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MMP27

From Wikipedia, the free encyclopedia
MMP27
Identifiers
AliasesMMP27, MMP-27, matrix metallopeptidase 27
External IDsOMIM: 618101; MGI: 3039232; HomoloGene: 23345; GeneCards: MMP27; OMA:MMP27 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

64066

234911

Ensembl

ENSG00000137675

ENSMUSG00000070323

UniProt

Q9H306

n/a

RefSeq (mRNA)

NM_022122

NM_001030289
NM_001310717

RefSeq (protein)

NP_071405

n/a

Location (UCSC)Chr 11: 102.69 – 102.71 MbChr 9: 7.57 – 7.58 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Matrix metallopeptidase 27 also known as MMP-27 is an enzyme which in humans is encoded by the MMP27 gene.[5]

Structure

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MMP-27 was discovered and cloned in 1998 by Yang and Kurkinen.[6] Initially compared to the so-called Chicken MMP (CMMP), MMP-27 actually shows very little sequence homology with this protease. Sequence homology predicts that the human MMP-27 gene encodes the canonical domains shared by most MMPs (annotation based on Uniprot entry Q9H306): (i) a signal peptide (residues 1-17), (ii) a propeptide (18-98) containing the cysteine switch motif (89-96), (iii) a catalytic domain (99-263) containing the typical HEXXHXXGXXH motif of the metzincins (M10 and M12 families of the MEROPS[2] database), (iv) a proline-rich hinge region (264-278) and (v) a hemopexin-like domain (279-465) folded as a four-bladed β-propeller through disulfide bond formation between the two flanking Cys residues (Cys279 and Cys465). MMP-27 could be classified in the stromelysin group of MMPs, since MMP-27 shows 51,6% homology with stromelysin-2 (MMP-10) and localizes in the cluster of MMPs located on chromosome 11.

Like the six known MT-MMPs, human MMP-27 is prolonged by an additional C-terminal domain (466-513). The Spoctopus algorithm for topological prediction[7] suggests that this C-terminal extension (CTE) includes a potential transmembrane domain (490-510). However, this sequence is less hydrophobic than in transmembrane MT-MMPs (MMP-14, -15, -16 and -24) as it contains hydrophilic/charged residues, in particular His492, Lys493, His504 and Lys507.

Function

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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 MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases.[8]

Cominelli A. and colleagues demonstrated that MMP-27 is an unusual protease which is not secreted and is efficiently retained in the endoplasmic reticulum in three mammalian cell lines.[9] Deletion mutants and swapping with recombinant MMP-10 demonstrate that the unique MMP-27 C-terminal extension (CTE) is necessary and sufficient for endoplasmic reticulum retention but does not provide a stable membrane anchorage. Despite sequence homology with MT-MMPs, the CTE is not a transmembrane domain and does not interact permanently with membrane. This unique feature for an MMP raises important questions about potential functions of MMP-27, which remains to be investigated.

Clinical significance

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Sparse information about MMP-27 expression was found in studies of gene expression profiling (micro-array) or in expression pattern analysis of MMP family members during developmental, physiological or pathological processes. MMP-27 transcript is detected in almost every tissue, except the brain, with the highest expression found in the liver during mouse development[10] In the adult, MMP-27 mRNA is mostly abundant in anti-IgG/IgM stimulated B lymphocytes,[11] bone and kidney but is present at lower levels in the heart.[12]

