Profiles of pure pancreatic secretions obtained by direct pancreatic duct cannulation in normal healthy human subjects

Rinderknecht, H.; Renner, Ian G.; Douglas, A.G.; Adham, Nabeel F.

doi:10.1016/0016-5085(78)90080-x

Cited by 69 publications

(14 citation statements)

References 13 publications

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“…Pure pancreatic juice was obtained by cannulation of the main pancreatic duct as described by Rinderknecht et al (1978b). Secretions were collected at one minute intervals for a total of 20 minutes after initial stimulation with secretin and cholecystokininpancreozymin (CCK-PZ) 10 minutes later.…”

Section: Collection Proceduresmentioning

confidence: 99%

“…A SSAY S Trypsinogen present in each of the one minute collections of PPJ was determined as active trypsin after activation with human enteropeptidase as described previously (Rinderknecht et al, 1978b). Trypsin activity is expressed in ,ug active site-titrated bovine trypsin/ml PPJ.…”

Section: Collection Proceduresmentioning

confidence: 99%

“…Trypsin (Worthington Biochemical Corp., Freehold, N J) is about 55-60% active. Pancreatic trypsin inhibitor was determined according to Rinderknecht et al (1978b). ELECTROPHORESIS Gels containing 8.5 % polyacrylamide and measuring 10.5 cm were prepared in siliconised tubes 0.7 cm in diameter.…”

Section: Collection Proceduresmentioning

confidence: 99%

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Trypsinogen variants in pancreatic juice of healthy volunteers, chronic alcoholics, and patients with pancreatitis and cancer of the pancreas

Rinderknecht¹,

Renner²,

Carmack³

1979

Gut

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Section: Collection Proceduresmentioning

confidence: 99%

Section: Collection Proceduresmentioning

confidence: 99%

See 1 more Smart Citation

Trypsinogen variants in pancreatic juice of healthy volunteers, chronic alcoholics, and patients with pancreatitis and cancer of the pancreas

Rinderknecht¹,

Renner²,

Carmack³

1979

Gut

Self Cite

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“…FFAs in PPJ are not likely to be coupled with any specific pancreatic secretory mechanism, because FFAs concentration and composition were not different between "secretin phase" and "CCK-PZ phase." FFAs concentration tended to be slightly higher in "wash-out phase," probably because the PPJ was concentrated in the pancreatic duct during an overnight fast (20). Therefore, FFAs in normal PPJ may be a result of permeation from the pancreatic interstitial fluid and/or the products of the physiological cell-cycle of the parenchymal cells of the pancreas.…”

Section: Discussionmentioning

confidence: 83%

Free Fatty Acids in Human Pure Pancreatic Juice

Miyake

Harada²,

Ochi³

et al. 1988

Pancreas

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Human pure pancreatic juice (PPJ) and serum were analyzed for free fatty acids (FFAs) to study whether the damage to pancreatic cell membranes in pancreatitis is reflected as abnormal FFAs concentration and composition. Patients consisted of 13 normal controls, 7 patients with acute pancreatitis (AP) in remission, and 27 with chronic pancreatitis (CP). PPJ was collected at 2-min intervals after secretin and then cholecystokininpancreozymin stimulation by endoscopic cannulation of the pancreas. The following results were obtained: (a) serum FFAs concentration and composition showed no significant difference between the three groups. (b) FFAs concentration in PPJ was significantly raised in CP through all secretory phases. The rise was significant only in "secretin phase" in AP. In many of the cases with raised FFAs concentration in PPJ, the FFAs composition was similar to that in serum. (c) Arachidonic acid, undetected in normal PPJ, was disproportionately high in concentration and composition in PPJ of eight patients with CP. Two mechanisms were proposed to explain these abnormalities: transudation of serum FFAs into the pancreatic duct and local production of arachidonic acid as a result of the damage to pancreatic cell membranes.

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“…According to previous studies, the major proteases in the small intestine are secreted by the pancreas and include trypsin, chymotrypsin, elastase, carboxypeptidase-A (CPA) and carboxypeptidase-B (CPB) [18,19,20]. In Figure 2A, the negative migration of the reflected light in bio-layer interferometry assays, measured as change in wavelength in nm, which is represented by δλ and indicated the proteases hydrolysis efficiency to the substrate.…”

Section: Resultsmentioning

confidence: 96%

Systematic Design of Trypsin Cleavage Site Mutated Exendin4-Cysteine 1, an Orally Bioavailable Glucagon-Like Peptide-1 Receptor Agonist

Sai

Tian

Yang

et al. 2017

IJMS

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Abstract:Exendin-4 is a strong therapeutic candidate for the treatment of metabolic syndrome. Related receptor agonist drugs have been on the market since 2005. However, technical limitations and the pain caused by subcutaneous injection have severely limited patient compliance. The goal of the study is to investigate a biologically active exendin-4 analog could be administered orally. Using intraperitoneal glucose tolerance tests, we discovered that exendin4-cysteine administered by oral gavage had a distinct hypoglycemic effect in C57BL/6J mice. Using Rosetta Design and Amber, we designed and screened a series of exendin4-cysteine analogs to identify those that retained biological activity while resisting trypsin digestion. Trypsin Cleavage Site Mutated Exendin4-cysteine 1 (TSME-1), an analog whose bioactivity was similar to exendin-4 and was almost completely resistant to trypsin, was screened out. In addition, TSME-1 significantly normalized the blood glucose levels and the availability of TSME-1 was significantly higher than that of exendin-4 and exendin4-cysteine. Collectively orally administered TSME-1, a trypsin-resistant exendin-4 analog obtained by the system, is a strong candidate for future treatments of type 2 diabetes.

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Profiles of pure pancreatic secretions obtained by direct pancreatic duct cannulation in normal healthy human subjects

Cited by 69 publications

References 13 publications

Trypsinogen variants in pancreatic juice of healthy volunteers, chronic alcoholics, and patients with pancreatitis and cancer of the pancreas

Trypsinogen variants in pancreatic juice of healthy volunteers, chronic alcoholics, and patients with pancreatitis and cancer of the pancreas

Free Fatty Acids in Human Pure Pancreatic Juice

Systematic Design of Trypsin Cleavage Site Mutated Exendin4-Cysteine 1, an Orally Bioavailable Glucagon-Like Peptide-1 Receptor Agonist

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