Bombesin-like peptide in hypothalamus: Chemical and immunological characterization

Villarreal, Jose; Brown, Marvin R.

doi:10.1016/0024-3205(78)90653-7

Cited by 90 publications

(18 citation statements)

References 7 publications

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“…This peptide is an active molecule known to affect smooth muscle contraction of a number of organ systems, including the lung (3,15,34,35).…”

Section: Speculationmentioning

confidence: 99%

“…A bombesin-like peptide is present in both mammalian brain and gut derivatives (3,7,34,35). This peptide is a physiologically active molecule, which affects smooth muscle contraction in a number of organ systems; stimulates gastric acid, cholecystokinin and exocrine pancreatic secretion; and centrally mediaies alterations in t h e r m~i e~u l a t i o n and glucose homeostask (3,15,34,35). Mammalian peptides having bombesin immunoreactivity and physiologic effects appear to be larger than the amphibian peptide (3,7,35).…”

Section: Weeks Monthsmentioning

confidence: 99%

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Pulmonary Neuroendocrine Cells in Hyaline Membrane Disease and Bronchopulmonary Dysplasia

et al. 1982

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Summary munoreactivity (2). Bombesin, a 14 amino acid peptide, is aThe number and distribution of bombesin immunoreactive pulmonary neuroendocrine cells (PNEC) in fetuses and infants up to 6 months of age was determined on postmortem lung specimens. Individual cells and clusters of cells (neuroepithelial bodies) were found in airways of all sizes, although greater than 95% of the positive cells were located in bronchioles, terminal bronchioles, and respiratory bronchioles. These infants were separated into two groups. In control infants, who died primarily from noncardiopulmonary causes, bombsin immunoreactive neuroendocrine cells were identified throughout the latter half of gestation. As gestation advanced, progressively more positive bronchioles/cm2 of lung tissue and cells/bronchiole were identified. In these control infants, the number of positive bronchioles/cm2 and cells/bronchiole were at the highest level at or near the time of delivery and then gradually declined throughout the first 6 months of life. In contrast, infants who died of acute hyaline membrane disease (1-7 days of life) or bronchiopulmonary dysplasia (2 wk to 6 months of life) demonstrated marked differences in the number of identifiable bombesin immunoreactive neuroendocrine cells when compared to control infants. In early hyaline membrane disease, the number of positive bronchioles/cm2 and cells/bronchiole was markedly decreased. During the transition to chronic bronchopulmonary dysplasia, there appeared to be a marked increase in the number of bombesin immunoreactive cells. The peak number of cells occurred a t 2-3 months of life, when substantially more bombesin-immunoreactive cells could be identified in children with bronchopulmonary dysplasia than control infants of similar age.

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“…This peptide is an active molecule known to affect smooth muscle contraction of a number of organ systems, including the lung (3,15,34,35).…”

Section: Speculationmentioning

confidence: 99%

Section: Weeks Monthsmentioning

confidence: 99%

Pulmonary Neuroendocrine Cells in Hyaline Membrane Disease and Bronchopulmonary Dysplasia

et al. 1982

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“…Immunoreactivity to bombesin, an amphibian tetradecapeptide (1), is distributed throughout mammalian tissues (2)(3)(4)(5). Bombesin administered through intraperitoneal or intracisternal injection or intravenous infusion elicits diverse physiological effects in a variety of animal species, including humans (6)(7)(8)(9)(10)(11)(12).…”

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confidence: 99%

A bombesin immunoreactive peptide in milk.

Jahnke¹,

Lazarus²

1984

Proc. Natl. Acad. Sci. U.S.A.

