Peptide hormone degradation by a rat mast cell chymase-heparin complex

Jahnke, Gloria D.; Lazarus, Lawrence H.; DiAugustine, Richard P.; Soldato, Cathy M.; Erisman, M D

doi:10.1016/0024-3205(81)90333-7

Cited by 7 publications

(2 citation statements)

References 11 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Thus, the data suggest that bombesin residues 6 and 7 (asparagine and glutamine) exist in milk bombesin in the appropriate sequence. Furthermore, the recovery of immunoreactivity after boiling milk eliminates the possibility that a proteolytic enzyme was responsible for the parallel RIA curves (48). The quantity of bombesin immunoreactivity in a half-pint of milk (ca.…”

Section: Resultsmentioning

confidence: 99%

A bombesin immunoreactive peptide in milk.

Jahnke¹,

Lazarus²

1984

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

View full text Add to dashboard Cite

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...

show abstract

Section: Resultsmentioning

confidence: 99%

A bombesin immunoreactive peptide in milk.

Jahnke¹,

Lazarus²

1984

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

View full text Add to dashboard Cite

show abstract

“…However, it is important to consider that the qualitative identification of most of the lung peptides in tissue sections or in extracts has relied on cross-immunoreactivity with antisera to known polypeptides. Therefore, careful consideration is necessary when using immunocytochemical techniques or radioimmunoassays, since these methods may yield false positives or negatives (37,(149)(150)(151)(152). It is imperative that investigators employ various physicochemical procedures and bioassays, if possible, to verify the identity of unknown immunoreactive material with a known peptide.…”

Section: Neuroepithelial Bodiesmentioning

confidence: 99%

Neuroendocrinelike (small granule) epithelial cells of the lung.

DiAugustine¹,

Sonstegard²

1984

Environ Health Perspect

View full text Add to dashboard Cite

The presence of neuroendocrinelike epithelial cells in the lung of numerous species has been demonstrated by light and electron microscopy. Histochemical methods used to identify these cells have included staining with silver, amine-type fluorescence (APUD cell), periodic acid Schiff (PAS)-lead hematoxylin, and immunohistochemical localization of neuron-specific enolase. Cytoplasmic dense core vesicles (70-200 nm in diameter) have served as the major ultrastructural characteristic. Lung neuroendocrinelike cells have been shown to occur in fetal and adult mammals as solitary-type cells or as distinct organoids known as neuroepithelial bodies ( NEBs ). Although the frequency of both populations is considered low, solitary-type cells with dense-core granules can be found in as high as 5% of epithelial cells in the cricoid region of the guinea-pig larynx. The solitary cells can be found throughout the airways of mammals, whereas the NEBs are confined to the intrapulmonary airways. Unmyelinated fibers have been traced from the lamina propria and into the NEB, where they ramified between the component cells of the NEB. The function of lung neuroendocrinelike cells is not known, but morphological and cytochemical studies suggest that the NEBs are intrapulmonary chemoreceptors that can respond to changes in airway gas composition. Hypoxia or hypercapnia has been shown to decrease the amine cytofluorescence in these organoids and apparently to increase the exocytosis of dense core vesicles from the basal region of the cell. Immunohistochemical studies have suggested that some lung epithelial cells may contain a known neuropeptide(s), but further investigation is needed to confirm the presence of such compounds in lung neuroendocrinelike cells and their physiochemical properties. Apparent hyperplasia of lung neuroendocrinelike cells can occur readily in hamsters treated with diethylnitrosamine. It has been postulated that human lung tumors with endocrinelike properties, namely, bronchial carcinoids and lung small cell carcinomas, may originate from lung neuroendocrinelike cells. However, a more plausible explanation, based on cytokinetic studies of epithelial neuroendocrinelike cells in the lung and other organs, is that these cells originate from a nonneuroendocrine population. Interaction of such a progenitor cell population with selected carcinogens may lead to stimulation of the rate of normal differentiation or, alternately, to selection of an abnormal route of differentiation that possesses a neuroendocrine phenotype. Images FIGURE 1. FIGURE 2. FIGURE 3. FIGURE 4. FIGURE 5. FIGURE 6. FIGURE 7. FIGURE 8. FIGURE 9. FIGURE 10. FIGURE 11. FIGURE 12. FIGURE 13. FIGURE 14. FIGURE 15.

show abstract

Role of Histamine in the Actions of Neuropeptides and Local Hormones

Chahl¹

1991

Histamine and Histamine Antagonists

View full text Add to dashboard Cite

Peptide hormone degradation by a rat mast cell chymase-heparin complex

Cited by 7 publications

References 11 publications

A bombesin immunoreactive peptide in milk.

A bombesin immunoreactive peptide in milk.

Neuroendocrinelike (small granule) epithelial cells of the lung.

Role of Histamine in the Actions of Neuropeptides and Local Hormones

Contact Info

Product

Resources

About