Disease relevance of Ranatensin

• GRP, the mammalian homolog of bombesin and its receptor, as well as NMB, the mammalian homolog of ranatensin, are expressed in human neoplasms and, in particular, in small cell lung carcinomas (SCLC) [1].

High impact information on Ranatensin

• The low molecular weight BN-GRP-LI extracted from spinal cord was more hydrophilic than bombesin or ranatensin [2].
• Sequence homology showed that the fGRP precursor is more homology showed that the fGRP precursor is more closely related to the mammalian GRP precursors than to either the frog bombesin or frog ranatensin precursors [3].
• The amidated decapeptide neuromedin B (NMB) is the mammalian homolog of the amphibian bombesin-like peptide ranatensin. cDNAs encoding human neuromedin B and amphibian ranatensin were isolated from human hypothalamic and Rana pipiens skin libraries, respectively [4].
• Phylogenetic analysis of bombesin-like peptide prohormone sequences showed that the phyllolitorin prohormones are much more closely related to the bombesin and ranatensin prohormones than to the GRP and NMB prohormones [5].
• It is concluded that bombesin- and ranatensin-like peptides have a stimulatory effect on GH and PRL release at the pituitary level [6].

Biological context of Ranatensin

• Antibodies specific for the carboxyl-terminal regions of bombesin and of ranatensin were used to study the tissue distribution of substances immunochemically similar to these two peptides in three amphibian species [7].
• 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 [8].
• Molecular biology of bombesin-like peptides. Comparison of cDNAs encoding human gastrin-releasing peptide, human neuromedin B, and amphibian ranatensin [9].

Anatomical context of Ranatensin

• Neuromedin B, a mammalian decapeptide which shares homology with the carboxyl terminal fragment of ranatensin R and bombesin, injected intracisternally (880 pmol) did not modify gastric acid secretion stimulated either by pylorus ligation in conscious rats or by pentagastrin infusion in urethane-anesthetized rats [10].
• It is concluded that ranatensin-like peptides are not confined to the skin and can be included as central nervous system neuropeptides in amphibians [7].
• One of these peptides (PG-L) was of the bombesin family and may be considered an N-elongation of the litorin/ranatensin molecule, with which it shares an identical spectrum of activity on isolated smooth muscle preparations [11].
• The studies on the active peptide in the skin of Rana rugosa. II. The structure of ranatensin-R, the new ranatensin analogue, and granuliberin-R, the new mast cell degranulating peptide [12].
• High-to-moderate concentrations of BN/GRP are present in the rat hypothalamus and thalamus, whereas moderate-to-high densities of neuromedin B and ranatensin-like peptides are present in the olfactory bulb and hippocampus, as well as in the hypothalamus and thalamus [13].

Associations of Ranatensin with other chemical compounds

• Molecular cloning of cDNAs encoding the human bombesin-like peptide neuromedin B. Chromosomal localization and comparison to cDNAs encoding its amphibian homolog ranatensin [4].
• The lengths of incubation time required to produce approximately 90% degradation of peptide immunoreactivity varied across peptides from less than 5 min (SP) to more than 60 min (BN and RT) [14].

Gene context of Ranatensin

• Sequence analysis revealed that NMB is encoded in a 76-amino acid precursor and ranatensin in an 82-amino acid precursor [4].
• Biochemical and histochemical characterization of ranatensin immunoreactive peptides in rat brain: lack of coexistence with bombesin/GRP [15].

Analytical, diagnostic and therapeutic context of Ranatensin

• By radioimmunoassay, endogenous BN/GRP, neuromedin B, and ranatensin-like peptides are present in the rat brain [13].

References