Matrix metallopeptidase 12

MMP12
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1JIZ, 1JK3, 1OS2, 1OS9, 1RMZ, 1ROS, 1UTT, 1UTZ, 1Y93, 1YCM, 1Z3J, 2HU6, 2JXY, 2K2G, 2K9C, 2KRJ, 2MLR, 2MLS, 2OXU, 2OXW, 2OXZ, 2POJ, 2W0D, 2WO8, 2WO9, 2WOA, 2Z2D, 3BA0, 3EHX, 3EHY, 3F15, 3F16, 3F17, 3F18, 3F19, 3F1A, 3LIK, 3LIL, 3LIR, 3LJG, 3LK8, 3LKA, 3N2U, 3N2V, 3NX7, 3RTS, 3RTT, 3TS4, 3TSK, 3UVC, 4EFS, 4GQL, 4GR0, 4GR3, 4GR8, 4GUY, 4H30, 4H49, 4H76, 4H84, 4I03, 4IJO, 2N8R, 5I4O, 5I0L, 5I2Z, 5I3M, 5I43
Identifiers
Aliases	MMP12, HME, ME, MME, MMP-12, Matrix metallopeptidase 12
External IDs	OMIM: 601046; MGI: 97005; HomoloGene: 20547; GeneCards: MMP12; OMA:MMP12 - orthologs
Gene location (Human)
Chr.	Chromosome 11 (human)
End	102,874,982 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	7,369,499 bp
RNA expression pattern
	Top expressed in
	periodontal fiber; ; mucosa of ileum; ; mucosa of sigmoid colon; ; decidua; ; cartilage tissue; ; appendix; ; amniotic fluid; ; rectum; ; testicle; ; epithelium of nasopharynx;
	Top expressed in
	zygote; ; secondary oocyte; ; lactiferous gland; ; embryo; ; calvaria; ; embryo; ; blastocyst; ; primary oocyte; ; right kidney; ; adrenal gland;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	peptidase activity; endopeptidase activity; hydrolase activity; metallopeptidase activity; metal ion binding; serine-type endopeptidase activity; metalloendopeptidase activity; calcium ion binding; collagen binding; zinc ion binding; sequence-specific DNA binding;
Cellular component	extracellular matrix; extracellular region; extracellular space; nucleus; cytoplasm;
Biological process	collagen catabolic process; wound healing, spreading of epidermal cells; extracellular matrix disassembly; positive regulation of epithelial cell proliferation involved in wound healing; wound healing; negative regulation of transcription by RNA polymerase II; proteolysis; protein import into nucleus; positive regulation of gene expression; positive regulation of transcription by RNA polymerase II; regulation of defense response to virus by host; negative regulation of type I interferon-mediated signaling pathway; positive regulation of type I interferon-mediated signaling pathway; cellular response to virus; response to hypoxia; elastin catabolic process; negative regulation of endothelial cell-matrix adhesion via fibronectin; extracellular matrix organization; response to amyloid-beta;
	Sources:Amigo / QuickGO
Orthologs
	4321
	17381
	ENSG00000262406
	ENSMUSG00000049723
	P39900
	P34960
	NM_002426
	NM_008605; NM_001320076; NM_001320077
	NP_002417
	NP_001307005; NP_001307006; NP_032631
	Wikidata
View/Edit Human	View/Edit Mouse

Search
PMC	articles
PubMed	articles
NCBI	proteins

macrophage elastase
macrophage elastase
Identifiers
EC no.	3.4.24.65
CAS no.	146888-86-0
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

Matrix metalloproteinase-12 (MMP-12) also known as macrophage metalloelastase (MME) or macrophage elastase (ME) is an enzyme that in humans is encoded by the MMP12 gene.^[5]^[6]^[7]

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. The prodomain is cleaved by extracellular proteinases when the enzyme is activated. The active enzyme is constituted by two domains, the catalytic domain resposnsible for its enzymatic activity and the hemopexin-like domain that in some MMPs plays a role in substrate recognition and can contribute to increasing catalytic efficiency. 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. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.^[5]

