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ADAM metallopeptidase domain 2

ADAM2, PH-30, Ftnb, CT15
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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: metalloprotease, CAN, ACID, V1a, OUT
Papers using ADAM2 antibodies
Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method.
Ikezu Tsuneya, In PLoS ONE, 2000
... and MEF APPΔCT15 cells [34] have been described previously.Ganglioside (Axxora, Lörrach, Germany) exposure was ...
Papers on ADAM2
Spatial and temporal distributions of aerosol concentrations and depositions in Asia during the year 2010.
Joo et al., Seoul, South Korea. In Sci Total Environ, Feb 2016
Aerosol Modeling System (AMS) that is consisted of the Asian Dust Aerosol Model2 (ADAM2) and the Community Multi-scale Air Quality (CMAQ) modeling system has been employed to document the spatial distributions of the monthly and the annual averaged concentration of both the Asian dust (AD) aerosol and the anthropogenic aerosol (AA), and their total depositions in the Asian region for the year 2010.
The APP Intracellular Domain Is Required for Normal Synaptic Morphology, Synaptic Plasticity, and Hippocampus-Dependent Behavior.
Müller et al., Heidelberg, Germany. In J Neurosci, Jan 2016
Thus, the APP-CT15 domain provides essential physiological functions, likely via recruitment of specific interactors.
Male fertility and apoptosis in normal spermatogenesis are regulated by vacuolar-ATPase isoform a2.
Beaman et al., North Chicago, United States. In J Reprod Immunol, Nov 2015
We found that the expression of the sperm maturation-related molecules SPAM1, ADAM1, and ADAM2 was significantly decreased in testes from anti-a2V-treated males.
Reduced Fertility and Altered Epididymal and Sperm Integrity in Mice Lacking ADAM7.
Cho et al., Kwangju, South Korea. In Biol Reprod, Sep 2015
Western blot analyses revealed reduced levels of integral membrane protein 2B (ITM2B) and ADAM2 in sperm from Adam7-null mice, suggesting a requirement for ADAM7 in normal expression of sperm membrane proteins involved in sperm functions.
Novel sex-dependent differentially methylated regions are demethylated in adult male mouse livers.
Yagi et al., Tokyo, Japan. In Biochem Biophys Res Commun, Aug 2015
Similarly, Adam2, Uggt2, and Scp2 were hypomethylated in female embryonic germ (EG) cells and not in male EG cells, indicating that these S-DMRs are liver-specific male hypo-S-DMRs.
Lack of ADAM2, CALR3 and SAGE1 Cancer/Testis Antigen Expression in Lung and Breast Cancer.
Gjerstorff et al., Odense, Denmark. In Plos One, 2014
In this study, we investigated the expression of the cancer/testis antigens ADAM2, CALR3 and SAGE1 in lung and breast cancer, the two most frequent human cancers, with the purpose of providing novel therapeutic targets for these diseases.
Construction and Analysis of the Cell Surface's Protein Network for Human Sperm-Egg Interaction.
Shamsir et al., Johor Bahru, Malaysia. In Isrn Bioinform, 2012
The PPI network showed a highly interconnected network and identified a set of candidate proteins: ADAM-ZP3, ZP3-CLGN, IZUMO1-CD9, and ADAM2-IZUMO1 that may have an important role in sperm-egg interaction.
Testicular and epididymal ADAMs: expression and function during fertilization.
Cho, Kwangju, South Korea. In Nat Rev Urol, 2012
Some of these sperm ADAMs are assembled into potentially functional complexes, including ADAM1B-ADAM2, ADAM2-ADAM3-ADAM4, ADAM2-ADAM3-ADAM5, and ADAM2-ADAM3-ADAM6.
Mechanisms of fertilization--a view from the study of gene-manipulated mice.
Okabe et al., Suita, Japan. In J Androl, 2011
Unexpectedly, sperm from 5 different gene-disrupted mouse lines (calmegin (Clgn), Adam1a, Adam2, Adam3, and Ace) all have defective zona-binding ability and oviduct-migrating ability.
