Matrix metallopeptidase 12

From Wikipedia, the free encyclopedia

Matrix metallopeptidase 12 (macrophage elastase)

PDB rendering based on 1jiz.

Available structures: 1jiz, 1jk3, 1os2, 1os9, 1rmz, 1ros, 1utt, 1utz, 1y93, 1ycm, 1z3j, 2hu6, 2oxu, 2oxw, 2oxz

Identifiers

Symbol(s)

MMP12; MME; HME; MGC138506

External IDs

OMIM: 601046 MGI: 97005 HomoloGene: 20547

Gene ontology
Molecular Function:	• macrophage elastase activity • calcium ion binding • zinc ion binding
Cellular Component:	• proteinaceous extracellular matrix
Biological Process:	• peptidoglycan metabolic process • proteolysis • cell motility

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002426 (mRNA)
NP_002417 (protein)

NM_008605 (mRNA)
NP_032631 (protein)

Location

Chr 11: 102.24 - 102.25 Mb

Chr 9: 7.35 - 7.37 Mb

Pubmed search

[1]

[2]

Matrix metallopeptidase 12 (macrophage elastase), also known as MMP12, is a human gene.^[1]

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. It is thought that the protein encoded by this gene is cleaved at both ends to yield the active enzyme, but this processing has not been fully described. The enzyme degrades soluble and insoluble elastin. It may play a role in aneurysm formation and studies in mice suggest a role in the development of emphysema. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.^[1]

[edit] References

^ ^a ^b Entrez Gene: MMP12 matrix metallopeptidase 12 (macrophage elastase).

[edit] Further reading

Nagase H, Woessner JF (1999). "Matrix metalloproteinases.". J. Biol. Chem. 274 (31): 21491–4. PMID 10419448.
Belaaouaj A, Shipley JM, Kobayashi DK, et al. (1995). "Human macrophage metalloelastase. Genomic organization, chromosomal location, gene linkage, and tissue-specific expression.". J. Biol. Chem. 270 (24): 14568–75. PMID 7782320.
Shapiro SD, Kobayashi DK, Ley TJ (1993). "Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages.". J. Biol. Chem. 268 (32): 23824–9. PMID 8226919.
Pendás AM, Santamaría I, Alvarez MV, et al. (1997). "Fine physical mapping of the human matrix metalloproteinase genes clustered on chromosome 11q22.3.". Genomics 37 (2): 266–8. PMID 8921407.
Gronski TJ, Martin RL, Kobayashi DK, et al. (1997). "Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase.". J. Biol. Chem. 272 (18): 12189–94. PMID 9115292.
Edelstein C, Shapiro SD, Klezovitch O, Scanu AM (1999). "Macrophage metalloelastase, MMP-12, cleaves human apolipoprotein(a) in the linker region between kringles IV-4 and IV-5. Potential relevance to lipoprotein(a) biology.". J. Biol. Chem. 274 (15): 10019–23. PMID 10187779.
Dias Neto E, Correa RG, Verjovski-Almeida S, et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags.". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. PMID 10737800.
Wert SE, Yoshida M, LeVine AM, et al. (2000). "Increased metalloproteinase activity, oxidant production, and emphysema in surfactant protein D gene-inactivated mice.". Proc. Natl. Acad. Sci. U.S.A. 97 (11): 5972–7. doi:10.1073/pnas.100448997. PMID 10801980.
Belaaouaj AA, Li A, Wun TC, et al. (2000). "Matrix metalloproteinases cleave tissue factor pathway inhibitor. Effects on coagulation.". J. Biol. Chem. 275 (35): 27123–8. doi:10.1074/jbc.M004218200. PMID 10859319.
Hiller O, Lichte A, Oberpichler A, et al. (2000). "Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII.". J. Biol. Chem. 275 (42): 33008–13. doi:10.1074/jbc.M001836200. PMID 10930399.
Terp GE, Christensen IT, Jørgensen FS (2000). "Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes.". J. Biomol. Struct. Dyn. 17 (6): 933–46. PMID 10949161.
Agapova OA, Ricard CS, Salvador-Silva M, Hernandez MR (2001). "Expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in human optic nerve head astrocytes.". Glia 33 (3): 205–16. PMID 11241738.
Lang R, Kocourek A, Braun M, et al. (2001). "Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 A crystal structure.". J. Mol. Biol. 312 (4): 731–42. doi:10.1006/jmbi.2001.4954. PMID 11575928.
Nar H, Werle K, Bauer MM, et al. (2001). "Crystal structure of human macrophage elastase (MMP-12) in complex with a hydroxamic acid inhibitor.". J. Mol. Biol. 312 (4): 743–51. doi:10.1006/jmbi.2001.4953. PMID 11575929.
Joos L, He JQ, Shepherdson MB, et al. (2002). "The role of matrix metalloproteinase polymorphisms in the rate of decline in lung function.". Hum. Mol. Genet. 11 (5): 569–76. PMID 11875051.
Andolfo A, English WR, Resnati M, et al. (2003). "Metalloproteases cleave the urokinase-type plasminogen activator receptor in the D1-D2 linker region and expose epitopes not present in the intact soluble receptor.". Thromb. Haemost. 88 (2): 298–306. PMID 12195704.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Vos CM, van Haastert ES, de Groot CJ, et al. (2003). "Matrix metalloproteinase-12 is expressed in phagocytotic macrophages in active multiple sclerosis lesions.". J. Neuroimmunol. 138 (1-2): 106–14. PMID 12742660.
Anghelina M, Schmeisser A, Krishnan P, et al. (2003). "Migration of monocytes/macrophages in vitro and in vivo is accompanied by MMP12-dependent tunnel formation and by neovascularization.". Cold Spring Harb. Symp. Quant. Biol. 67: 209–15. PMID 12858542.