INT22782
From wiki-pain
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Sentences Mentioned In
Key: | Protein | Mutation | Event | Anatomy | Negation | Speculation | Pain term | Disease term |
Immunohistochemical localization of trypsinogen and trypsin in acute and chronic pancreatitis. | |||||||||||||||
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Immunohistochemical localization of trypsinogen and trypsin in acute and chronic pancreatitis. | |||||||||||||||
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Immunoreactive trypsin was localized with the peroxidase-antiperoxidase technique in normal human pancreatic tissue and in the glands of patients suffering from acute or chronic pancreatitis. | |||||||||||||||
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In chronic pancreatitis, the localization of trypsin in acinar cells was similar to that in normal pancreas. | |||||||||||||||
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Increased interdigestive pancreatic trypsin secretion in alcoholic pancreatic disease. | |||||||||||||||
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A recent study showed that cathepsin B is abundantly present in the secretory compartment of the healthy human pancreas and is secreted together with trypsinogen and active trypsin into the pancreatic juice of patients with chronic pancreatitis [8]. | |||||||||||||||
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To date, only a few cases have demonstrated that pancreatitis is caused by simultaneous CFTR and SPINK1 mutations (5.5%), of PRSS1 and SPINK1 (1.3%), and of PRSS1 and CFTR (1.8%). | |||||||||||||||
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Mutational screening of the cationic trypsinogen gene in a large cohort of subjects with idiopathic chronic pancreatitis. | |||||||||||||||
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A recent study showed that cathepsin B is abundantly present in the secretory compartment of the healthy human pancreas and is secreted together with trypsinogen and active trypsin into the pancreatic juice of patients with chronic pancreatitis [8]. | |||||||||||||||
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The correlation was first observed in patients with hyperparathyroidism while trypsin activation, secretion stimulus and stabilization are suspected mechanisms [16]. | |||||||||||||||
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Augmentation of trypsin secretion was the most pronounced. | |||||||||||||||
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One drop of a 1 mg/ml CCK-OP solution applied intranasally, three times daily during 3 weeks resulted in a significant increase in volume, trypsin, lipase and amylase secretion in response to the Lundh test meal. | |||||||||||||||
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Measurement of the pancreatic response to feeding showed a 90% reduction in enzyme secretion compared to healthy volunteers, but no change in the uptake of stable isotope labeled amino acids into secreted trypsin. | |||||||||||||||
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Furthermore, trypsin-induced secretion was inhibited by the Ca(2+)-ATPase inhibitor cyclopiazonic acid and in low-Ca(2+) buffer. | |||||||||||||||
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Another study demonstrated that trypsin secretion in AP patients, especially with necrotizing AP, is significantly suppressed compared to healthy individuals. | |||||||||||||||
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Commercial enzymes (trypsin, carboxypeptidase B) were used to release methionine- and leucine-enkephalin from precursors. | |||||||||||||||
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A more recent study in healthy volunteers showed that EN can be given without stimulating pancreatic trypsin secretion provided that it is delivered into the mid-distal jejunum [31]. | |||||||||||||||
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As already mentioned, the pancreas is in a state of unresponsiveness during an attack of AP and the secretion of pancreatic juice and trypsin is reduced during AP [34, 37]. | |||||||||||||||
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Urinary trypsin inhibitor exists naturally in the human body and is secreted in greater quantities during stressful conditions, such as inflammation, cancer, infection, and tissue damage [15]. | |||||||||||||||
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Search parameters were as follows: cleavage by trypsin, one missed cleavage site allowed, carbamidomethylcysteine as fixed modification, and oxidized methionine as optional modification. | |||||||||||||||
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General Comments
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