ADAM2
Disintegrin and metalloproteinase domain-containing protein 2 is an enzyme that in humans is encoded by the ADAM2 gene.[3][4][5]
This gene encodes a member of the ADAM (a disintegrin and metalloprotease domain) 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 member is a subunit of an integral sperm membrane glycoprotein called fertilin, which plays an important role in sperm-egg interactions.[5]
References
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ Gupta SK, Alves K, Palladino LO, Mark GE, Hollis GF (August 1996). "Molecular cloning of the human fertilin beta subunit". Biochem Biophys Res Commun. 224 (2): 318–26. doi:10.1006/bbrc.1996.1027. PMID 8702389.
- ↑ Burkin HR, Burkin DJ, Davey PM, Griffin DK, Affara NA (June 1997). "Mapping, sequence, and expression analysis of the human fertilin beta gene (FTNB)". Genomics. 40 (1): 190–2. doi:10.1006/geno.1996.4531. PMID 9070941.
- 1 2 "Entrez Gene: ADAM2 ADAM metallopeptidase domain 2 (fertilin beta)".
Further reading
- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928
. PMID 15489334.
- 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.
- Eto K, Huet C, Tarui T, et al. (2002). "Functional classification of ADAMs based on a conserved motif for binding to integrin alpha 9beta 1: implications for sperm-egg binding and other cell interactions.". J. Biol. Chem. 277 (20): 17804–10. doi:10.1074/jbc.M200086200. PMID 11882657.
- Ikawa M, Nakanishi T, Yamada S, et al. (2002). "Calmegin is required for fertilin alpha/beta heterodimerization and sperm fertility.". Dev. Biol. 240 (1): 254–61. doi:10.1006/dbio.2001.0462. PMID 11784061.
- Cho C, Ge H, Branciforte D, et al. (2000). "Analysis of mouse fertilin in wild-type and fertilin beta(-/-) sperm: evidence for C-terminal modification, alpha/beta dimerization, and lack of essential role of fertilin alpha in sperm-egg fusion.". Dev. Biol. 222 (2): 289–95. doi:10.1006/dbio.2000.9703. PMID 10837118.
- Chen MS, Tung KS, Coonrod SA, et al. (1999). "Role of the integrin-associated protein CD9 in binding between sperm ADAM 2 and the egg integrin alpha6beta1: implications for murine fertilization.". Proc. Natl. Acad. Sci. U.S.A. 96 (21): 11830–5. doi:10.1073/pnas.96.21.11830. PMC 18372. PMID 10518536.
- Chen H, Sampson NS (1999). "Mediation of sperm-egg fusion: evidence that mouse egg alpha6beta1 integrin is the receptor for sperm fertilinbeta.". Chem. Biol. 6 (1): 1–10. doi:10.1016/S1074-5521(99)80015-5. PMID 9889149.
- Vidaeus CM, von Kapp-Herr C, Golden WL, et al. (1997). "Human fertilin beta: identification, characterization, and chromosomal mapping of an ADAM gene family member.". Mol. Reprod. Dev. 46 (3): 363–9. doi:10.1002/(SICI)1098-2795(199703)46:3<363::AID-MRD15>3.0.CO;2-#. PMID 9041139.
- Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
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