Ask about this productRelated genes to: HSPA5 antibody
- Gene:
- HSPA5 NIH gene
- Name:
- heat shock protein family A (Hsp70) member 5
- Previous symbol:
- GRP78
- Synonyms:
- BiP
- Chromosome:
- 9q33.3
- Locus Type:
- gene with protein product
- Date approved:
- 1991-07-26
- Date modifiied:
- 2015-11-19
- Gene:
- TMEM132A NIH gene
- Name:
- transmembrane protein 132A
- Previous symbol:
- HSPA5BP1
- Synonyms:
- GBP, FLJ20539
- Chromosome:
- 11q12.2
- Locus Type:
- gene with protein product
- Date approved:
- 2004-02-04
- Date modifiied:
- 2014-11-19
Related products to: HSPA5 antibody
Related articles to: HSPA5 antibody
- Transmembrane protein 132A (TMEM132A, KIAA1583) was first isolated as a novel gene that is enriched during the embryonic and postnatal stages of rat brain development and interacts with GRP78. However, the biological functions of TMEM132A are scarcely characterized because the protein does not contain any known structural domains. Using a cell-surface biotinylation assay and immunocytochemical staining, we found that TMEM132A is a transmembrane glycoprotein consisting of a large extracellular domain in the N-terminal region and a small cytosolic domain in the C-terminal region. Partial deletions of the intracellular domain of TMEM132A had little effect on its expression level and cell-surface localization in transfected HEK293 cells, whereas deletions of the extracellular domain hampered transport to the cell surface. The expression pattern of each N-terminal mutant was immunocytochemically confirmed in HeLa cells transfected with the same constructs. Treatment with tunicamycin, an inhibitor of protein glycosylation, led to the accumulation of the unglycosylated form of TMEM132A in inverse proportion to the glycosylated form; however, both forms were localized at the cell surface at almost equal rates. In contrast, GRP78 overexpression led to the accumulation of unglycosylated TMEM132A, which was not detected on the cell surface. Inhibition of ER-Golgi transport by treatment with brefeldin A or the overexpression of mutant Sar1 attenuated the amount of cell-surface localized TMEM132A in HEK293 cells. Treatment with reagents disrupting intracellular calcium rapidly down-regulated the amount of TMEM132A protein in Neuro2a cells without affecting the expression level of its mRNA. Taken together, our data show that the novel cell-surface localized glycoprotein, TMEM132A, is regulated by several factors, including GRP78, Sar1, and intracellular calcium, in a post-transcriptional manner. - Source: PubMed
Publication date: 2012/07/22
Oh-hashi KentaroKoga HisashiNagase TakahiroHirata YokoKiuchi Kazutoshi - Transmembrane protein 132A (TMEM132A) is a novel GRP78 binding protein that we recently discovered. However, the biological functions of TMEM132A are merely characterized because it does not encode any known structural domains. In this study, we down regulated intrinsic TMEM132A by RNA interference and identified a variety of genes that fluctuated during TMEM132A gene silencing using microarray analysis. TMEM132A-knockdown in Neuro2a cells caused neurite-like projection without any stimuli and enhanced the expression of ATF6 mRNA, an ER stress transducer, and GADD153 mRNA, a stress inducible gene. Under serum-deprived condition, TMEM132A-knockdown cells gradually retarded neurite-like projection and decreased cell viability. Moreover, TMEM132A knockdown markedly induced GADD153 expression due to serum starvation without affecting the level of cleaved caspase-3. Our data suggest that TMEM132A is an important factor of cell survival in regulating certain ER stress-related gene expression in neuronal cells. - Source: PubMed
Publication date: 2010/05/09
Oh-hashi KentaroImai KazuhideKoga HisashiHirata YokoKiuchi Kazutoshi - We previously reported that a novel GRP78-binding protein (GBP) is predominantly expressed in rat brain and its expression declines through the aging process. To characterize its biological function, we established C6 glioblastoma cells that stably overexpressed GBP. Stable overexpression of GBP attenuated cAMP-induced expression of the glial fibrillary acidic protein (GFAP) gene, which was accompanied by a decrease in cAMP-induced signal transducer and activators of transcription 3 (STAT3) phosphorylation. Other distinct cAMP-induced events, including a transient reduction in extracellular signal-regulated protein kinase phosphorylation and a slowdown in cell proliferation, were hardly affected by GBP overexpression. Most importantly, treatment with siRNA against endogenous GBP markedly downregulated GBP expression in C6 glioblastoma cells, and dramatically augmented cAMP-induced GFAP mRNA expression in parallel with hyper-phosphorylation of STAT3. These results suggest a novel function of GBP in regulating GFAP gene expression via STAT3 phosphorylation. - Source: PubMed
Publication date: 2006/06/21
Oh-hashi KentaroHirata YokoKoga HisashiKiuchi Kazutoshi - The full-length cDNA clone of a novel GRP78-binding protein (GBP) was isolated from rat brain using PCR-selected cDNA subtraction. GBP was predominantly expressed in neuronal cells among various brain tissues. GBP mRNA was already detected in the E12 brain and then gradually increased to reach a peak within P0-2 weeks after birth. GBP expression in the brain decreased age-dependently to approximately 30% of the postnatal level at 12 months. GBP encoded 1021 amino acids and was predicted to have two transmembrane regions and glutamic acid- and proline-rich regions. Because the sequence of GBP offered few clues to the possible function, we performed a GST-tagged GBP pull-down assay in PC12 lysates and identified GRP78, one of the heat shock proteins, as a counterpart. Observation of COS7 cells expressing green fluorescent protein- or Myc-tagged GBP showed that GBP was localized in the endoplasmic reticulum-Golgi domain where BODIPY 558/568 (4,4-difluro-5-(2-thienyl)-4-bora-3alpha,4alpha-diaza-S-indacene)-labeled brefeldin A accumulated. To investigate a biological role for GBP, we established Neuro2a cells stably expressing Myc-tagged GBP. Overexpression of GBP did not affect cell growth or morphological features but attenuated the time-dependent decrease in cell viability caused by serum deprivation compared with control cells. After 48 h of serum starvation, Neuro2a cells overexpressing GBP were resistant to the cell death induced by serum withdrawal. These results suggest that GBP would have a relevant functional role in embryonic and postnatal development of the brain. - Source: PubMed
Publication date: 2003/01/03
Oh-hashi KentaroNaruse YoshihisaAmaya FumimasaShimosato GoshunTanaka Masaki