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Biomedical subjects

M Reiss

Publications and source records attributed to M Reiss.

At least 217 records · Page 12Linked to original sources

Inhibition by somatostatin of gastrin release and gastric acid responses to meals and to pentagastrin in man.

The inhibitory actions of intravenous somatostatin on the gastric secretory responses to pentagastrin (1.5 microng/kg-h i.v.) and to a meal (10% peptone, pH 5.5) were studied in six healthy subjects. Meal-induced gastric acid output was estimated by means of a modified Fordtran and Walsh method of intragastric titration. Somatostatin (5 microng/kg-h; cyclic form) significantly inhibited the total 1-hour acid response to pentagastrin by about 70% (inhibition of pepsin secretion: about 70%) and that to a test meal by about 75%. During the last 30 min of somatostatin infusion the pentagastrin-stimulated secretion of acid was significantly reduced by about 90% (inhibition of pepsin output: about 85%) while the corresponding figure in the test with meal-induced secretion was about 95%. Serum gastric--elevated in response to the test meal--was found to be merely lowered by about 30% during somatostatin infusion. Consequently, it is tempting to assume that inhibition of human gastric acid secretion by exogenous somatostatin largely results from a direct antisecretory effect upon parietal cells and, only to a minor extent, from an indirect action via reduction of gastrin release.

Adult↗

Superior immunoreactivity of 125I (Des-Tyr-betaAla)-secretin with rabbit anti-secretin sera compared to 125I-secretin and 125 I-6-Tyrosyl secretin.

A secretin analogue in which the normal amino acid sequence had been elongated by a (Des-Tyr-betaAla)-residue was studied as tracer for secretin radioimmunoassay. 125I-(DATA)-secretin exhibited superior immunoreactivity with several rabbit anti-secretin sera compared to 125I-6-Tyr-secretin and also to secretin iodinated at its N-terminal histidyl residue. This may be due, at least in part, to higher conformational integrity of the secretin moiety in the 125I-(DATA)-secretin molecule. Thus, at present, 125I-(DATA)-secretin appears to be most suitable as tracer for sensitive secretin radioimmunoassay.

Amino Acid Sequence↗

[Redioimmunoassay for secretin (author's transl)].

The synthesis of a secretin with an elongated N-terminus, namely Nalpha-(deaminotyrosyl-beta-alanyl)- secretin (DATA-secretin), using a conventional strategy, is described. After purification of the product by means of ion exchange chromatography on SP-Sephadex C-25 and by continuous carrier-free electrophoresis, immunological studies on the synthetic DATA-secretin were carried out using secretin antibodies. In comparison to 125iodine-labelled secretin and [Tyr6]secretin, 125iodine-DATA-secretin proved to be by far the best "tracer". Elaboration of a radioimmunoassay for secretin is therefore possible.

Animals↗