ADAM3
A disintegrin and metalloprotease 3, or ADAM3, belongs to a family of peptidase proteins referred to as ADAMs. Many of these are solely found in spermatogenic cells, specifically in the anterior portion of capacitated spermatozoa heads. This membrane protein is critical for crucial steps in fertilization such as migration of sperm through the uterus to the oviduct as well as binding to the zona pellucida. Inactivation of ADAM3 is a cause of male infertility. Numerous studies have detailed that in ADAM3 null mice, the spermatozoa fail to migrate through the utero-tubal junction. Furthermore, knockout of the closely related ADAM1a gene in mice, an estrogen receptor not found in mature spermatozoa, causes loss of surface ADAM3 and decreased zona pellucida binding. Other studies have shown ADAM3-/- mouse spermatozoa fail to show sperm-sperm aggregation, although the significance of this is still unknown. ADAM3 has not yet been found in humans.
A disintegrin and metalloprotease 3, or ADAM3, belongs to a family of peptidase proteins referred to as ADAMs. Many of these are solely found in spermatogenic cells, specifically in the anterior portion of capacitated spermatozoa heads. This membrane protein is critical for crucial steps in fertilization such as migration of sperm through the uterus to the oviduct as well as binding to the zona pellucida. Inactivation of ADAM3 is a cause of male infertility.[1]
Numerous studies have detailed that in ADAM3 null mice, the spermatozoa fail to migrate through the utero-tubal junction. Furthermore, knockout of the closely related ADAM1a gene in mice, an estrogen receptor not found in mature spermatozoa, causes loss of surface ADAM3 and decreased zona pellucida binding. Other studies have shown ADAM3-/- mouse spermatozoa fail to show sperm-sperm aggregation, although the significance of this is still unknown. ADAM3 has not yet been found in humans.
[2] [3] [4] [5] [6] [7] [8] [9] [10] [11]
References
[edit]- ^ "Adam3 MGI Mouse Gene Detail - MGI:102518 - a Disintegrin and Metallopeptidase Domain 3 (cyritestin)." Adam3 MGI Mouse Gene Detail - MGI:102518 - a Disintegrin and Metallopeptidase Domain 3 (cyritestin). N.p., n.d. Web. 04 Dec. 2016.
- ^ Wolfsberg, TG (1995). "ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain". Dev Biol. 169 (1): 378–383. doi:10.1006/dbio.1995.1152. PMID 7750654.
- ^ Cho, C (1998). "Fertilization defects in sperm from mice lacking fertilin beta". Science. 281 (5384): 1857–1859. doi:10.1126/science.281.5384.1857. PMID 9743500.
- ^ Yamaguchi, R (2009). "Disruption of ADAM3 impairs the migration of sperm into oviduct in mouse". Biol Reprod. 81 (1): 142–146. doi:10.1095/biolreprod.108.074021. PMID 19339711.
- ^ Fujihara, Y (2014). "GPI-anchored protein complex, LY6K/TEX101, is required for sperm migration into the oviduct and male fertility in mice". Biol Reprod. 90 (3): 60. doi:10.1095/biolreprod.113.112888. PMID 24501175.
- ^ Yamaguchi, R (2006). "Aberrant distribution of ADAM3 in sperm from both angiotensin-converting enzyme (Ace)- and calmegin (Clgn)-deficient mice". Biol Reprod. 75 (5): 760–766. doi:10.1095/biolreprod.106.052977. PMID 16870943.
- ^ Nishimura, H (2004). "Possible function of the ADAM1a/ADAM2 Fertilin complex in the appearance of ADAM3 on the sperm surface". J Biol Chem. 279 (33): 34957–34962. doi:10.1074/jbc.m314249200. PMID 15194697.
- ^ Ikawa, M (2001). "Calmegin is required for fertilin alpha/beta heterodimerization and sperm fertility". Dev Biol. 240 (1): 254–261. doi:10.1006/dbio.2001.0462. PMID 11784061.
- ^ Hagaman, JR (1998). "Angiotensin-converting enzyme and male fertility". Proc Natl Acad Sci USA. 95 (5): 2552–2557. Bibcode:1998PNAS...95.2552H. doi:10.1073/pnas.95.5.2552. PMC 19410. PMID 9482924.
- ^ Han, C (2010). "Impaired sperm aggregation in Adam2 and Adam3 null mice". Fertil. Steril. 93 (8): 2754–6. doi:10.1016/j.fertnstert.2010.03.013. PMID 20400072.
- ^ Grzmil, P (2001). "Human cyritestin genes (CRYN1 and CRYN2) are non-functional". Biochem J. 357 (Pt 2): 551–556. doi:10.1042/0264-6021:3570551. PMC 1221984. PMID 11439107.
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