High impact information on Ptges3

• The hsp90 Co-chaperone XAP2 alters importin beta recognition of the bipartite nuclear localization signal of the Ah receptor and represses transcriptional activity [1].
• These data provide the first evidence of nuclear import and export of a major Hsp70/Hsp90 co-chaperone and the regulation of this nuclear-cytoplasmic shuttling by cell cycle status and cell cycle kinases [2].
• The signal for mPGES-1 immunostaining became stronger at the morula stage and was strongly seen at the blastocyst stage. cPGES immunostaining was strongly observed in zygotes, 2-cell and 8-cell embryos [3].
• In urinary bladder, cPGES expression was restricted to the transitional epithelial cells [4].
• RNase protection assay revealed constitutive expression of cPGES was greatest in the testis with lower levels in the ovary, kidney, bladder and uterus [4].

Biological context of Ptges3

• The cPGES gene promoter is GC-rich and contains many SP1 sites but lacks an obvious TATA box motif [4].
• Analysis of a cPGES cDNA with partially sequenced cPGES genomic clones and bioinformatic databases demonstrates that the murine cPGES gene spans approximately 22 kb and consists of eight exons [4].

Anatomical context of Ptges3

• In the female reproductive tissues, cPGES was mainly localized in ovarian primary and secondary follicles and oviductal epithelial cells with less expression in uterine endometrium [4].

Analytical, diagnostic and therapeutic context of Ptges3

• Full-length mouse cPGES cDNA was cloned by reverse transcript-polymerase chain reaction (RT-PCR) and 5'- and 3'-rapid amplification of cDNA ends (RACE) [4].
• In situ hybridization studies demonstrated that cPGES mRNA was most highly expressed in the epithelial cells of seminiferous tubules in the testis [4].

References