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PubMed1988

Temporal pattern of appearance and distribution of cholecystokinin-like peptides during development in Xenopus laevis.

Cholecystokinin (CCK) radioimmunoassay and immunocytochemistry were used to localize the expression of CCK-like peptides in the gut, brain, and skin of Xenopus laevis during development from fertilization through metamorphosis to the adult form. CCK-like peptides were first detected in the gut shortly before food was first observed in the lumen of the intestine. This CCK-like immunoreactivity (CCK-li) was localized in endocrine cells in the duodenal mucosa. Gut CCK-li decreased during metamorphosis coincident with gut histolysis. After metamorphosis, gut CCK-li appeared in the newly organized gastric antrum at Nieuwkoop-Faber stage 62-63 and reappeared in the reconstituted duodenum at stage 63-64. In both cases, CCK-li was localized in endocrine cells. In both the gastric antrum and the duodenum, the first appearance of CCK-li preceded the functional activity of its target tissues. CCK-li increased in the brain during brain primary differentiation and again during metamorphic climax coincidentally with the differentiation of the hypothalamo-hypophysial system. Brain CCK-li then declined during the transition from larva to adult. We conclude that the first presence of food in the lumen of the larval gut does not induce the appearance of CCK-li and that CCK may play a role in regulating the development of the gastrointestinal tract and brain in X. laevis.

Animals↗
PubMed1995

Effect of age on the response of blood lipids, body composition, and aerobic power to physical conditioning and deconditioning.

The influence of age on the response of plasma lipids, body composition, and cardiovascular performance to physical training and detraining was studied in 12 older and 12 young adult male cyclists. The athletes were first examined at the peak of their seasonal preparation and then again 2 months after its suspension. Sedentary males matched for age, weight, and height comprised the respective control groups. During training, body fat mass (BFM) was significantly lower and maximum oxygen consumption (VO2max) higher in both groups of cyclists as compared with controls. No differences in serum total cholesterol (TC), low-density lipoprotein cholesterol (LDL-C), apolipoprotein (apo) B, apo A-II, and fibrinogen were found. During the same phase, triglycerides (TG) and the LDL-C to high-density lipoprotein cholesterol (HDL-C) ratio were significantly lower and apo A-I, HDL-C, HDL3-C, and the apo A-I/apo B ratio were significantly higher in the athletes than in their corresponding sedentary controls. After physical deconditioning, BFM increased and VO2max decreased significantly in both groups of athletes. TG, very-low-density lipoprotein cholesterol (VLDL-C), and fibrinogen increased in young athletes while the LDL-C/HDL-C ratio increased, and apo A-I, HDL-C, HDL2-C, and HDL3-C decreased significantly in both young and older athletes. Thus, an aerobic training program induced an antiatherogenic lipoprotein profile and beneficial modifications in body composition and aerobic power in both older and younger subjects; a 2-month interruption in the program changed these parameters unfavorably in both groups. Age does not seem to influence significantly the plasma lipid response to physical deconditioning.

Adult↗
PubMed1993

Bombesin/GRP-preferring and neuromedin B-preferring receptors in the rat urogenital system.

Bombesin binding sites were localized in the rat urogenital system by autoradiography of 125I-Tyr4-bombesin binding to frozen tissue sections. Saturable binding was observed in the bladder, seminal vesicle, uterus, and oviduct. In all organs, the binding sites corresponded to layers of smooth muscle. Radioligand binding studies were performed on homogenized membrane preparations from bladder, uterus, and seminal vesicle. Membrane binding was saturable, reversible, time- and temperature-dependent, and specific for bombesin and related peptides. Analysis of saturable equilibrium binding from all three organs yielded a best fit to a one-site model of high affinity binding with apparent KdS of 720 pM for bladder, 470 pM for uterus, and 700 pM for seminal vesicle. Neuromedin B was potent in displacing saturable 125I-Tyr4-bombesin binding from bladder and seminal vesicle but not uterus membranes. In order to characterize these binding sites further, the ability of these membranes to interact with a specific bombesin receptor antagonist, [Leu13-psi-CH2NH-Leu14]-bombesin, and with GTP-gamma-S was determined. [Leu13-psi-CH2NH-Leu14]-bombesin was much more potent in displacing saturable 125I-Tyr4-bombesin binding from uterus than from bladder and seminal vesicle membranes, further supporting the distinction between the uterus and the bladder/seminal vesicle binding sites as bombesin receptor subtypes. GTP-gamma-S inhibited saturable 125I-Tyr4-bombesin binding to membranes from all three organs, indicating that both receptor subtypes are linked to GTP-binding proteins. We conclude that smooth muscle in the rat urogenital system expresses bombesin receptors and that endogenous GRP and neuromedin B may regulate some reproductive and excretory functions. The bladder and seminal vesicle express the neuromedin B-preferring subtype and the uterus expresses the bombesin/GRP-preferring subtype of bombesin receptor.