A recent investigation of the transcriptome from distinct tissue compartments of the menstrual endometrium disclosed specific MMP-27 overexpression in areas of stromal breakdown.[13] In another transcriptomic study, MMP-27 was found to be increased in the human endometrium at the end of the secretory phase, before menstruation.[14] Moreover, MMP-27 expression is down-regulated in macrophages when co-cultured with ovarian cancer cells[15] but up-regulated in cartilages from patients with osteoarthritis[16] or in abdominal aortic aneurysms.[17] MMP-27 was also identified, at the protein level, in MDA-MB-231 breast cancer cell line[18] and in primary human breast cancer.[19] Recently, MMP-27 has been demonstrated to be expressed by CD163+/CD206+ macrophages in the human endometrium and in superficial endometriotic lesions.[20]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000137675 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000070323 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Nagase H, Woessner JF (July 1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. doi:10.1074/jbc.274.31.21491. PMID 10419448.
  6. ^ Yang M, Kurkinen M (1998). "Cloning and characterization of a novel matrix metalloproteinase (MMP), CMMP, from chicken embryo fibroblasts. CMMP, Xenopus XMMP, and human MMP19 have a conserved unique cysteine in the catalytic domain". J. Biol. Chem. 273 (28): 17893–900. doi:10.1074/jbc.273.28.17893. PMID 9651395.
  7. ^ Viklund H, Bernsel A, Skwark M, Elofsson A (2008). "SPOCTOPUS: a combined predictor of signal peptides and membrane protein topology". Bioinformatics. 24 (24): 2928–9. doi:10.1093/bioinformatics/btn550. PMID 18945683.
  8. ^ "Entrez Gene: MMP27".
  9. ^ Cominelli A, Halbout M, N'Kuli F, Lemoine P, Courtoy PJ, Marbaix E, Tyteca D, Henriet P (2014). "A unique C-terminal domain allows retention of matrix metalloproteinase-27 in the endoplasmic reticulum". Traffic. 15 (4): 401–17. doi:10.1111/tra.12149. PMID 24548619. S2CID 38579214.
  10. ^ Nuttall RK, Sampieri CL, Pennington CJ, Gill SE, Schultz GA, Edwards DR (2004). "Expression analysis of the entire MMP and TIMP gene families during mouse tissue development". FEBS Lett. 563 (1–3): 129–34. Bibcode:2004FEBSL.563..129N. doi:10.1016/S0014-5793(04)00281-9. PMID 15063736. S2CID 41113107.
  11. ^ Bar-Or A, Nuttall RK, Duddy M, Alter A, Kim HJ, Ifergan I, Pennington CJ, Bourgoin P, Edwards DR, Yong VW (2003). "Analyses of all matrix metalloproteinase members in leukocytes emphasize monocytes as major inflammatory mediators in multiple sclerosis". Brain. 126 (Pt 12): 2738–49. doi:10.1093/brain/awg285. PMID 14506071.
  12. ^ Bernal F, Hartung HP, Kieseier BC (2005). "Tissue mRNA expression in rat of newly described matrix metalloproteinases". Biol. Res. 38 (2–3): 267–71. doi:10.4067/S0716-97602005000200016. PMID 16238105.
  13. ^ Gaide Chevronnay HP, Galant C, Lemoine P, Courtoy PJ, Marbaix E, Henriet P (2009). "Spatiotemporal coupling of focal extracellular matrix degradation and reconstruction in the menstrual human endometrium". Endocrinology. 150 (11): 5094–105. doi:10.1210/en.2009-0750. PMID 19819954.
  14. ^ Talbi S, Hamilton AE, Vo KC, Tulac S, Overgaard MT, Dosiou C, Le Shay N, Nezhat CN, Kempson R, Lessey BA, Nayak NR, Giudice LC (2006). "Molecular phenotyping of human endometrium distinguishes menstrual cycle phases and underlying biological processes in normo-ovulatory women". Endocrinology. 147 (3): 1097–121. doi:10.1210/en.2005-1076. PMID 16306079.
  15. ^ Hagemann T, Wilson J, Burke F, Kulbe H, Li NF, Plüddemann A, Charles K, Gordon S, Balkwill FR (2006). "Ovarian cancer cells polarize macrophages toward a tumor-associated phenotype". J. Immunol. 176 (8): 5023–32. doi:10.4049/jimmunol.176.8.5023. PMID 16585599.
  16. ^ Kevorkian L, Young DA, Darrah C, Donell ST, Shepstone L, Porter S, Brockbank SM, Edwards DR, Parker AE, Clark IM (2004). "Expression profiling of metalloproteinases and their inhibitors in cartilage". Arthritis Rheum. 50 (1): 131–41. doi:10.1002/art.11433. PMID 14730609.
  17. ^ Lamblin N, Ratajczak P, Hot D, Dubois E, Chwastyniak M, Beseme O, Drobecq H, Lemoine Y, Koussa M, Amouyel P, Pinet F (2010). "Profile of macrophages in human abdominal aortic aneurysms: a transcriptomic, proteomic, and antibody protein array study". J. Proteome Res. 9 (7): 3720–9. doi:10.1021/pr100250s. PMID 20513153.
  18. ^ Hegedüs L, Cho H, Xie X, Eliceiri GL (2008). "Additional MDA-MB-231 breast cancer cell matrix metalloproteinases promote invasiveness". J. Cell. Physiol. 216 (2): 480–5. doi:10.1002/jcp.21417. PMID 18286480. S2CID 10734191.
  19. ^ Köhrmann A, Kammerer U, Kapp M, Dietl J, Anacker J (2009). "Expression of matrix metalloproteinases (MMPs) in primary human breast cancer and breast cancer cell lines: New findings and review of the literature". BMC Cancer. 9: 188. doi:10.1186/1471-2407-9-188. PMC 2706257. PMID 19531263.
  20. ^ Cominelli A, Gaide Chevronnay HP, Lemoine P, Courtoy PJ, Marbaix E, Henriet P (2014). "Matrix metalloproteinase-27 is expressed in CD163+/CD206+ M2 macrophages in the cycling human endometrium and in superficial endometriotic lesions". Mol. Hum. Reprod. 20 (8): 767–75. doi:10.1093/molehr/gau034. PMID 24810263.
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  • The MEROPS online database for peptidases and their inhibitors: M10.027

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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