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Immunoreactivity to the amphibian peptide bombesin was found in instant nonfat dry milk (ca. 0.7 ng/ml) and in the whey of whole or skim bovine milk (ca. 1.2 ng/ml) even after ultracentrifugation. The soluble immunoreactivity was associated with a peptide exhibiting the following characteristics: (i) parallel displacement in an immunoassay using an antiserum recognizing bombesin amino acid residues 5-8; (ii) separation from both gastrin-releasing peptide and amphibian bombesin by gel filtration-the approximate Mr was 3,200; (iii) denaturation in urea, reduction by dithiothreitol, and acetylation by iodoacetamide had no effect on its elution profile by gel-filtration chromatography and the aggregation of added bombesin to milk proteins or peptides was not observed; (iv) reversed-phase HPLC separated milk immunoreactivity from gastrin-releasing peptide and bombesin; (v) digestion by trypsin yielded a smaller immunoreactive peptide fragment, whereas nearly all immunoreactivity was lost by treatment with a-chymotrypsin; and (vi) the level of immunoreactivity was unaffected by boiling. These data show that milk is an exogenous source of bombesin-like immunoreactivity,, which may account for the increase of gastric acid and gastrointestinal hormone levels after the consumption of milk.Immunoreactivity to bombesin, an amphibian tetradecapeptide (1), is distributed throughout mammalian tissues (2-5). Bombesin administered through intraperitoneal or intracisternal injection or intravenous infusion elicits diverse physiological effects in a variety of animal species, including humans (6-12). These effects include hypertension (1, 6, 13, 14), satiety (for review, see ref. 15), change in sugar metabolism (16, 17), hypothermia (18), modulation of the level of many gastrointestinal-associated peptide hormones (6)(7)(8)(9)(10)(11)(12)(19)(20)(21)(22)(23)(24), and increase of gastric acid secretion (7,10,13,14,19,20). Bombesin also releases both gastrin and gastric acid from isolated fundic mucosa (25) and acts as a spasmogen in isolated smooth muscle preparations (1,6,13,14,26 MATERIALS AND METHODSMilk. Pasteurized skim and whole milk from several different local dairies were purchased 5-7 days before the expiration date. Instant nonfat dry milk was the product of several major companies and reconstituted according to the manu- [Tyr8]Bombesin and GRP were iodinated every 4-6 weeks as described (43). The production of the antiserum to bombesin has been described (44). Optimum RIA conditions, which were systematically determined, are as follows: 0.1 M sodium cacodylate, pH 5.6/bovine serum albumin (5 mg/ml)/125I-labeled [Tyr8]bombesin (or GRP) (2,500 cpm)/antiserum (final dilution, 1:4,000)/standard or test solution in a total vol of 100 ,ul. Nonionic (Triton X-100, Nonidet P-40) and ionic (sodium lauryl sulfate) detergents above 0.1% and chaotropic agents (urea, (Fig. 1). Other known peptides, such as physalaemin, neurotensin, and braAbbreviations: RIA, radioimmunoassay; GRP, gastrin-releasing peptide (bombesin-lik...

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“…The tetradecapeptide bombesin was isolated from frog skin by Anastasi et al (1971) and, subsequently, bombesin/gastrin-releasing peptide-like immunoreactivity (BN-GRP-LI) was found in the gastrointestinal tract (Polak et al, 1976;McDonald et al, 1978;, lung (Wharton et al, 1978), sympathetic ganglia (Schultzberg, 1980), brain Villareal and Brown, 1978;Moody et al, 1981a), and spinal cord (Moody et al, 1981b) of several mammalian species. The location of BN-GRP-LI in the rat brain and spinal cord using a rabbit antiserum against bombesin has been reported (Panula et al, 1982).…”

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Immunohistochemical localization of bombesin/gastrin-releasing peptide and substance P in primary sensory neurons

Panula¹,

Hadjiconstantinou²,

Yang³

et al. 1983

J. Neurosci.

146

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The existence of bombesin/gastrin-releasing peptide-like immunoreactivity (BN-GRP-LI) in rat sensory ganglia and spinal cord was confirmed using immunocytochemistry, gel filtration chromatography, and high performance liquid chromatography combined with radioimmunoassay. Immunohistochemical studies showed that in the spinal sensory ganglia of the rat about 5% of the neurons exhibited BN-GRP-LI, whereas about 20% of the neurons exhibited substance P-like immunoreactivity (SP-LI). The two immunoreactivities were found in different cells, but both were located in small ganglion cells. In the posterior horn of the spinal cord, BN-GRP-LI and SP-LI were located in the superficial layers, and this distribution was different from that of Met5-enkephalin-like immunoreactivity.The results are in agreement with the concept that there is a primary sensory pathway from the sensory ganglia to the spinal cord which contains BN-GRP-LI and that these neurons are separate from those containing substance P. In extracts prepared from spinal ganglia, two molecular weight forms of BN-GRP-LI were found using gel filtration chromatography. The high molecular weight form coeluted with porcine GRP and the low molecular weight form was smaller than bombesin. The low molecular weight BN-GRP-LI extracted from spinal cord was more hydrophilic than bombesin or ranatensin.

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Bombesin-like peptide in hypothalamus: Chemical and immunological characterization

Cited by 90 publications

References 7 publications

Pulmonary Neuroendocrine Cells in Hyaline Membrane Disease and Bronchopulmonary Dysplasia

Pulmonary Neuroendocrine Cells in Hyaline Membrane Disease and Bronchopulmonary Dysplasia

A bombesin immunoreactive peptide in milk.

Immunohistochemical localization of bombesin/gastrin-releasing peptide and substance P in primary sensory neurons

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