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ADAM12
Identifiers
Aliases	ADAM12, ADAM12-OT1, CAR10, MCMP, MCMPMltna, MLTN, MLTNA, ADAM metallopeptidase domain 12
External IDs	OMIM: 602714; MGI: 105378; HomoloGene: 74862; GeneCards: ADAM12; OMA:ADAM12 - orthologs
Gene location (Human)
Chr.	Chromosome 10 (human)
End	126,388,477 bp
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)
End	133,833,875 bp
RNA expression pattern
	Top expressed in
	placenta; ; stromal cell of endometrium; ; buccal mucosa cell; ; tibia; ; decidua; ; mucosa of paranasal sinus; ; cartilage tissue; ; gallbladder; ; testicle; ; tendon of biceps brachii;
	Top expressed in
	gastrula; ; calvaria; ; body of femur; ; mesothelium of peritoneum; ; umbilical cord; ; decidua; ; facial skeleton; ; efferent ductule; ; mandible; ; lesser wing of sphenoid bone;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	SH3 domain binding; peptidase activity; metalloendopeptidase activity; protein binding; hydrolase activity; metal ion binding; metallopeptidase activity;
Cellular component	integral component of membrane; extracellular region; membrane; nucleoplasm; plasma membrane;
Biological process	cell adhesion; myoblast fusion; proteolysis; extracellular matrix organization; positive regulation of angiogenesis;
	Sources:Amigo / QuickGO
Orthologs
	8038
	11489
	ENSG00000148848
	ENSMUSG00000054555
	O43184
	Q61824
	NM_021641; NM_001288973; NM_001288974; NM_001288975; NM_003474
	NM_007400
	NP_001275902; NP_001275903; NP_001275904; NP_003465; NP_067673
	NP_031426
	Wikidata
View/Edit Human	View/Edit Mouse

Disintegrin and metalloproteinase domain-containing protein 12 (previously Meltrin) is an enzyme that in humans is encoded by the ADAM12 gene.^[5]^[6] ADAM12 has two splice variants: ADAM12-L, the long form, has a transmembrane region and ADAM12-S, a shorter variant, is soluble and lacks the transmembrane and cytoplasmic domains.^[7]

Function

This gene encodes a member of the ADAM (a disintegrin and metalloprotease) protein family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. This gene has two alternatively spliced transcripts: a shorter secreted form and a longer membrane-bound form. The shorter form is found to stimulate myogenesis.^[8]

Clinical Significance

ADAM 12, a metalloprotease that binds insulin growth factor binding protein-3 (IGFBP-3), appears to be an effective early Down syndrome marker. Decreased levels of ADAM 12 may be detected in cases of trisomy 21 as early as 8 to 10 weeks gestation. Maternal serum ADAM 12 and PAPP-A levels at 8 to 9 weeks gestation in combination with maternal age yielded a 91% detection rate for Down syndrome at a 5% false-positive rate. When nuchal translucency data from approximately 12 weeks gestation was added, this increased the detection rate to 97%.^[9]

ADAM12 has also been implicated in the development of pathology in various cancers, hypertension, liver fibrogenesis, and asthma.^[10] In asthma, ADAM12 is upregulated in lung epithelium in response to TNF-alpha.^[11]

In a study of about 1200 persons with extremely high intelligence (IQ about 170), variants of the gene were associated with high IQ compared with a general population.^[12]

Interactions

ADAM12 has been shown to interact with:

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000148848 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000054555 – 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.
^ Gilpin BJ, Loechel F, Mattei MG, Engvall E, Albrechtsen R, Wewer UM (Feb 1998). "A novel, secreted form of human ADAM 12 (meltrin alpha) provokes myogenesis in vivo". J. Biol. Chem. 273 (1): 157–66. doi:10.1074/jbc.273.1.157. PMID 9417060.
^ Kveiborg M, Albrechtsen R, Couchman JR, Wewer UM (Jun 2008). "Cellular roles of ADAM12 in health and disease". Int. J. Biochem. Cell Biol. 40 (9): 1685–702. doi:10.1016/j.biocel.2008.01.025. PMID 18342566.
^ Yagami-Hiromasa T, Sato T, Kurisaki T, Kamijo K, Nabeshima Y, Fujisawa-Sehara A (1995). "A metalloprotease-disintegrin participating in myoblast fusion". Nature. 377 (6550): 652–6. Bibcode:1995Natur.377..652Y. doi:10.1038/377652a0. PMID 7566181. S2CID 4348744.
^ "Entrez Gene: ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha)".
^ Danforth's Obstetrics and Gynecology, 10th Edition; Copyright ©2008 Lippincott Williams & Wilkins; Chapter 7: Prenatal Diagnosis, Page 113
^ Nyren-Erickson EK, Jones JM, Srivastava DK, Mallik S (2013). "A disintegrin and metalloproteinase-12 (ADAM12): function, roles in disease progression, and clinical implications". Biochim. Biophys. Acta. 1830 (10): 4445–55. doi:10.1016/j.bbagen.2013.05.011. PMC 3740046. PMID 23680494.
^ Estrella C, Rocks N, Paulissen G, Quesada-Calvo F, Noel A, Vilain E, Lassalle P, Tillie-Leblond I, Cataldo D, Gosset P (2009). "Role of a disintegrin and metalloprotease-12 in neutrophil recruitment induced by airway epithelium". Am. J. Respir. Cell Mol. Biol. 41 (4): 449–58. doi:10.1165/rcmb.2008-0124OC. hdl:2268/5767. PMID 19213876.
^ Dzirasa K (2017-08-02). "A brilliant approach to study the basis of intelligence?". Science Translational Medicine. 9 (401). doi:10.1126/scitranslmed.aao0978. ISSN 1946-6234. S2CID 44125138.
^ Galliano MF, Huet C, Frygelius J, Polgren A, Wewer UM, Engvall E (May 2000). "Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha -actinin-2, is required for myoblast fusion". J. Biol. Chem. 275 (18): 13933–9. doi:10.1074/jbc.275.18.13933. PMID 10788519.
^ Shi Z, Xu W, Loechel F, Wewer UM, Murphy LJ (Jun 2000). "ADAM 12, a disintegrin metalloprotease, interacts with insulin-like growth factor-binding protein-3". J. Biol. Chem. 275 (24): 18574–80. doi:10.1074/jbc.M002172200. PMID 10849447.
^ Loechel F, Fox JW, Murphy G, Albrechtsen R, Wewer UM (Nov 2000). "ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3". Biochem. Biophys. Res. Commun. 278 (3): 511–5. doi:10.1006/bbrc.2000.3835. PMID 11095942.
^ Kang Q, Cao Y, Zolkiewska A (Jul 2001). "Direct interaction between the cytoplasmic tail of ADAM 12 and the Src homology 3 domain of p85alpha activates phosphatidylinositol 3-kinase in C2C12 cells". J. Biol. Chem. 276 (27): 24466–72. doi:10.1074/jbc.M101162200. PMID 11313349.