Amino Acid Sequence↗
PubMed1983

Gastrin/cholecystokinin-like immunoreactive peptides in the Dungeness crab, Cancer magister (Dana): immunochemical and biological characterization.

The purpose of this investigation was to characterize a gastrin/cholecystokinin-like immunoreactant (G/CCK-LI) extractable from the crab, Cancer magister. G/CCK-LI was extracted best in boiling water and was found mainly in the stomach, hemolymph and carapace. A relatively large immunoreactive peptide in the stomach and apparently smaller forms in the hemolymph and carapace were separated by Sephadex G-50 fractionation. Anion-exchange chromatography further fractionated the stomach form into three major peaks. The crab material cross-reacted with three antisera specific for the common C-terminus of gastrin/CCK, but cross-reacted much less with three antisera directed against other portions of the gastrin molecule. Partially purified crab stomach G/CCK-LI inhibited the binding of labeled CCK to mouse brain G/CCK receptors but not to rat pancreatic CCK receptors. The crab peptide did not stimulate rat gastric acid or rat pancreatic amylase secretion. These results indicate that the crab peptides are structurally similar to, but distinguishable from, the bioactive C-terminal amino acid sequence common to gastrins and CCKs.

Amylases↗
PubMed1984

Characterization of cholecystokinin receptors in bullfrog (Rana catesbeiana) brain and pancreas.

The binding of biologically active 125I-Bolton-Hunter-CCK-33 to bullfrog brain and pancreatic membrane particles was characterized. Both tissues exhibited time-dependent, saturable, reversible, and high affinity binding without evidence for cooperative interaction. Both bullfrog CCK receptors resembled their mammalian counterparts in having acidic pH optima for tracer binding and a Kd of about 0.5 nM. However, the receptors differed from their mammalian counterparts in that (1) the bullfrog brain membranes bound more tracer per mg protein than did the pancreatic membranes, (2) both bullfrog CCK receptors were relatively insensitive to dibutyryl cGMP, and (3) both bullfrog brain and pancreatic CCK receptors exhibited the same general specificity toward a variety of CCK and gastrin peptides. For both tissues, the relative order of receptor binding potency was CCK-8 greater than caerulein = CCK-33 greater than gastrin-17-II greater than CCK-8-ns = gastrin-17-I greater than caerulein-ns greater than gastrin-4 with the sulfated CCK peptides being 1000-fold more potent than their nonsulfated analogs. Sulfated gastrin was also relatively potent, being only 10-fold weaker than CCK-8. Gastrin-4 was 20 000-fold weaker than CCK-8 in interacting with the brain CCK receptor. The latter finding is in sharp contrast to the mammalian brain CCK receptor. We conclude that the bullfrog brain and pancreas contain similar CCK receptors of probable physiological significance and may represent an ancestral condition from which the two distinct CCK receptors present in mammalian brain and pancreas have evolved.

Animals↗
PubMed1995

Characterization and distribution of bombesin binding sites in the goldfish hypothalamic feeding center and pituitary.

