Disease relevance of Neuromedin B

• The mammalian bombesin-like peptides gastrin-releasing peptide (GRP) and neuromedin B regulate numerous and varied cell physiologic processes in various cell types and have also been implicated as autocrine growth factors influencing the pathogenesis and progression of human small cell lung carcinomas [1].
• Neuromedin B is present in lung cancer cell lines [2].
• Furthermore, addition of neuromedin B to Rat-1 cells transfected with the neuromedin B preferring receptor also activated p42(mapk) and p74(raf-1) in a PKC-independent and pertussis toxin-insensitive manner [3].
• Activation of neuromedin B-preferring bombesin receptors on rat glioblastoma C-6 cells increases cellular Ca2+ and phosphoinositides [4].
• The distributions of three novel peptides, 7B2, neuromedin B, and neuromedin U, in rat, mouse, and human pituitaries, rat hypothalamus, and 30 human pituitary tumors were investigated with immunocytochemistry [5].

Psychiatry related information on Neuromedin B

• Similar administration of neuromedin B had a biphasic effect; there was a dose-dependent decrease in reaction time lasting about 6 min followed by a delayed increase in reaction time to above control values at 31-46 min [6].

High impact information on Neuromedin B

• RESULTS: Neuromedin B and GRP receptor mRNAs were detected in human and rabbit colonic smooth muscle cells [7].
• Quantitative ligand displacement analysis using various unlabeled GRPr agonists shows a rank order of potency characteristic of the GRPr: bombesin > or = GRP > > neuromedin B [8].
• The relative rank potency of bombesin-like peptides for this receptor was [Phe13]bombesin > [Leu13]bombesin > GRP > neuromedin B [9].
• The predicted end product resembles neuromedin B, which was originally isolated from mammalian spinal cord [10].
• Neuromedin B (NB), a bombesin-like peptide, was first isolated from porcine spinal cord and subsequently found in the central nervous systems of rat, cat, and human [11].

Chemical compound and disease context of Neuromedin B

• Therefore, to further examine the possible function of these peptides in the spinal cord, the present study compares the effects of intrathecal administration of bombesin, neuromedin C and neuromedin B on reaction time in the tail flick test in the rat [6].
• The effects of neuromedin B (NMB) on C6 glioma cells were investigated [12].

Biological context of Neuromedin B

• Production of neuromedin B and neuromedin B gene expression in human lung tumor cell lines [13].
• The cDNA of the human neuromedin B gene (NMB) mapped to 15q11-qter recognizes an XbaI RFLP [14].
• This hormone action involved a significant upregulation of 1080 genes (e.g., neuromedin B), and a significant downregulation of 518 genes (e.g., small proline-rich protein 2A) [15].
• These results suggest an independent role for neuromedin B receptors in suppression of food intake by bombesin-like peptides and demonstrate the utility of this group of antagonists for in vivo experiments [16].
• We have previously demonstrated the presence of two distinct bombesin receptor subtypes in the rat CNS and distinguished them as bombesin/gastrin-releasing peptide (BBS/GRP) and neuromedin B (NMB)-preferring binding sites [17].

Anatomical context of Neuromedin B

• The bombesin-like peptides gastrin releasing peptide (GRP) and neuromedin B are found in the submucosal and myenteric plexuses of the human gastrointestinal tract [18].
• The receptor that interacts with the mammalian bombesin-related peptide neuromedin B (NMB) is ubiquitous in the gastrointestinal tract and central nervous system [19].
• Incubation of oocytes in the phospholipase C inhibitor U73122 or the protein kinase C (PKC) inhibitors chelerythrine and staurosporine significantly reduced the inhibition of GIRK currents by neuromedin B, whereas the Ca2+ chelator, BAPTA-AM had no effect [20].
• Localization of 7B2, neuromedin B, and neuromedin U in specific cell types of rat, mouse, and human pituitary, in rat hypothalamus, and in 30 human pituitary and extrapituitary tumors [5].
• Evidence for neuromedin-B synthesis in the rat anterior pituitary gland [21].

Associations of Neuromedin B with other chemical compounds

• Neuromedin B (NMB), the mammalian counterpart of amphibian ranatensin, has been shown to be a mitogen for SCLC cell lines in vitro [13].
• Hypothalamic concentrations of the other six peptides examined (bombesin, galanin, neuromedin B, substance P, somatostatin, and vasoactive intestinal peptide) did not differ significantly between STZ-D and control groups at any time [22].
• 6. The results of the present study demonstrate that bombesin and the structurally related peptides gastrin-releasing peptide (GRP) and neuromedin B depolarized a subpopulation of raphe 5-HT neurones by acting on a postsynaptically located receptor linked to potassium channels [23].
• In contrast, 125I-Tyr4 bombesin binding was not displaced by neuromedin B, somatostatin, bradykinin and insulin [24].
• Role of neuromedin B in the in vitro thyrotropin release in response to thyrotropin-releasing hormone from anterior pituitaries of eu-, hypo-, and hyperthyroid rats [25].

Gene context of Neuromedin B

• Neuromedin B (NMB) is one of the bombesin (BN)-related peptides in mammals [26].
• In all of the cases, the receptors corresponded to the GRP receptor subtype of bombesin receptors, having high affinity for GRP and bombesin and lower affinity for neuromedin B [27].
• Four amino acid residues are critical for high affinity binding of neuromedin B to the neuromedin B receptor [28].
• The fifth transmembrane segment of the neuromedin B receptor is critical for high affinity neuromedin B binding [29].
• The lysosomal degradation of neuromedin B is dependent on tripeptidyl peptidase-I: evidence for the impairment of neuropeptide degradation in late-infantile neuronal ceroid lipofuscinosis [30].

Analytical, diagnostic and therapeutic context of Neuromedin B

• Molecular cloning of cDNAs encoding the human bombesin-like peptide neuromedin B. Chromosomal localization and comparison to cDNAs encoding its amphibian homolog ranatensin [31].
• To examine this hypothesis, we have used Northern blotting to demonstrate that neuromedin-B is present in the anterior pituitary as a result of local synthesis and have examined the effects of endocrine manipulations on its mRNA and immunoreactive peptide content [21].
• The distribution and localization of neuromedin B, a novel bombesin-like decapeptide isolated from porcine spinal cord, was investigated by newly established radioimmunoassay and immunocytochemistry in the pig, cat and rat spinal cord [32].
• Reverse phase high pressure liquid chromatography showed that material corresponding to the later peak was eluted in the exact position of synthetic porcine neuromedin B, whereas the larger molecular size material from the earlier peak was more hydrophobic in nature [33].
• Prior to measurements of the tissue contents, immunoreactive neuromedin B and C were characterized by gel-filtration and high performance liquid chromatography [34].

References