Gerkema FE, Liu D, Belozerov VE, Sang QX (Aug 2000). "Identification and characterization of human endometase (Matrix metalloproteinase-26) from endometrial tumor". J Biol Chem 275 (27): 20540–4. doi:10.1074/jbc.M002349200. PMID 10801841.
^ de Coignac AB, Elson G, Delneste Y, Magistrelli G, Jeannin P, Aubry JP, Berthier O, Schmitt D, Bonnefoy JY, Gauchat JF (Jul 2000). "Cloning of MMP-26. A novel matrilysin-like proteinase". Eur J Biochem 267 (11): 3323–9. doi:10.1046/j.1432-1327.2000.01363.x. PMID 10824119.
^ ^a ^b "Entrez Gene: MMP26 matrix metallopeptidase 26".

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Uría JA, López-Otín C (2000). "Matrilysin-2, a new matrix metalloproteinase expressed in human tumors and showing the minimal domain organization required for secretion, latency, and activity". Cancer Res. 60 (17): 4745–51. PMID 10987280.
Marchenko GN, Ratnikov BI, Rozanov DV, et al. (2001). "Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial origin". Biochem. J. 356 (Pt 3): 705–18. doi:10.1042/0264-6021:3560705. PMC 1221897. PMID 11389678.
Gearing AJ, Thorpe SJ, Miller K, et al. (2002). "Selective cleavage of human IgG by the matrix metalloproteinases, matrilysin and stromelysin". Immunol. Lett. 81 (1): 41–8. doi:10.1016/S0165-2478(01)00333-9. PMID 11841844.
Marchenko ND, Marchenko GN, Strongin AY (2002). "Unconventional activation mechanisms of MMP-26, a human matrix metalloproteinase with a unique PHCGXXD cysteine-switch motif". J. Biol. Chem. 277 (21): 18967–72. doi:10.1074/jbc.M201197200. PMID 11889136.
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Park HI, Turk BE, Gerkema FE, et al. (2002). "Peptide substrate specificities and protein cleavage sites of human endometase/matrilysin-2/matrix metalloproteinase-26". J. Biol. Chem. 277 (38): 35168–75. doi:10.1074/jbc.M205071200. PMID 12119297.
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Park HI, Jin Y, Hurst DR, et al. (2004). "The intermediate S1' pocket of the endometase/matrilysin-2 active site revealed by enzyme inhibition kinetic studies, protein sequence analyses, and homology modeling". J. Biol. Chem. 278 (51): 51646–53. doi:10.1074/jbc.M310109200. PMID 14532275.
Zhao YG, Xiao AZ, Park HI, et al. (2004). "Endometase/matrilysin-2 in human breast ductal carcinoma in situ and its inhibition by tissue inhibitors of metalloproteinases-2 and -4: a putative role in the initiation of breast cancer invasion". Cancer Res. 64 (2): 590–8. doi:10.1158/0008-5472.CAN-03-1932. PMID 14744773.
Pilka R, Domanski H, Hansson S, et al. (2005). "Endometrial TIMP-4 mRNA is high at midcycle and in hyperplasia, but down-regulated in malignant tumours. Coordinated expression with MMP-26". Mol. Hum. Reprod. 10 (9): 641–50. doi:10.1093/molehr/gah092. PMID 15273280.
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