The mechanism of sperm-egg interaction and the involvement of IZUMO1 in fusion.
Okabe et al., Suita, Japan. In Asian J Androl, 2011
However, this is not likely, as there are already six different gene-disrupted mouse lines (Calmegin, Adam1a, Adam2, Adam3, Ace and Pgap1), all of which result in male sterility.
Impaired sperm aggregation in Adam2 and Adam3 null mice.
Cho et al., Kwangju, South Korea. In Fertil Steril, 2010
we report that Adam2 and Adam3 knockout sperm have severely impaired sperm aggregation and that this defect is not restored over time during in vitro cultivation.
ADAM2 interactions with mouse eggs and cell lines expressing α4/α9 (ITGA4/ITGA9) integrins: implications for integrin-based adhesion and fertilization.
Evans et al., Baltimore, United States. In Plos One, 2009
data indicate that ITGA9-ITGB7 functions as an ADAM binding partner in certain cellular contexts, with implications for mammalian fertilization and integrin function
[Molecular feactures of fertilization: gamete binding and fusion].
Coy et al., Murcia, Spain. In Rev Invest Clin, 2008
Among the molecules that participate on binding and fusion of gametes are included disintegrins on the sperm (ADAM1 and ADAM2) which interact with integrins (alpha6/beta-1, CD9, GPI-protein) in the egg plasma membrane, while cysteine-rich secretory proteins (CRISP) and the proteins named as Izumo participate in the fusion.
ADAM2 promotes migration of neuroblasts in the rostral migratory stream to the olfactory bulb.
Horwitz et al., Charlottesville, United States. In Eur J Neurosci, 2008
ADAM2 contributes to migration from the subventricular zone along the rostral migratory stream, possibly through cell-cell interactions that mediate the rapid migration of the neuroblasts to their endpoint.
Identification of an ADAM2-ADAM3 complex on the surface of mouse testicular germ cells and cauda epididymal sperm.
Primakoff et al., Davis, United States. In J Biol Chem, 2007
Results suggest that association with ADAM2 is a key element for stability of ADAM3 in epididymal sperm, and the presence of the ADAM2-ADAM3 complex in sperm also suggests a potential role of ADAM2 with ADAM3 in sperm binding to the egg zona pellucida.
Association between fertilin beta, protamines 1 and 2 and spermatid-specific linker histone H1-like protein mRNA levels, fertilization ability of human spermatozoa, and quality of preimplantation embryos.
Jedrzejczak et al., Poznań, Poland. In Folia Histochem Cytobiol, 2006
The fertilin beta contributes not only to successful fertilization, but may has an important impact in development of preimplantation embryos.
Sperm-egg interaction and gene manipulated animals.
Okabe et al., Suita, Japan. In Soc Reprod Fertil Suppl, 2006
It is intriguing that the disruption of a number of genes, e.g., Clgn, Ace, Adamla, Adam2 and Adam3 results in a similar sperm phenotype, i.e., failure of sperm to bind to the zona pellucida (ZP).
A metalloprotease-disintegrin participating in myoblast fusion.
Fujisawa-Sehara et al., Tokyo, Japan. In Nature, 1995
Here we report the identification of three new, myoblast-expressed gene products, meltrin-alpha, beta and gamma, with homology to both viper haemorrhagic factors and fertilin (PH-30), a membrane protein involved in egg-sperm fusion.
A novel metalloprotease/disintegrin-like gene at 17q21.3 is somatically rearranged in two primary breast cancers.
Nakamura et al., Tokyo, Japan. In Nat Genet, 1993
The gene (MDC) encodes a 524-amino acid metalloprotease-like, disintegrin-like and cysteine-rich protein with sequence similarity to members of the snake-venom metalloprotease/disintegrin family and guinea-pig sperm-surface protein PH-30.
A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion.
White et al., San Francisco, United States. In Nature, 1992
We have hypothesized that proteins mediating cell-cell fusion events resemble viral fusion proteins and have shown that PH-30, a sperm surface protein involved in sperm-egg fusion, shares biochemical characteristics with viral fusion proteins.
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