Bombesin (BBS)/gastrin-releasing peptide (GRP) binding sites were characterized and their distribution examined in the goldfish brain and pituitary by radioligand binding and autoradiography. Binding of 125I-[Tyr4]-BBS-14 to tissue sections was found to be saturable, reversible, time-dependent and displaceable by BBS/GRP-like peptides. Analysis of saturable equilibrium binding revealed a one-site model fit with a Kd of 0.665 +/- 0.267 nM. This binding site displayed high affinity for members of the BBS subfamily of peptides, including GRP10 (Ki; 0.292 +/- 0.038 nM) and GRP27 (Ki; 2.034 +/- 1.597 nM), but showed no affinity for the BBS8-14 fragment. While an approximate 100-fold lower binding affinity was displayed by the binding site for neuromedin B (Ki; 6.15 +/- 28.2 nM), litorin was highly effective in displacing radiolabeled BBS binding (Ki; 1.469 +/- 0.427 nM). The localization of saturable and high affinity BBS/GRP binding sites in specific areas of the goldfish brain and pituitary generally revealed a similar anatomical distribution to BBS/GRP-like immunoreactive material reported previously by our laboratory. Quantitative densitometric analysis of radiolabeled BBS binding to brain nuclei and the pituitary revealed a moderate concentration of BBS/GRP binding sites in the hypothalamic feeding area, including the nucleus diffusus libi inferioris, nucleus recessus lateralis, nucleus lateral tuberis, and nucleus anterior tuberis. Other brain nuclei known to influence the brain feeding center which contained a high density of BBS/GRP binding sites included nuclei of the dorsal and ventro-medial telencephalon, the preoptic hypothalamus, and the optic tectum. High densities of BBS/GRP binding sites were also localized in the dorsal cerebellum, and nucleus habenularis. In the pituitary, BBS/GRP binding sites were present in high concentration in the neurointermediate lobe, with a relatively lower density localized in the pars distalis. The present study further supports a role for BBS/GRP-like peptides in the regulation of feeding behavior and anterior pituitary hormone secretion in teleosts.

Amino Acid Sequence↗
PubMed1996

Localization and characterization of neuropeptide Y/peptide YY receptors in the brain of the smooth dogfish (Mustelis canis).

Multiple receptor subtypes specific for the neuropeptide Y (NPY)/peptide Y (PYY) family of peptides exist in mammals, but little is known about the distribution of this receptor family in other vertebrates. Saturable binding sites for 125I-labeled porcine PYY were localized in frozen sections of the brain of the smooth dogfish (Mustelis canis) by radioligand binding and autoradiography. Saturable 125I-porcine PYY binding sites were distributed widely in the cerebral hemispheres, optic lobes, hypothalamus, cerebellum and hindbrain. Binding was saturable, specific for PYY and related peptides, and of high affinity (Kd = 2.53 nM). The specificity of the binding site was analyzed by performing competitive inhibition experiments with nonradioactive PYY, NPY, and [Leu31, Pro34]-NPY and NPY13-36, synthetic peptide analogs specific for the mammalian Y1 and Y2 receptor subtypes, respectively. Saturable 125I-porcine PYY binding sites in all regions of the dogfish brain closely resembled the mammalian Y1 NPY receptor subtype in specificity for these substances. There was no evidence for expression of multiple receptor subtypes. We conclude that a single receptor specific for the NPY/PYY family of peptides is widely expressed in the smooth dogfish brain and that this receptor closely resembles the mammalian Y1 receptor subtype, suggesting that the Y1 receptor is the ancestral receptor in this family.

Animals↗
PubMed1996

Localization of substance P NK-1 receptors in rat tongue.

In rat tongue, neurons containing substance P terminate in connective tissue, in taste buds, and in lingual epithelium surrounding taste buds in fungiform, foliate and circumvallate papillae. Although many functions have been attributed to these neurons, virtually nothing is known about their physiological function. As a step towards this end, immunocytochemical methods were used to identify the NK-1 receptors (SPR) in rat tongue. SPR-IR was found in the basolateral membranes of taste cells in fungiform, circumvallate and foliate papillae. SPR-IR was not found in the dorsal epithelium or in any structure that could be clearly identified as a neuron. SPR-IR was also found in von Ebner's glands in circumvallate and foliate papillae and in blood vessels in connective tissue in all three papillae. These data suggest that substance P may play a role in taste and/or in oral pain.

Amino Acid Sequence↗
PubMed1985

Cholecystokinin and its receptors in vertebrates and invertebrates.

