Biomedical subjects

Surajlal Unniappan

Publications and source records attributed to Surajlal Unniappan.

3 recordsLinked to original sources

PubMed2003

Characterization of complementary deoxyribonucleic acids encoding preprogalanin and its alternative splice variants in the goldfish.

This paper reports the identification of five preprogalanin complementary deoxyribonucleic acids encoding preprogalanin peptides in the goldfish. Preprogalanin 1A, 1B and 1C are encoded in galanin gene 1 and 2A and 2B are encoded in gene 2. Preprogalanin 1B and 2B have a 24 amino acids insert in the mature peptide region and form 1C has a deletion of 23 amino acids in the middle of the galanin message associated peptide region. The mature peptides from the preprogalanin 1A and 1C are 29 amino acids. However, the mature peptide is 31 amino acids from preprogalanin 2A, 53 amino acids from 1B and 55 amino acids from 2B. The physiological significance of multiple forms of galanin peptide is unknown. Organization of galanin gene 1, which is similar to the mammalian galanin gene has been identified. Expression of preprogalanin messenger ribonucleic acids was widely detected in goldfish brain and several peripheral tissues.

Alternative Splicing↗

PubMed2003

Endogenous hypothalamic somatostatins differentially regulate growth hormone secretion from goldfish pituitary somatotropes in vitro.

Using Southern blot analysis of RT-PCR products, mRNA for three different somatostatin (SS) precursors (PSS-I, -II, and -III), which encode for SS(14), goldfish brain (gb)SS(28), and [Pro(2)]SS(14), respectively, were detected in goldfish hypothalamus. PSS-I and -II mRNA, but not PSS-III mRNA, were also detected in cultured pituitary cells. We subsequently examined the effects of the mature peptides, SS(14), gbSS(28), and [Pro(2)]SS(14), on somatotrope signaling and GH secretion. The gbSS(28) was more potent than either SS(14) or [Pro(2)]SS(14) in reducing basal GH release but was the least effective in reducing basal cellular cAMP. The ability of SS(14), [Pro(2)]SS(14), and gbSS(28) to attenuate GH responses to GnRH were comparable. However, gbSS(28) was less effective than SS(14) and [Pro(2)]SS(14) in diminishing dopamine- and pituitary adenylate cyclase-activating polypeptide-stimulated GH release, as well as GH release resulting from the activation of their underlying signaling cascades. In contrast, the actions of a different 28-amino-acid SS, mammalian SS(28), were more similar to those of SS(14) and [Pro(2)]SS(14). We conclude that, in goldfish, SSs differentially couple to the intracellular cascades regulating GH secretion from pituitary somatotropes. This raises the possibility that such differences may allow for the selective regulation of various aspects of somatotrope function by different SS peptides.

Animals↗

PubMed2002

Goldfish ghrelin: molecular characterization of the complementary deoxyribonucleic acid, partial gene structure and evidence for its stimulatory role in food intake.

Complementary deoxyribonucleic acid (cDNA) encoding goldfish preproghrelin was identified using rapid amplification of the cDNA ends (RACE) and reverse transcription (RT)-polymerase chain reaction (PCR). The 490 bp cDNA encodes a 103 amino acid preproghrelin which has a 26 amino acid signal region, 19 amino acid mature peptide and a 55 amino acid C-terminal peptide region. The mature peptide region of goldfish ghrelin has two putative cleavage sites and amidation signals (GRR); one after 12 amino acids and the other after 19 amino acids. The serine (S) in the second amino acid position in the "active core" of ghrelin is substituted with threonine (T). The goldfish ghrelin gene has four exons and three short introns and resembles the human ghrelin gene. Ghrelin messenger RNA (mRNA) expression was detected in the brain, pituitary, intestine, liver, spleen and gill by RT-PCR followed by Southern blot analysis, and in the intestine by Northern blot. Intracerebroventricular (ICV) injection of n-octanoylated goldfish ghrelin (1-19) stimulates food intake in goldfish.

Amino Acid Sequence↗