ArticleAnnals of translational medicine2021
N-glycosylation of somatostatin receptor type 2 protects rats from acute pancreatitis.
Article in Annals of translational medicine, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 5 citations in OpenAlex.
- PIGT promotes cell growth, glycolysis, and metastasis in bladder cancer by modulating GLUT1 glycosylation and membrane trafficking.Journal of translational medicine · 2024Article
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Authors and funding
5 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundThe growth hormone inhibitor somatostatin and its analogs are promising therapeutic agents for acute pancreatitis. However, the therapeutic effects remain controversial. Somatostatin analogs preferentially bind to somatostatin receptor 2 (SSTR2), and this study aimed to investigate whether N-glycosylation affects SSTR2 stability, membrane trafficking, and signal transduction.
methodsWestern blot analysis following PNGase F digestion was performed to confirm N-glycosylation of SSTR2 in rat pancreatic acinar AR42J cells. Rats were subjected to 4 hourly intraperitoneal injections of cerulein (50 µg/kg) plus LPS (5 µg/mL) to induce acute pancreatitis. Mass spectrometry was conducted to identify the glycosylation sites of SSTR2, and immunofluorescent staining was carried out to examine the localization of wild-type and asparagine 9 (N9)Q-mutant SSTR2. Proteasome inhibitor MG132 was employed to assess the stability of SSTR2, and overexpression of wild-type or N9Q-mutant SSTR2 was used to examine the role of N-glycosylation in SSTR2 signal transduction
resultsSSTR2 protein in AR42J cells was N-glycosylated at the N9 residue. Wild-type SSTR2 localized in the plasma membrane whereas N9Q-mutant SSTR2 was retained in the endoplasmic reticulum (ER). MG132 rapidly restored the ectopic expression of mutant but not wild-type SSTR2 protein in AR42J cells. Overexpression of wild-type but not N9Q-mutant SSTR2 activated NF-κB signaling and facilitated nuclear transportation of p65 in AR42J cells upon cerulein plus LPS stimulation. Furthermore, pretreatment with wild-type but not N9Q-mutant SSTR2-overexpressing vectors significantly ameliorated biochemical parameters and pancreatic histological impairments in rats with pancreatitis.
conclusionsN-glycosylation of SSTR2 is essential for membrane localization, stability, and signal transduction of SSTR2 in pancreatic cells, playing a protective role in experimental acute pancreatitis.
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