Recent studies have indicated that cholecystokinin (CCK) peptides have a long evolutionary history. However, whereas all vertebrates examined have been shown to contain CCK-like peptides, this has not been possible to demonstrate for all invertebrate groups. Immunostaining studies indicate that CCK peptides originate only in neurons in groups below the level of the protochordates. It seems likely that CCK gastrointestinal endocrine cells evolved first at the level of the protochordates, possibly from sensory gut neurons similar to those seen in the invertebrates. Immunochemical and biological studies of a few invertebrate CCK-like peptides suggest that those molecules are substantially different in structure from vertebrate CCKs. Gastrin appears to have evolved from CCK at the level of the appearance of amniotes in vertebrate phylogeny. In mammals, central and peripheral CCK receptors differ in specificity for CCK- and gastrin-like peptides. Comparative studies reveal that this is true for birds as well, but reptiles, amphibia, and fish brain and pancreas CCK receptors exhibit nearly identical specificity patterns. This suggests that the lower vertebrate CCK receptor is ancestral to the distinct brain and pancreas CCK receptors seen in birds and mammals.

Animals↗
PubMedDate not supplied

Receptor binding sites for atrial natriuretic factor are expressed by brown adipose tissue.

To explore the possibility that atrial natriuretic factor (ANF) is involved in thermoregulation we used quantitative receptor autoradiography and homogenate receptor binding assays to identify ANF bindings sites in neonatal rat and sheep brown adipose tissue, respectively. Using quantitative receptor autoradiography were were able to localize high levels of specific binding sites for 125I-rat ANF in neonatal rat brown adipose tissue. Homogenate binding assays on sheep brown fat demonstrated that the radioligand was binding to the membrane fraction and that the specific binding was not due to a lipophilic interaction between 125I-rat ANF and brown fat. Specific binding of 125I-rat ANF to the membranes of brown fat cells was inhibited by unlabeled rat ANF with a Ki of 8.0 x 10(-9) M, but not by unrelated peptides. These studies demonstrate that brown fat cells express high levels of ANF receptor binding sites in neonatal rat and sheep and suggest that ANF may play a role in thermoregulation.

Adipose Tissue, Brown↗
PubMedDate not supplied

Biological activity of oxidized and reduced iodinated bombesins.

A method is reported for preparing oxidized and reduced iodinated Tyr4-bombesin. Iodogen was used to iodinate Tyr4-bombesin and the reaction products were separated by reverse-phase HPLC. The peak of oxidized label was then reduced by incubation with 725 mM dithiothreitol at 80 degrees C (pH 8.0) for one hour and the reaction products separated by HPLC as before. The reduced but not oxidized peaks of 125I-Tyr4-bombesin stimulated amylase release from rat pancreatic acini in vitro. We conclude that oxidation of bombesin producing C-terminal methionine sulfoxide destroys the biological activity of the peptide and that this form of oxidation can be reversed.

Amylases↗
PubMedDate not supplied

Substance P and substance K receptor binding sites in the human gastrointestinal tract: localization by autoradiography.

Quantitative receptor autoradiography was used to localize and quantify the distribution of binding sites for 125I-radiolabeled substance P (SP), substance K (SK) and neuromedin K (NK) in the human GI tract using histologically normal tissue obtained from uninvolved margins of resections for carcinoma. The distribution of SP and SK binding sites is different for each gastrointestinal (GI) segment examined. Specific SP binding sites are expressed by arterioles and venules, myenteric plexus, external circular muscle, external longitudinal muscle, muscularis mucosa, epithelial cells of the mucosa, and the germinal centers of lymph nodules. SK binding sites are distributed in a pattern distinct from SP binding sites and are localized to the external circular muscle, external longitudinal muscle, and the muscularis mucosa. Binding sites for NK were not detected in any part of the human GI tract. These results demonstrate that: 1) surgical specimens from the human GI tract can be effectively processed for quantitative receptor autoradiography; 2) of the three mammalian tachykinins tested, SP and SK, but not NK binding sites are expressed in detectable levels in the human GI tract; 3) whereas SK receptor binding sites are expressed almost exclusively by smooth muscle, SP binding sites are expressed by smooth muscle cells, arterioles, venules, epithelial cells of the mucosa and cells associated with lymph nodules; and 4) both SP and SK binding sites expressed by smooth muscle are more stable than SP binding sites expressed by blood vessels, lymph nodules, and mucosal cells.

