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193 results on '"St. Pierre, Serge"'

1. Calcitonin gene-related peptide in viscerosensitive response to colorectal distension in rats

Author

Plourde, Victor, St-Pierre, Serge, and Quirion, Remi

Subjects
Nociceptors -- Physiological aspects, Calcitonin -- Physiological aspects, Colorectal diseases -- Research, Biological sciences
Abstract

Research shows that cacitonin gene-related peptide (CGRP) is critical to the visceral afferent nerve sensitization from gastrointestinal origin. Studies on colorectal distension-induced visceral pain using conscious rats indicate that CGRP actively stimulates abdominal contractions caused by colorectal distension. Experimental evidence suggests that CGRP promotes nociceptive transmission.

Published
1997

5. Neurotensin

Author

Jolicoeur, François B., Rioux, Francis, St.-Pierre, Serge, and Lajtha, Abel, editor

Published
1985
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6. Motilin receptors in the human antrum

Author

MILLER, PAUL, ROY, ANDRE, ST-PIERRE, SERGE, DAGENAIS, MICHEL, LAPOINTE, REAL, and POITRAS, PIERRE

Subjects
Smooth muscle -- Physiological aspects, Peptides -- Research, Gastrointestinal system -- Analysis, Biological sciences
Abstract

Paul Miller, Andre Roy, Serge St-Pierre, Michel Dagenais, Real Lapointe, and Pierre Poitras. Motilin receptors in the human antrum. Am. J. Physiol. Gastrointest. Liver Physiol. 278: G18-G23, 2000.--Motilin is an intestinal peptide that stimulates contraction of gut smooth muscle. The motilin receptor has not been cloned yet, but motilin-receptor agonists appear to be potent prokinetic agents for the treatment of dysmotility disorders. The aim of this study was to determine neural or muscular localization of motilin receptors in human upper gastrointestinal tract and to investigate their pharmacological characteristics. The binding of [sup.125] I-labeled motilin to tissue membranes prepared from human stomach and duodenum was studied; rabbit tissues were used for comparison. Solutions enriched in neural synaptosomes or in smooth muscle plasma membranes were obtained. Various motilin analogs were used to displace the motilin radioligand from the various tissue membranes. The highest concentration of human motilin receptors was found in the antrum, predominantly in the neural preparation. Human motilin receptors were sensitive to the [NH.sub.2]-terminal portion of the motilin molecule, but comparison with rabbit showed that both species had specific affinities for various motilin analogs [i.e., Mot-(1--9), Mot-(1--12), Mot-(1--12) ([CH.sub.2]NH).sub.10-11], and erythromycin]. Motilin receptors obtained from synaptosomes or muscular plasma membranes of human antrum expressed different affinity for two motilin-receptor agonists, Mot-(1--12) and Mot-(1--12) ([CH.sub.2]NH).sub.10-11], suggesting that they correspond to specific receptor subtypes. We conclude that human motilin receptors are located predominantly in nerves of the antral wall, are functionally (and probably structurally) different from those found in other species such as the rabbit, and express specific functional (and probably structural) characteristics dependent on their localization on antral nerves or muscles, suggesting the existence of specific receptor subtypes, potentially of significant physiological or pharmacological relevance. gastrointestinal motility; regulatory peptides; receptor sub-types

Published
2000

8. Biological Activities of GLP-1 Analogs In Vitro and In Vivo

Author

XIAO, QIANG, GIGUERE, JULIE, JENG, WINNIE, ST. PIERRE, SERGE, BRUBAKER, PATRICIA L., and WHEELER, MICHAEL B.

Subjects
Diabetes -- Care and treatment, Glucagon -- Physiological aspects, Health
Abstract

Although studies support a role for GLP-1 as a potential treatment for diabetes, the fact that the GLP-1 is rapidly degraded limits its clinical application. Hence, understanding the structure-activity of [...]

Published
2000

39. Functional Identification of Peptide Receptors.

Author

Boulton, Alan A., Baker, Glen B., Pittman, Q. J., and St-Pierre, Serge A.

Abstract

With the advent of modern chromatographic instrumentation and improved sequencing methods that allow for isolation and characterization of minute amounts of biological material, a host of biologically active peptides are now known. More recently, the dramatic development of genetic engineering has contributed to revealing the structure of complete genes coding for known, as well as novel, biologically active peptides, in addition to a large number of other peptide sequences of unknown significance. Even though precise physiological functions could be assigned to insulin, parathyroid hormone (PTH), calcitonin, growth hormone (GH), and growth hormone releasing factor (GHRH), corticotropin (ACTH) and corticotropin releasing factor (CRF), atria1 natriuretic factor (ANF), oxytocin, and a few others, the role of more than one hundred peptides displaying various biological activities in vitro or in vivo is still awaiting definition. Moreover, recent advances in immunocytochemistry and receptor imaging have revealed the ubiquity of several among these "well-established" peptides and their corresponding receptors, for which the localization and action had been previously assigned to given target organs or tissues. Most remarkable are the peptides of the now so-called "brain-gutheart" axis, for which coexistence among themselves and/or with classical neurotransmitters such as the catecholamines in nerve fibers has been recently demonstrated (Cuello, 1982). [ABSTRACT FROM AUTHOR]

Published
1987
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42. Neurobehavioral profile of neuropeptide Y

Author

Jolicoeur, François B., primary, Michaud, Jean-Nil, additional, Rivest, Robert, additional, Menard, Daniel, additional, Gaudin, Daniel, additional, Fournier, Alain, additional, and St-Pierre, Serge, additional

Published
1991
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