External links

The MEROPS online database for peptidases and their inhibitors: M12.212
ADAM12 on the Atlas of Genetics and Oncology
Human ADAM12 genome location and ADAM12 gene details page in the UCSC Genome Browser.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000148848 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000054555 – 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.

[pmid9417060-5] Gilpin BJ, Loechel F, Mattei MG, Engvall E, Albrechtsen R, Wewer UM (Feb 1998). "A novel, secreted form of human ADAM 12 (meltrin alpha) provokes myogenesis in vivo". J. Biol. Chem. 273 (1): 157–66. doi:10.1074/jbc.273.1.157. PMID 9417060.

[pmid18342566-6] Kveiborg M, Albrechtsen R, Couchman JR, Wewer UM (Jun 2008). "Cellular roles of ADAM12 in health and disease". Int. J. Biochem. Cell Biol. 40 (9): 1685–702. doi:10.1016/j.biocel.2008.01.025. PMID 18342566.

[7] Yagami-Hiromasa T, Sato T, Kurisaki T, Kamijo K, Nabeshima Y, Fujisawa-Sehara A (1995). "A metalloprotease-disintegrin participating in myoblast fusion". Nature. 377 (6550): 652–6. Bibcode:1995Natur.377..652Y. doi:10.1038/377652a0. PMID 7566181. S2CID 4348744.

[entrez-8] "Entrez Gene: ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha)".

[9] Danforth's Obstetrics and Gynecology, 10th Edition; Copyright ©2008 Lippincott Williams & Wilkins; Chapter 7: Prenatal Diagnosis, Page 113

[pmid23680494-10] Nyren-Erickson EK, Jones JM, Srivastava DK, Mallik S (2013). "A disintegrin and metalloproteinase-12 (ADAM12): function, roles in disease progression, and clinical implications". Biochim. Biophys. Acta. 1830 (10): 4445–55. doi:10.1016/j.bbagen.2013.05.011. PMC 3740046. PMID 23680494.

[11] Estrella C, Rocks N, Paulissen G, Quesada-Calvo F, Noel A, Vilain E, Lassalle P, Tillie-Leblond I, Cataldo D, Gosset P (2009). "Role of a disintegrin and metalloprotease-12 in neutrophil recruitment induced by airway epithelium". Am. J. Respir. Cell Mol. Biol. 41 (4): 449–58. doi:10.1165/rcmb.2008-0124OC. hdl:2268/5767. PMID 19213876.

[12] Dzirasa K (2017-08-02). "A brilliant approach to study the basis of intelligence?". Science Translational Medicine. 9 (401). doi:10.1126/scitranslmed.aao0978. ISSN 1946-6234. S2CID 44125138.

[pmid10788519-13] Galliano MF, Huet C, Frygelius J, Polgren A, Wewer UM, Engvall E (May 2000). "Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha -actinin-2, is required for myoblast fusion". J. Biol. Chem. 275 (18): 13933–9. doi:10.1074/jbc.275.18.13933. PMID 10788519.

[pmid10849447-14] Shi Z, Xu W, Loechel F, Wewer UM, Murphy LJ (Jun 2000). "ADAM 12, a disintegrin metalloprotease, interacts with insulin-like growth factor-binding protein-3". J. Biol. Chem. 275 (24): 18574–80. doi:10.1074/jbc.M002172200. PMID 10849447.

[pmid11095942-15] Loechel F, Fox JW, Murphy G, Albrechtsen R, Wewer UM (Nov 2000). "ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3". Biochem. Biophys. Res. Commun. 278 (3): 511–5. doi:10.1006/bbrc.2000.3835. PMID 11095942.

[pmid11313349-16] Kang Q, Cao Y, Zolkiewska A (Jul 2001). "Direct interaction between the cytoplasmic tail of ADAM 12 and the Src homology 3 domain of p85alpha activates phosphatidylinositol 3-kinase in C2C12 cells". J. Biol. Chem. 276 (27): 24466–72. doi:10.1074/jbc.M101162200. PMID 11313349.

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PROFILPELAJAR.COM

ADAM12

Function

Clinical Significance

Interactions

References

Further reading

External links

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