MMP24

MMP24
Identifiers
Aliases	MMP24 , MMP-24, MMP25, MT-MMP 5, MT-MMP5, MT5-MMP, MT5MMP, MTMMP5, matrix metallopeptidase 24
External IDs	OMIM: 604871 MGI: 1341867 HomoloGene: 21331 GeneCards: MMP24
Gene location (Human)
Chr.	Chromosome 20 (human) [1]
End	35,276,998 bp [1]
Gene location (Mouse)
Chr.	Chromosome 2 (mouse) [2]
End	155,818,366 bp [2]
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• zinc ion binding ; • cadherin binding ; • metal ion binding ; • peptidase activity ; • enzyme activator activity ; • metalloendopeptidase activity ; • hydrolase activity ; • metallopeptidase activity ;
Cellular component	• integral component of membrane ; • Golgi apparatus ; • trans-Golgi network membrane ; • membrane ; • extracellular matrix ; • proteinaceous extracellular matrix ; • cell membrane ; • integral component of plasma membrane ; • extracellular region ; • extracellular exosome ; • extracellular ;
Biological process	• glial cell differentiation ; • proteolysis ; • detection of temperature stimulus involved in sensory perception of pain ; • neuronal stem cell population maintenance ; • cell-cell adhesion mediated by cadherin ; • cell adhesion ; • positive regulation of catalytic activity ; • cell-cell adhesion via plasma-membrane adhesion molecules ; • extracellular matrix organization ; • collagen catabolic process ;
	Sources:Amigo / QuickGO
Orthologs
	10893
	17391
	ENSG00000125966
	ENSMUSG00000027612
	Q9Y5R2
	Q9R0S2
	NM_006690
	NM_010808
	NP_006681
	NP_034938
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated April 16, 2020

Matrix metalloproteinase-24 is an enzyme that in humans is encoded by the MMP24 gene.^[5]^[6]

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. However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. This protein activates MMP2 by cleavage. The gene has previously been referred to as MMP25 but has been renamed MMP24.^[6]

Related Research Articles

Matrix metallopeptidase 9 (MMP-9), also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B (GELB), is a matrixin, a class of enzymes that belong to the zinc-metalloproteinases family involved in the degradation of the extracellular matrix. In humans the MMP9 gene encodes for a signal peptide, a propeptide, a catalytic domain with inserted three repeats of fibronectin type II domain followed by a C-terminal hemopexin-like domain.

72 kDa type IV collagenase also known as matrix metalloproteinase-2 (MMP-2) and gelatinase A is an enzyme that in humans is encoded by the MMP2 gene. The MMP2 gene is located on chromosome 16 at position 12.2.

Matrix metalloproteinase-14 is an enzyme that in humans is encoded by the MMP14 gene.

Tissue inhibitor of metalloproteinases 2 (TIMP2) is a gene and a corresponding protein. The gene is a member of the TIMP gene family. The protein is thought to be a metastasis suppressor.

Matrilysin also known as matrix metalloproteinase-7 (MMP-7), pump-1 protease (PUMP-1), or uterine metalloproteinase is an enzyme in humans that is encoded by the MMP7 gene. The enzyme has also been known as matrin, putative metalloproteinase-1, matrix metalloproteinase pump 1, PUMP-1 proteinase, PUMP, metalloproteinase pump-1, putative metalloproteinase, MMP).

Stromelysin-2 also known as matrix metalloproteinase-10 (MMP-10) or transin-2 is an enzyme that in humans is encoded by the MMP10 gene.

Collagenase 3 is an enzyme that in humans is encoded by the MMP13 gene. It is a member of the matrix metalloproteinase (MMP) family. Like most MMPs, it is secreted as an inactive pro-form. It is activated once the pro-domain is cleaved, leaving an active enzyme composed of the catalytic domain and the hemopexin-like domain PDB: 1PEX. Although the actual mechanism has not been described, the hemopexin domain participates in collagen degradation, the catalytic domain alone being particularly inefficient in collagen degradation. During embryonic development, MMP13 is expressed in the skeleton as required for restructuring the collagen matrix for bone mineralization. In pathological situations it is highly overexpressed; this occurs in human carcinomas, rheumatoid arthritis and osteoarthritis.

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.

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

Matrix metalloproteinase-19 (MMP-19) also known as matrix metalloproteinase RASI is an enzyme that in humans is encoded by the MMP19 gene.

Stromelysin-3 (SL-3) also known as matrix metalloproteinase-11 (MMP-11) is an enzyme that in humans is encoded by the MMP11 gene.

