About: Intracellular autoactivation of human cationic trypsinogen mutants causes reduced trypsinogen secretion and acinar cell death

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About: Intracellular autoactivation of human cationic trypsinogen mutants causes reduced trypsinogen secretion and acinar cell death Goto Sponge NotDistinct Permalink

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scientific article published on 29 September 2009

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description	videnskabelig artikel (da) article científic (ca) articolo scientifico (it) artigo científico (pt) bilimsel makale (tr) vedecký článok (sk) vetenskaplig artikel (sv) vědecký článek (cs) wetenschappelijk artikel (nl) wissenschaftlicher Artikel (de) научни чланак (sr) article scientifique (fr) artículu científicu espublizáu en 2009 (ast) наукова стаття, опублікована у вересні 2009 (uk) scientific article published on 29 September 2009 (en) مقالة علمية نشرت في 29 سبتمبر 2009 (ar)
publication date	wds:Q37446172-6B51FA25-702A-4A4F-BDA9-48F109764CF7
publication date	2009-09-29 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q37446172-A46401DC-3D00-4A92-BD75-6A81E9F83E3F
language of work or name	English
cites work	wds:Q37446172-0F1CE0C7-60C3-47FA-B2D6-FE05223E8A7D wds:Q37446172-13D408B2-0EA6-4DD3-A122-1A70AC331C74 wds:Q37446172-190074DB-C6AC-4661-91B9-2A787C824E92 wds:Q37446172-1E95DAF3-0619-406B-B1B6-E56D5BE6545C wds:Q37446172-2122500C-E449-4AE1-9793-996C207A377B wds:Q37446172-2AD360D3-BDFA-4214-BF88-CAECD769337C wds:Q37446172-312F78D0-977F-42BD-BDD8-CDE0378B6E5B wds:Q37446172-3DD86A4A-5799-4B8E-BE61-8A6F7875B0D7 wds:Q37446172-3E78E7CE-42C2-419E-8543-020E121A4262 wds:Q37446172-4213B9B7-3CE5-4ABF-9159-4BB7CB61FCC2 wds:Q37446172-4468CFDA-072D-434D-B387-4FA62FDDFBD3 wds:Q37446172-6209A3C0-7C0F-4B07-BD99-19668F838600 wds:Q37446172-644B3C9E-2913-4540-B1F9-C8A9585E75B4 wds:Q37446172-6C79EB55-F654-4145-9B00-8F79DE1E9780 wds:Q37446172-70CA1C32-E68B-47DE-8789-77D607301799 wds:Q37446172-7207B69A-ED73-40AA-814F-F05A90A08CB1 wds:Q37446172-82143CB6-222C-400C-AE54-27EC9DEB2C69 wds:Q37446172-909AA137-E81C-4C5B-B49E-BBF97F5ABB1B wds:Q37446172-9338DAE2-C182-4276-9387-3D6CC34280F3 wds:Q37446172-A6754DC8-5C1C-45BB-8FA1-142FDB6DA038 wds:Q37446172-AF25C7B0-A823-4BFA-A3E6-FDA77AEABC09 wds:Q37446172-BC609951-D806-4C22-A547-3E2C5D8AFCAC wds:Q37446172-C6B6D854-CEF5-4C5B-A895-4745F0D3F445 wds:Q37446172-C96565F4-A1CD-46AB-B00A-624E49C6ED75 wds:Q37446172-CA86E2F0-57AE-47DA-BE52-623C3C2A6E93 wds:Q37446172-CED6351B-77D8-4CE0-B188-86404670B5FA wds:Q37446172-D3CB38DD-B15E-4994-A875-55ED9A2CDA14 wds:Q37446172-E1B8370D-DAF5-4427-B6A9-5E37B6DB8BBC wds:Q37446172-E20505AC-B9A1-4066-8BBF-5809B8D5B355 wds:Q37446172-E236ABA7-23A6-489D-A821-E9D833BCB01A wds:Q37446172-ED52AF86-2C31-4657-8BC9-9BE9E0018E48 wds:Q37446172-F7C4D586-9445-4C1E-AB40-49CFEA6A75B3 wds:Q37446172-F8FC0C8E-7F29-436D-9071-04DF4F6344A0 wds:Q37446172-FBC2425D-0A22-431B-98A8-991877E43C30
cites work	Human mesotrypsin exhibits restricted S1' subsite specificity with a strong preference for small polar side chains Human cationic trypsinogen. Role of Asn-21 in zymogen activation and implications in hereditary pancreatitis Signal integration in the endoplasmic reticulum unfolded protein response Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene From endoplasmic-reticulum stress to the inflammatory response That which does not kill me makes me stronger: adapting to chronic ER stress Involvement of autophagy in trypsinogen activation within the pancreatic acinar cells Mutations of human cationic trypsinogen (PRSS1) and chronic pancreatitis Biochemical models of hereditary pancreatitis Signal peptide variants that impair secretion of pancreatic secretory trypsin inhibitor (SPINK1) cause autosomal dominant hereditary pancreatitis Hereditary pancreatitis caused by a novel PRSS1 mutation (Arg-122 --> Cys) that