2019
Early trypsin activation develops independently of autophagy in caerulein-induced pancreatitis in mice
Malla SR, Krueger B, Wartmann T, Sendler M, Mahajan UM, Weiss FU, Thiel FG, De Boni C, Gorelick FS, Halangk W, Aghdassi AA, Reinheckel T, Gukovskaya AS, Lerch MM, Mayerle J. Early trypsin activation develops independently of autophagy in caerulein-induced pancreatitis in mice. Cellular And Molecular Life Sciences 2019, 77: 1811-1825. PMID: 31363815, PMCID: PMC8221268, DOI: 10.1007/s00018-019-03254-7.Peer-Reviewed Original Research
2010
Dantrolene mitigates caerulein-induced pancreatitis in vivo in mice
Orabi AI, Shah AU, Ahmad MU, Choo-Wing R, Parness J, Jain D, Bhandari V, Husain SZ. Dantrolene mitigates caerulein-induced pancreatitis in vivo in mice. AJP Gastrointestinal And Liver Physiology 2010, 299: g196-g204. PMID: 20448143, PMCID: PMC2904115, DOI: 10.1152/ajpgi.00498.2009.Peer-Reviewed Original ResearchMeSH KeywordsAmylasesAnimalsApoptosisCalcium Channel BlockersCalcium SignalingCeruletideCytoprotectionDantroleneDisease Models, AnimalEnzyme ActivationFluorescent Antibody TechniqueIn Situ Nick-End LabelingMaleMiceMice, Inbred C57BLMicroscopy, ElectronPancreasPancreatitisRyanodine Receptor Calcium Release ChannelSeverity of Illness IndexTime FactorsTrypsinConceptsPancreatic trypsin activityCaerulein-induced pancreatitisRyanodine receptorAcinar cellsMouse pancreatic sectionsHigh-risk settingsTUNEL-positive cellsLater time pointsRyR inhibitor dantroleneDantrolene pretreatmentHistological severityAcute pancreatitisPancreatic acinar cellsInflammatory disordersProphylactic treatmentRyR inhibitionSerum amylasePancreatitis inductionPancreatic sectionsPancreatitisAdequate treatmentTrypsin activityEarly markerCaerulein hyperstimulationUltrastructural derangements
1999
Mechanisms of intracellular zymogen activation
Gorelick F, Otani T. Mechanisms of intracellular zymogen activation. Best Practice & Research Clinical Gastroenterology 1999, 13: 227-240. PMID: 11030603, DOI: 10.1053/bega.1999.0021.Peer-Reviewed Original ResearchConceptsTrypsinogen activation peptideAcinar cellsZymogen processingDistinct subcellular compartmentsZymogen activationSerine proteasesIntracellular serine proteaseIntracellular zymogen activationCaerulein-induced pancreatitisAcinar cell compartmentPancreatic acinar cellsAcute pancreatitisSubcellular compartmentsHuman pancreatitisPancreatitisExperimental pancreatitisSupramaximal concentrationsHereditary pancreatitisLow-pH compartmentsPancreatic aciniTrypsinogen activationTrypsinogen processingGenetic diseasesCell pathwaysIntracellular activation
1998
Codistribution of TAP and the granule membrane protein GRAMP-92 in rat caerulein-induced pancreatitis
Otani T, Chepilko S, Grendell J, Gorelick F. Codistribution of TAP and the granule membrane protein GRAMP-92 in rat caerulein-induced pancreatitis. American Journal Of Physiology 1998, 275: g999-g1009. PMID: 9815030, DOI: 10.1152/ajpgi.1998.275.5.g999.Peer-Reviewed Original ResearchConceptsAcinar cell compartmentNumber of vesiclesRecycling endosomesSupranuclear compartmentPancreatic acinar cellsTime-dependent mannerProcessing siteCell compartmentTrypsinogen processingPhysiological levelsZymogen granulesImmunofluorescence studiesCaerulein-induced pancreatitisAcinar cellsActivation peptideTrypsinogen activation peptidePathological activationCompartmentsActivation
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