Dataset Information

Expression of ?-subunit of ?-glucosidase II in adult mouse brain regions and selected organs.

ABSTRACT: ?-Glucosidase II (GII), a resident of endoplasmic reticulum (ER) and an important enzyme in the folding of nascent glycoproteins, is heterodimeric, consisting of ? (GII?) and ? (GII?) subunits. The catalytic GII? subunit, with the help of mannose 6-phosphate receptor homology domain of GII?, sequentially hydrolyzes two ?1-3-linked glucose residues in the second step of N-linked oligosaccharide-mediated protein folding. The soluble GII? subunit is retained in the ER through its interaction with the HDEL-containing GII? subunit. N-glycosylation and correct protein folding are crucial for protein stability and trafficking and cell surface expression of several proteins in the brain. Alterations in N-glycosylation lead to abnormalities in neuronal migration and mental retardation, various neurodegenerative diseases, and invasion of malignant gliomas. Inhibitors of GII are used to inhibit cell proliferation and migration in a variety of different pathologies, such as viral infection, cancer, and diabetes. Despite the widespread use of GII? inhibitory drugs and the role of GII? in brain function, little is known about its expression in brain and other tissues. Here, we report generation of a highly specific chicken antibody to the GII? subunit and its characterization by Western blotting and immunoprecipitation using cerebral cortical extracts. By using this antibody, we showed that the GII? protein is highly expressed in testis, kidney, and lung, with the lowest amount in heart. GII? polypeptide levels in whole brain were comparable to those in spleen. However, a higher expression of GII? protein was detected in the cerebral cortex, reflecting its continuous requirement in correct folding of cell surface proteins.

SUBMITTER: Anji A

PROVIDER: S-EPMC4237662 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature

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Expression of α-subunit of α-glucosidase II in adult mouse brain regions and selected organs.

Anji Antje A Miller Hayley H Raman Chandrasekar C Phillips Mathew M Ciment Gary G Kumari Meena M

Journal of neuroscience research 20140818 1

α-Glucosidase II (GII), a resident of endoplasmic reticulum (ER) and an important enzyme in the folding of nascent glycoproteins, is heterodimeric, consisting of α (GIIα) and β (GIIβ) subunits. The catalytic GIIα subunit, with the help of mannose 6-phosphate receptor homology domain of GIIβ, sequentially hydrolyzes two α1-3-linked glucose residues in the second step of N-linked oligosaccharide-mediated protein folding. The soluble GIIα subunit is retained in the ER through its interaction with t ...[more]

PMID: 25131991

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Project description:BackgroundUrothelial carcinoma (UC) is among the most prevalent malignancies. The muscle-invasive bladder cancer (MIBC) shows an invasive feature and has poor prognosis, while the non-muscle invasive bladder cancer (NMIBC) shows a better prognosis as compared with the MIBC. However, a significant proportion (10%-30%) of NMIBC cases progress to MIBC. Identification of efficient biomarkers for the prediction of the course of UC remains challenging nowadays. Recently, there is an emerging study showed that post-translational modifications (PTMs) by glycosylation is an important process correlated with tumor angiogenesis, invasion and metastasis. Herein, we reported a data-driven discovery and experimental validation of GANAB, a key regulator of glycosylation, as a novel prognostic marker in UC.MethodsIn the present study, we conducted immunohistochemistry (IHC) assay to evaluate the correlation between the expression levels of GANAB protein and the prognosis of UC in our cohort of 107 samples using whole slide image (WSI) analysis. In vitro experiments using RNAi were also conducted to investigate the biological functions of GANAB in UC cell lines.ResultsWe observed that positive GANAB protein expression was significantly correlated with poor prognosis of UC in our cohort, with p-value of 0.0017 in Log-rank test. Notably, tumor cells at the invasive front of the tumor margin showed stronger GANAB expression than the tumor cells inside the tumor body in UCs. We further validated that the elevated expression levels of GANAB were significantly correlated with high grade tumors (p-values of 1.72 × 10-10), advanced stages (6.47 × 10-6), and elevated in luminal molecular subtypes. Moreover, knocking-down GANAB using RNAi in UM-UC-3 and T24 cells inhibited cell proliferation and migration in vitro. Knockdown of GANAB resulted in cell cycle arrest at G1 phase. We demonstrated that GANAB mediated HIF1A and ATF6 transcriptional activation in the ER stress signaling, and regulated the gene expression of cell cycle-related transcriptional factors E2F7 and FOXM1.ConclusionsThe elevated expression of GANAB is a novel indicator of poorer prognosis of UC. Our data suggests that GANAB is not only a new and promising prognostic biomarker for UC, but also may provide important cues for the development of PTM-based therapeutics for UC treatment.

Dataset Information

Expression of ?-subunit of ?-glucosidase II in adult mouse brain regions and selected organs.

Publications

Expression of α-subunit of α-glucosidase II in adult mouse brain regions and selected organs.

Similar Datasets

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