Matrix metalloproteinase-16 is an enzyme that in humans is encoded by the MMP16 gene.

Reversion-inducing-cysteine-rich protein with kazal motifs, also known as RECK, is a human gene, thought to be a metastasis suppressor.

Matrix metalloproteinase-17 (MMP-17) also known as membrane-type matrix metalloproteinase 4 is an enzyme that in humans is encoded by the MMP17 gene.

Matrix metalloproteinase-25 is an enzyme that in humans is encoded by the MMP25 gene.

Matrix metalloproteinase-23 is an enzyme that in humans is encoded by the MMP23B gene.

Matrix metalloproteinase-20 (MMP-20) also known as enamel metalloproteinase or enamelysin is an enzyme that in humans is encoded by the MMP20 gene.

Neutrophil collagenase, also known as matrix metalloproteinase-8 (MMP-8) or PMNL collagenase (MNL-CL), is a collagen cleaving enzyme which is present in the connective tissue of most mammals. In humans, the MMP-8 protein is encoded by the MMP8 gene. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is stored in secondary granules within neutrophils and is activated by autolytic cleavage.

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

Matrix metalloproteinase 15 also known as MMP15 is an enzyme that in humans is encoded by the MMP15 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000125966 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027612 - 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.
↑ Llano E, Pendas AM, Freije JP, Nakano A, Knauper V, Murphy G, Lopez-Otin C (Jun 1999). "Identification and characterization of human MT5-MMP, a new membrane-bound activator of progelatinase a overexpressed in brain tumors". Cancer Res. 59 (11): 2570–6. PMID 10363975.
1 2 "Entrez Gene: MMP24 matrix metallopeptidase 24 (membrane-inserted)".

Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. doi: 10.1074/jbc.274.31.21491 . PMID 10419448.
Kinoh H, Hayashita H, Kajita M, et al. (2000). "Assignment of the genes for membrane-type-4 matrix metalloproteinase (Mmp17, MMP17) to mouse chromosome 5, human chromosome band 12q24.3 and membrane-type-5 matrix metalloproteinase (Mmp24, MMP24) to mouse chromosome 2 and human chromosome band 20q11.2→q12, respectively, by radiation hybrid and in situ hybridization". Cytogenet. Cell Genet. 87 (1–2): 97–8. doi:10.1159/000015402. PMID 10640822.
Romanic AM, Burns-Kurtis CL, Ao Z, et al. (2001). "Upregulated expression of human membrane type-5 matrix metalloproteinase in kidneys from diabetic patients". Am. J. Physiol. Renal Physiol. 281 (2): F309–17. doi:10.1152/ajprenal.2001.281.2.F309. PMID 11457723.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. doi: 10.1038/414865a . PMID 11780052.
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. PMC 139241 . PMID 12477932.
Jung M, Römer A, Keyszer G, et al. (2003). "mRNA expression of the five membrane-type matrix metalloproteinases MT1-MT5 in human prostatic cell lines and their down-regulation in human malignant prostatic tissue". Prostate. 55 (2): 89–98. doi:10.1002/pros.10194. PMID 12661033.
Takino T, Koshikawa N, Miyamori H, et al. (2003). "Cleavage of metastasis suppressor gene product KiSS-1 protein/metastin by matrix metalloproteinases". Oncogene. 22 (30): 4617–26. doi:10.1038/sj.onc.1206542. hdl: 2297/2668 . PMID 12879005.
Wang P, Wang X, Pei D (2004). "Mint-3 regulates the retrieval of the internalized membrane-type matrix metalloproteinase, MT5-MMP, to the plasma membrane by binding to its carboxyl end motif EWV". J. Biol. Chem. 279 (19): 20461–70. doi: 10.1074/jbc.M400264200 . PMID 14990567.
Gaetje R, Holtrich U, Engels K, et al. (2008). "Expression of membrane-type 5 matrix metalloproteinase in human endometrium and endometriosis". Gynecol. Endocrinol. 23 (10): 567–73. doi:10.1080/09513590701556921. PMID 17952761.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000125966 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027612 - 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.

[pmid10363975-5] Llano E, Pendas AM, Freije JP, Nakano A, Knauper V, Murphy G, Lopez-Otin C (Jun 1999). "Identification and characterization of human MT5-MMP, a new membrane-bound activator of progelatinase a overexpressed in brain tumors". Cancer Res. 59 (11): 2570–6. PMID 10363975.

[entrez-6] 1 2 "Entrez Gene: MMP24 matrix metallopeptidase 24 (membrane-inserted)".

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

MMP24

Related Research Articles

References

Further reading