Stanford Home
Ovarian Kaleidoscope Database (OKdb)

Home

History

Transgenic Mouse Models

INFORGRAPHICS

Search
Submit
Update
Chroms
Browse
login /off

Hsueh lab

HPMR

Visits
since 01/2001:
176557

Glutathione S-transferase, Mu-5 OKDB#: 3072
 Symbols: GSTM5 Species: human
 Synonyms: GTM5, GSTM5-5,GLUTATHIONE S-TRANSFERASE M5|GLUTATHIONE S-TRANSFERASE, CLASS MU, 5  Locus: 1p13.3 in Homo sapiens


For retrieval of Nucleotide and Amino Acid sequences please go to: OMIM Entrez Gene
Mammalian Reproductive Genetics   Endometrium Database Resource   Orthologous Genes   UCSC Genome Browser   GEO Profiles new!   Amazonia (transcriptome data) new!

R-L INTERACTIONS   MGI

DNA Microarrays
SHOW DATA ...
link to BioGPS
General Comment

NCBI Summary: Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Diversification of these genes has occurred in regions encoding substrate-binding domains, as well as in tissue expression patterns, to accommodate an increasing number of foreign compounds.
General function Enzyme
Comment
Cellular localization Cytoplasmic
Comment
Ovarian function Early embryo development
Comment
Expression regulated by
Comment
Ovarian localization Oocyte
Comment Maternal housekeeping proteins translated during bovine oocyte maturation and early embryo development. Massicotte L et al. Protein synthesis from maternal mRNA is needed to sustain oocyte maturation and embryo development prior to the maternal-embryonic transition (MET). Therefore, proteins that are expressed throughout this time are important and may be considered as maternal housekeeping proteins (MHKP). Our objectives were first, identify the translated protein patterns of bovine embryo development and secondly, determine the MHKP. Proteins synthesized during oocyte maturation and embryo development (2, 4 and 8-cell stages) were labeled using [S(35)]-Met and [S(35)]-Cys, and visualized by 2-DE. Embryos were cultured with alpha-amanitine to inhibit new transcription. Only 46 proteins were present throughout all stages. Ten spots were identified by MALDI-TOF and MS/MS: HSC71; HSP70; CypA; UCH-L1; GSTM5; Cct5; E-FABP; 2,3-BPGM, ubiquitin-conjugating enzyme E2D3; and beta-actin/gamma-actin. A new method called in silico protein identification confirmation was developed using EST databases. This method is a promising approach for use in rare tissue or from species with an incomplete protein database. This study has revealed that the translated protein patterns show a transition that brings the embryo to the MET. The needs in translated proteins between oocyte maturation and embryo development are different. In summary, this study represents the bases for future proteomics studies on bovine oocytes and embryos.
Follicle stages
Comment
Phenotypes
Mutations 0 mutations
SNPs
D E M O
Links
OMIM (Online Mendelian Inheritance in Man: an excellent source of general gene description and genetic information.)
OMIM \ Animal Model
KEGG Pathways
Recent Publications
None
Search for Antibody
Discuss..
blog comments powered by Disqus
Related Genes
Beta
Show data ...


created: June 7, 2006, 2:33 p.m. by: hsueh   email:
home page:
last update: June 7, 2006, 2:34 p.m. by: hsueh    email:



Use the back button of your browser to return to the Gene List.

Click here to return to gene search form