MMP10

MMP10
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1Q3A, 3V96, 4ILW
Identifiers
Aliases	MMP10 , SL-2, STMY2, matrix metallopeptidase 10
External IDs	OMIM: 185260 MGI: 97007 HomoloGene: 20546 GeneCards: MMP10
EC number	3.4.24.22
Gene location (Human)
Chr.	Chromosome 11 (human)
End	102,780,628 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	7,510,241 bp
RNA expression pattern
	Top expressed in
	palpebral conjunctiva; ; islet of Langerhans; ; stromal cell of endometrium; ; pancreatic epithelial cell; ; Achilles tendon; ; appendix; ; amniotic fluid; ; periodontal fiber; ; bronchial epithelial cell; ; trachea;
	Top expressed in
	duodenum; ; jejunum; ; Paneth cell; ; ileum; ; colon; ; ovary; ; muscle of leg; ; uterus; ; integument; ; integument;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	zinc ion binding ; peptidase activity ; metalloendopeptidase activity ; hydrolase activity ; metallopeptidase activity ; metal ion binding ; serine-type endopeptidase activity ;
Cellular component	extracellular region ; extracellular space ; extracellular matrix ;
Biological process	collagen catabolic process ; extracellular matrix disassembly ; regulation of cell migration ; proteolysis ; response to hypoxia ; extracellular matrix organization ;
	Sources:Amigo / QuickGO
Orthologs
	4319
	17384
	ENSG00000166670
	ENSMUSG00000047562
	P09238
	O55123
	NM_002425
	NM_019471
	NP_002416
	NP_062344
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated August 19, 2023

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.^[5]^[6]

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 MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades proteoglycans and fibronectin. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.^[7]

Clinical significance

MMP10 has been linked to cancer stem cell vitality and metastasis.^[8]

MMP10 is a potential prognostic biomarker for oral cancer.^[9]^{[ unreliable medical source ]}

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.

Interstitial collagenase, also known as fibroblast collagenase, and matrix metalloproteinase-1(MMP-1) is an enzyme that in humans is encoded by the MMP1 gene. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. MMP-1 was the first vertebrate collagenase both purified to homogeneity as a protein, and cloned as a cDNA. MMP-1 has an estimated molecular mass of 54 kDa.

Stromelysin-1 also known as matrix metalloproteinase-3 (MMP-3) is an enzyme that in humans is encoded by the MMP3 gene. The MMP3 gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. MMP-3 has an estimated molecular weight of 54 kDa.

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). Human MMP-7 has a molecular weight around 30 kDa.

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. MMP-13 has an predicted molecular weight around 54 kDa. 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, MMP-13 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.

PITSLRE serine/threonine-protein kinase CDC2L2 is an enzyme that in humans is encoded by the CDC2L2 gene.

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

Thrombospondin-2 is a protein that in humans is encoded by the THBS2 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.

Metalloproteinase inhibitor 4 is an enzyme that in humans is encoded by the TIMP4 gene.

Transcription factor IIIA is a protein that in humans is encoded by the GTF3A gene. It was first isolated and characterized by Wolffe and Brown in 1988.

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

Matrix metalloproteinase 28 also known as epilysin is an enzyme that in humans is encoded by the MMP28 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 metalloproteinase-21 (MMP-21) is an enzyme that in humans is encoded by the MMP21 gene.

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

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000166670 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000047562 - 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.
↑ Muller D, Quantin B, Gesnel MC, Millon-Collard R, Abecassis J, Breathnach R (July 1988). "The collagenase gene family in humans consists of at least four members". The Biochemical Journal. 253 (1): 187–92. doi:10.1042/bj2530187. PMC 1149273 . PMID 2844164.
↑ Jung JY, Warter S, Rumpler Y (1990). "Localization of stromelysin 2 gene to the q22.3-23 region of chromosome 11 by in situ hybridization". Annales de Génétique. 33 (1): 21–3. PMID 2369069.
↑ "Entrez Gene: MMP10 matrix metallopeptidase 10 (stromelysin 2)".
↑ Justilien V, Regala RP, Tseng IC, Walsh MP, Batra J, Radisky ES, Murray NR, Fields AP (2012). "Matrix metalloproteinase-10 is required for lung cancer stem cell maintenance, tumor initiation and metastatic potential". PLOS ONE. 7 (4): e35040. Bibcode:2012PLoSO...735040J. doi: 10.1371/journal.pone.0035040 . PMC 3335833 . PMID 22545096.
↑ Upadhyay P, Gardi N, Desai S, Chandrani P, Joshi A, Dharavath B, Arora P, Bal M, Nair S, Dutt A (2017). "Genomic characterization of tobacco/nut chewing HPV-negative early stage tongue tumors identify MMP10 asa candidate to predict metastases". Oral Oncology. 73: 56–64. doi:10.1016/j.oraloncology.2017.08.003. PMC 5628952 . PMID 28939077.

External links

The MEROPS online database for peptidases and their inhibitors: M10.006
Overview of all the structural information available in the PDB for UniProt : P09238 (Stromelysin-2) at the PDBe-KB .

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000166670 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000047562 - 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.

[pmid2844164-5] Muller D, Quantin B, Gesnel MC, Millon-Collard R, Abecassis J, Breathnach R (July 1988). "The collagenase gene family in humans consists of at least four members". The Biochemical Journal. 253 (1): 187–92. doi:10.1042/bj2530187. PMC 1149273 . PMID 2844164.

[pmid2369069-6] Jung JY, Warter S, Rumpler Y (1990). "Localization of stromelysin 2 gene to the q22.3-23 region of chromosome 11 by in situ hybridization". Annales de Génétique. 33 (1): 21–3. PMID 2369069.

[entrez-7] "Entrez Gene: MMP10 matrix metallopeptidase 10 (stromelysin 2)".

[pmid22545096-8] Justilien V, Regala RP, Tseng IC, Walsh MP, Batra J, Radisky ES, Murray NR, Fields AP (2012). "Matrix metalloproteinase-10 is required for lung cancer stem cell maintenance, tumor initiation and metastatic potential". PLOS ONE. 7 (4): e35040. Bibcode:2012PLoSO...735040J. doi: 10.1371/journal.pone.0035040 . PMC 3335833 . PMID 22545096.

[pmid28939077-9] Upadhyay P, Gardi N, Desai S, Chandrani P, Joshi A, Dharavath B, Arora P, Bal M, Nair S, Dutt A (2017). "Genomic characterization of tobacco/nut chewing HPV-negative early stage tongue tumors identify MMP10 asa candidate to predict metastases". Oral Oncology. 73: 56–64. doi:10.1016/j.oraloncology.2017.08.003. PMC 5628952 . PMID 28939077.

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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 Coenzyme 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)