<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>9(22)</volume><submitter>Huang M</submitter><pubmed_abstract>&lt;h4>Background&lt;/h4>The 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.&lt;h4>Methods&lt;/h4>Western 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 carr</pubmed_abstract><journal>Annals of translational medicine</journal><pagination>1667</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8667150</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>N-glycosylation of somatostatin receptor type 2 protects rats from acute pancreatitis.</pubmed_title><pmcid>PMC8667150</pmcid><pubmed_authors>Huang M</pubmed_authors><pubmed_authors>Chen W</pubmed_authors><pubmed_authors>Chen MM</pubmed_authors><pubmed_authors>Xu F</pubmed_authors><pubmed_authors>Han D</pubmed_authors></additional><is_claimable>false</is_claimable><name>N-glycosylation of somatostatin receptor type 2 protects rats from acute pancreatitis.</name><description>&lt;h4>Background&lt;/h4>The 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.&lt;h4>Methods&lt;/h4>Western 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 carr</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Nov</publication><modification>2025-06-01T03:23:15.438Z</modification><creation>2025-06-01T03:23:15.438Z</creation></dates><accession>S-EPMC8667150</accession><cross_references><pubmed>34988176</pubmed><doi>10.21037/atm-21-5249</doi></cross_references></HashMap>