alters autoactivation and autodegradation of cationic trypsinogen Cathepsin B cleavage of the trypsinogen activation peptide Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide Why does pancreatic overstimulation cause pancreatitis? Chymotrypsin C (caldecrin) stimulates autoactivation of human cationic trypsinogen Stable monomeric form of an originally dimeric serine proteinase inhibitor, ecotin, was constructed via site directed mutagenesis The tetra-aspartate motif in the activation peptide of human cationic trypsinogen is essential for autoactivation control but not for enteropeptidase recognition Gain-of-function mutations associated with hereditary pancreatitis enhance autoactivation of human cationic trypsinogen. Alteration of the specificity of ecotin, an E. coli serine proteinase inhibitor, by site directed mutagenesis. Chronic pancreatitis associated with an activation peptide mutation that facilitates trypsin activation Affinity purification of recombinant trypsinogen using immobilized ecotin. Presence of cathepsin B in the human pancreatic secretory pathway and its role in trypsinogen activation during hereditary pancreatitis Glucocorticoids increase amylase mRNA levels, secretory organelles, and secretion in pancreatic acinar AR42J cells Hereditary pancreatitis caused by mutation-induced misfolding of human cationic trypsinogen: a novel disease mechanism Intracellular trypsin induces pancreatic acinar cell death but not NF-kappaB activation Evolution of trypsinogen activation peptides Possible lysosomal activation of pancreatic zymogens. Activation of both human trypsinogens by cathepsin B and spontaneous acid. Activation of human trypsinogen 1 Mutations in the cationic trypsinogen gene and evidence for genetic heterogeneity in hereditary pancreatitis. Structural reorganization of the rough endoplasmic reticulum without size expansion accounts for dexamethasone-induced secretory activity in AR42J cells. Expression of mutated cationic trypsinogen reduces cellular viability in AR4-2J cells Expression of human cationic trypsinogen with an authentic N terminus using intein-mediated splicing in aminopeptidase P deficient Escherichia coli Glucocorticoids increase cholecystokinin receptors and amylase secretion in pancreatic acinar AR42J cells. Coupled induction of exocrine proteins and intracellular compartments involved in the secretory pathway in AR4-2J cells by glucocorticoids. The guinea pig pancreas secretes a single trypsinogen isoform, which is defective in autoactivation.
author name string	wds:Q37446172-483088AF-1B0A-4183-8F8A-C5B20DBE064F
author name string	Miklós Sahin-Tóth
rdfs:label	Intracellular autoactivation of human cationic trypsinogen mutants causes reduced trypsinogen secretion and acinar cell death (en) Intracellular autoactivation of human cationic trypsinogen mutants causes reduced trypsinogen secretion and acinar cell death (nl) Intracellular autoactivation of human cationic trypsinogen mutants causes reduced trypsinogen secretion and acinar cell death (ast)
skos:prefLabel	Intracellular autoactivation of human cationic trypsinogen mutants causes reduced trypsinogen secretion and acinar cell death (en) Intracellular autoactivation of human cationic trypsinogen mutants causes reduced trypsinogen secretion and acinar cell death (nl) Intracellular autoactivation of human cationic trypsinogen mutants causes reduced trypsinogen secretion and acinar cell death (ast)
name	Intracellular autoactivation of human cationic trypsinogen mutants causes reduced trypsinogen secretion and acinar cell death (en) Intracellular autoactivation of human cationic trypsinogen mutants causes reduced trypsinogen secretion and acinar cell death (nl) Intracellular autoactivation of human cationic trypsinogen mutants causes reduced trypsinogen secretion and acinar cell death (ast)

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