Amino Acid Sequence↗
PubMedDate not supplied

Vasoactive intestinal peptide (VIP) receptors in the canine gastrointestinal tract.

Vasoactive intestinal peptide (VIP) is a putative neurotransmitter in both the brain and peripheral tissues. To define possible target tissues of VIP we have used quantitative receptor autoradiography to localize and quantify the distribution of 125I-VIP receptor binding sites in the canine gastrointestinal tract. While the distribution of VIP binding sites was different for each segment examined, specific VIP binding sites were localized to the mucosa, the muscularis mucosa, the smooth muscle of submucosal arterioles, lymph nodules, and the circular and longitudinal smooth muscle of the muscularis externa. These results identify putative target tissues of VIP action in the canine gastrointestinal tract. In correlation with physiological data, VIP sites appear to be involved in the regulation of a variety of gastrointestinal functions including epithelial ion transport, gastric secretion, hemodynamic regulation, immune response, esophageal, gastric and intestinal motility.

Animals↗
PubMedDate not supplied

The localization of sensory nerve fibers and receptor binding sites for sensory neuropeptides in canine mesenteric lymph nodes.

Previous work has established that the central nervous system can modulate the immune response. Direct routes through which this regulation may occur are the sympathetic and sensory innervation of lymphoid organs. We investigated the innervation of canine mesenteric lymph nodes using immunohistochemistry and the expression of binding sites for sensory neuropeptides using quantitative receptor autoradiography. The sympathetic innervation of lymph nodes was examined by immunohistochemical methods using an antiserum directed against tyrosine hydroxylase (TOH), the rate limiting enzyme in catecholamine synthesis. TOH-containing fibers were associated with 90% of the blood vessels (arteries, veins, arterioles and venules) in the hilus, medullary and internodular regions of lymph nodes and in trabeculae with no obvious relationship to blood vessels. The sensory innervation of lymph nodes was investigated using antisera directed against the putative sensory neurotransmitters calcitonin gene-related peptide (CGRP) and substance P (SP). CGRP- and SP-containing fibers were detected in the hilus, the medullary region, and the internodular region of lymph nodes usually in association with arterioles and venules. About 50% of the arterioles and venules exhibited a CGRP innervation and a smaller fraction (5-10%) were innervated by SP-containing fibers. Few if any TOH, CGRP, and SP nerve fibers were detected in the germinal centers of lymph nodes. Using quantitative receptor autoradiography we studied the distribution of receptor binding sites for the sensory neuropeptides CGRP, SP, substance K (SK), vasoactive intestinal peptide (VIP), somatostatin (SOM), and bombesin. Specific CGRP binding sites were expressed throughout lymph nodes by trabeculae, arterioles, venules and 25% of the germinal centers. SP receptor binding sites were localized to arterioles and venules in the T cell regions and 25-30% of the germinal centers. VIP binding sites were localized to the internodular and T cell regions, to medullary cords, and to 10-20% of germinal centers. SK, SOM, and bombesin binding sites were not detected in the lymph nodes, although receptor binding sites for these peptides were detected with high specific/nonspecific binding ratios in other canine peripheral tissues. Taken together with previous results these findings suggest that the sympathetic and sensory innervation of mesenteric lymph nodes appears to be involved with the regulation of their blood and lymph flow. The neuropeptide receptor binding sites in lymph node germinal centers may be expressed by lymphocytes upon activation by antigens.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMedDate not supplied

Receptors for sensory neuropeptides in human inflammatory diseases: implications for the effector role of sensory neurons.

Glutamate and several neuropeptides are synthesized and released by subpopulations of primary afferent neurons. These sensory neurons play a role in regulating the inflammatory and immune responses in peripheral tissues. Using quantitative receptor autoradiography we have explored what changes occur in the location and concentration of receptor binding sites for sensory neurotransmitters in the colon in two human inflammatory diseases, ulcerative colitis and Crohn's disease. The sensory neurotransmitter receptors examined included bombesin, calcitonin gene related peptide-alpha, cholecystokinin, galanin, glutamate, somatostatin, neurokinin A (substance K), substance P, and vasoactive intestinal polypeptide. Of the nine receptor binding sites examined only substance P binding sites associated with arterioles, venules and lymph nodules were dramatically up-regulated in the inflamed tissue. These data suggest that substance P is involved in regulating the inflammatory and immune responses in human inflammatory diseases and indicate a specificity of efferent action for each sensory neurotransmitter in peripheral tissues.