Clinical significance

MMP12 may play a role in aneurysm formation^[8] and studies in mice and humans suggest a role in the development of emphysema.^[9]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000262406 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000049723 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b "Entrez Gene: MMP12 matrix metallopeptidase 12 (macrophage elastase)".
^ Shapiro SD, Kobayashi DK, Ley TJ (November 1993). "Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages". J. Biol. Chem. 268 (32): 23824–9. PMID 8226919.
^ Belaaouaj A, Shipley JM, Kobayashi DK, Zimonjic DB, Popescu N, Silverman GA, Shapiro SD (June 1995). "Human macrophage metalloelastase. Genomic organization, chromosomal location, gene linkage, and tissue-specific expression". J. Biol. Chem. 270 (24): 14568–75. doi:10.1074/jbc.270.24.14568. PMID 7782320.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ Curci JA, Liao S, Huffman MD, Shapiro SD, Thompson RW (December 1998). "Expression and localization of macrophage elastase (matrix metalloproteinase-12) in abdominal aortic aneurysms". J. Clin. Invest. 102 (11): 1900–10. doi:10.1172/JCI2182. PMC 509141. PMID 9835614.
^ Woodruff PG, Koth LL, Yang YH, Rodriguez MW, Favoreto S, Dolganov GM, Paquet AC, Erle DJ (December 2005). "A Distinctive Alveolar Macrophage Activation State Induced by Cigarette Smoking". Am. J. Respir. Crit. Care Med. 172 (11): 1383–92. doi:10.1164/rccm.200505-686OC. PMC 2718436. PMID 16166618.

External links

The MEROPS online database for peptidases and their inhibitors: M10.009

This article on a gene on human chromosome 11 is a stub. You can help Wikipedia by expanding it.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000262406 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000049723 – 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.

[entrez-5] "Entrez Gene: MMP12 matrix metallopeptidase 12 (macrophage elastase)".

[pmid8226919-6] Shapiro SD, Kobayashi DK, Ley TJ (November 1993). "Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages". J. Biol. Chem. 268 (32): 23824–9. PMID 8226919.

[pmid7782320-7] Belaaouaj A, Shipley JM, Kobayashi DK, Zimonjic DB, Popescu N, Silverman GA, Shapiro SD (June 1995). "Human macrophage metalloelastase. Genomic organization, chromosomal location, gene linkage, and tissue-specific expression". J. Biol. Chem. 270 (24): 14568–75. doi:10.1074/jbc.270.24.14568. PMID 7782320.{{cite journal}}: CS1 maint: unflagged free DOI (link)

[pmid9835614-8] Curci JA, Liao S, Huffman MD, Shapiro SD, Thompson RW (December 1998). "Expression and localization of macrophage elastase (matrix metalloproteinase-12) in abdominal aortic aneurysms". J. Clin. Invest. 102 (11): 1900–10. doi:10.1172/JCI2182. PMC 509141. PMID 9835614.

[pmid16166618-9] Woodruff PG, Koth LL, Yang YH, Rodriguez MW, Favoreto S, Dolganov GM, Paquet AC, Erle DJ (December 2005). "A Distinctive Alveolar Macrophage Activation State Induced by Cigarette Smoking". Am. J. Respir. Crit. Care Med. 172 (11): 1383–92. doi:10.1164/rccm.200505-686OC. PMC 2718436. PMID 16166618.

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v t e Proteases: metalloendopeptidases (EC 3.4.24)
ADAM proteins	Alpha secretases ADAM9 ADAM10 ADAM17 ADAM19 ADAM2 ADAM7 ADAM8 ADAM11 ADAM12 ADAM15 ADAM18 ADAM22 ADAM23 ADAM28 ADAM33 ADAMTS1 ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 ADAMTS8 ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13
Matrix metalloproteinases	Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28
Other	Neprilysin Procollagen peptidase Thermolysin Pregnancy-associated plasma protein A Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Function

Clinical significance

References

Further reading

External links