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Biomedical subjects

R E Chance

Publications and source records attributed to R E Chance.

At least 55 records · Page 3Linked to original sources
PubMed1977

Bovine pancreatic peptide: action on gastric and pancreatic secretion in dogs.

Bovine pancreatic peptide (BPP) is a straight chain peptide containing 36 amino acid residues that has recently been isolated from pancreatic tissue. At a dose of 40 mug/kg-h intravenously, it stimulated gastric acid secretion when given alone but inhibited the submaximal secretion induced by the C-terminal pentapeptide of gastrin. Basal pancreatic secretion of dogs was inhibited by BPP (1-10 mug/kg-h) inhibited pancreatic protein secretion but often showed a biphasic action on water-bicarbonate response, an initial augmentation followed by reduction. BPP (2-5 mug/kg-h) inhibited pancreatic water-bicarbonate and protein secretions induced by an infusion of secretin plus cholecystokinin. Des-tyrosyl-NH2 BPP lacking the C-terminal tyrosyl amide, failed to inhibit gastric acid induced by C-terminal pentapeptide of gastrin or pancreatic secretion induced by secretin. BPP had no hyper- or hypoglycemic, hyperkalemic, or diuretic actions in the dog.

Animals↗
PubMed1977

Serum levels of human pancreatic polypeptide in renal disease.

The newly recognized pancreatic polypeptide (PP) has been demonstrated in the circulation of healthy subjects, although its physiological role is not definately established. In order to investigate the renal role in the elimination of PP from the circulation, PP was determined in patients with varying degrees of renal damage, in patients on chronic haemodialysis, and in patients who have undergone renal transplantation. A close correlation was found between glomerular filtration rate and serum PP. In the uraemic group, PP levels were highly elevated as compared to normal individuals. After renal transplantation, PP values declined in step with the improvement in glomerular filtration rate. The increased serum PP levels in renal failure raise the possibility of PP being involved in the development of uraemic gastrointestinal symptoms.

Adolescent↗
PubMed1976

Pancreatic-polypeptide response to food in duodenal-ulcer patients before and after vagotomy.

In 21 normal fasting subjects basal serum-pancreatic-polypeptide (H.P.P.), as measured by a specific radioimmunoassay, was 43 +/- 4 pmol/l (mean +/- S.E.M). This basal concentration was of the same magnitude as that of other gastrointestinal peptide hormones. In normal subjects the H.P.P. response to food was bisphasic. A rapid eightfold increase, reaching a maximum 20--30 min after beginning of the meal, was followed by a secondary, prolonged increase. H.P.P. did not return to basal concentration within five hours. 14 duodenal-ulcer (D.U.) patients were studied before and after truncal vagotomy. Before operation the D.U. patients had higher basal H.P.P. concentrations than the normal group (110 +/- 40 pmol/l) whereas their H.P.P. response pattern to food was similar to that of the normal subjects. After vagotomy the primary rapid increase in H.P.P. concentration was eliminated and the secondary, prolonged response was significantly reduced (P less than 0-005). The results indicate that H.P.P. is a digestive hormone under vagal control.

Adult↗
PubMed1976

The immunogenicity of insulin preparations.

Patients who had never received insulin were administered porcine or bovine Lente insulins prepared from either conventional USP-grade insulin, "single-peak" insulin (SPI), or "single-component" insulin (SCI) in an attempt to determine if insulin immunogenecity was related to the purity of various insulin preparations. Serum insulin antibody titers were monitored by a sensitive I125-insulin binding procedure. All six groups of patients had some degree of antibody formation after six months of continuous insulin administration. Based upon the percent of I125-insulin bound by the serum, the least immunogenic insulin preparation was the porcine SCI. The most immunogenic insulins were the bovine preparations, all three of which gave comparable antibody responses. The patients who received porcine USP insulin and porcine SPI had similar antibody titers, both of which were significantly higher than the titers from the patients on porcine SCI, but significantly lower than the antibody titers from the patients treated with any of the bovine preparations. The immunogenicity of bovine SCI was significantly reduced by administering multiple daily doses of the neutral regular form instead of one or two daily injections of the Lente form, Although these purer insulin preparations (SPI and SCI) are still associated with various degrees of immunogenecity, they are significant improvements for the treatment of insulin lipoatrophy and insulin allergy.

Adolescent↗
PubMed1976

Occurrence of human pancreatic polypeptide in pancreatic endocrine tumors. Possible implication in the watery diarrhea syndrome.

Eighteen endocrine pancreatic tumors were examined for the occurrence of cells producing insulin, glucagon, gastrin, human pancreatic polypeptide (HPP), and vasoactive intestinal polypeptide (VIP) and for A1 cells. More than half of the tumors were mixed, i.e., they contained more than one type of hormone-producing cell. The clinical symptoms were attributable only to one of the hormones produced by the mixed tumors. Three of four tumors causing the watery diarrhea syndrome contained both VIP and HPP cells. In one such tumor there was a strong predominance of HPP cells; the serum HPP levels of this patient were a thousandfold elevated, whereas her VIP levels were within the normal range. Several lines of evidence point to HPP as a possible agent causing the watery diarrhea syndrome. In many of our patients, HPP cells hyperplasia was present in the extratumoral pancreas. Such hyperplasia may give rise to the raised serum HPP levels seen in many patients having endocrine pancreatic tumors.

Diarrhea↗
PubMed1968

Porcine proinsulin: characterization and amino acid sequence.

Proinsulin in nearly homogeneous form has been isolated from a preparation of porcine insulin. A molecular weight close to 9100 was calculated from the amino acid composition and from sedimentation-equilibrium studies. Through the action of trypsin this single-chain protein is transformed to desalanine insulin by cleavage of a polypeptide chain connecting the carboxy-terminus of the B chain to the amino-terminus of the A chain of insulin. The amino acid sequence of this connecting peptide was found to be Arg-Arg-Glu-Ala-Gln-Asn-Pro-Gln-Ala-Gly-Ala-Val-Glu-Leu-Gly-Gly-Gly-Leu-Gly-Gly-Leu-Gln-Ala-Leu-Ala-Leu-Glu-Gly-Pro-Pro-Gln-Lys-Arg.

Amino Acid Sequence↗