Animals↗
PubMedDate not supplied

Characterization of bombesin receptors on canine antral gastrin cells.

Dispersed canine antral mucosal cells were prepared by sequential steps of collagenase digestion and EDTA treatment. Cell preparations enriched in gastrin cells were made by centrifugal elutriation followed by step density gradient centrifugation. Specific, saturable, and reversible binding of 125I-[Tyr4]-bombesin was found in all preparations. This saturable binding was time, temperature, and cell number dependent. In both velocity (elutriator) and density cell separation experiments, saturable binding of bombesin correlated with the distribution of cells containing gastrin- but not somatostatin-like immunoreactivity. Maximal specific binding to gastrin (G) cell-enriched fractions was reached in 45 min at 37 degrees C and constituted 90% of total binding. Addition of 100 nM nonradioactive bombesin to cells incubated with 50 pM 125I-[Tyr4]-bombesin for 45 min resulted in time-dependent dissociation of specifically bound tracer to about 40% of the maximal equilibrium binding. Analysis of saturable equilibrium binding yielded a best fit to a one-site model of high affinity binding sites with an apparent Kd of 85 +/- 14 pM and a Bmax of 231,000 +/- 71,000 receptors/gastrin cell. Nonradioactive [Tyr4]-bombesin and related analogs inhibited the specific binding of the tracer in a dose-related manner. The rank order of potency, determined at the IC50, of [Tyr4]-bombesin and related analogs for inhibition of specific binding was bombesin greater than [Tyr4]-bombesin = hGRP-27 greater than GRP-10 greater than ranatensin much greater than neuromedin B. Cholecystokinin, somatostatin, substance K, and kassinin each tested at a concentration of 1 microM did not inhibit bombesin binding.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMedDate not supplied

Characterization of peptide YY receptors in rabbit colonic mucosa.

Quantitative receptor autoradiography localized a high-affinity binding site for 125I-peptide YY to the mucosa in rabbit distal colon. Scatchard binding analysis revealed a single-affinity binding site (KD = 0.29 nM) with binding specificity similar to other peptide YY-preferring receptors (peptide YY > or = neuropeptide Y >> pancreatic polypeptide). Radioligand binding studies using colonic mucosal membranes confirmed high-affinity peptide YY binding sites (KD = 0.26 nM) with time, temperature, and protein dependence, as well as saturability characteristic of receptor-ligand binding. Selective peptide analogues showed a subpopulation of these 125I-peptide YY binding sites to resemble the Y1-type neuropeptide Y receptor. Peptide YY may exert local antisecretory effects on the colonic epithelium via these binding sites.

Animals↗
PubMed1994

Gastric inhibitory polypeptide (GIP) binding sites in rat brain.

Synthetic porcine gastric inhibitory polypeptide (GIP) was iodinated and purified by reverse-phase HPLC and used to localize saturable [125I]GIP binding sites by radioligand binding to frozen sections of rat brain followed by autoradiography. Saturable [125I]GIP binding sites were expressed in several brain regions including cerebral cortex, anterior olfactory nucleus, lateral septal nucleus, subiculum, inferior colliculus, and inferior olive. Saturable [125I]GIP binding was time dependent, reversible, high affinity, and specific for GIP. Scatchard analysis of equilibrium binding resulted in an estimated dissociation constant (Kd) of 16-62 pM for the rat brain [125I]GIP binding sites. Peptides with amino acid sequences similar to GIP such as secretin, vasoactive intestinal polypeptide (VIP), glucagon, and peptide histidine isoleucine (PHI) only partially inhibited saturable [125I]GIP binding at concentrations approximately 10,000-100,000-fold higher than GIP. Saturable [125I]GIP binding was not observed in other rat organs surveyed such as spinal cord, pituitary, stomach, small intestine, colon, pancreas, liver, heart, or skeletal muscle. We conclude that a saturable [125I]GIP binding site with the pharmacological properties of an authentic GIP receptor is expressed in certain regions of the rat brain.

Animals↗