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Biomedical subjects

J M Conlon

Publications and source records attributed to J M Conlon.

348 records · Page 20Linked to original sources
PubMedDate not supplied

Purification and primary structure of alligator neurotensin.

The gastrointestinal neurohormones of reptiles have been poorly characterized structurally. Neurotensin has been purified to apparent homogeneity from an extract of the small intestine of the alligator, Alligator mississipiensis. The primary structure of the peptide (pGlu-Leu-His-Val-Asn-Lys-Ala-Arg-Arg-Pro-Tyr-Ile-Leu) is identical to that of chicken neurotensin. The data provide further evidence for a close phylogenetic relationship between crocodilians and birds.

Alligators and Crocodiles↗
PubMedDate not supplied

Receptor binding profile of neuropeptide gamma and its fragments: comparison with the nonmammalian peptides carassin and ranakinin at three mammalian tachykinin receptors.

The tachykinin binding site preferences of neuropeptide gamma (NP gamma), its C-terminal fragments AcNP gamma(3-21), AcNP gamma(5-21), AcNP gamma(7-21), and AcNP gamma(9-21), other mammalian tachykinins, and the nonmammalian tachykinins ranakinin and carassin were examined in membrane binding competition studies. [125I]-Bolton-Hunter [Sar9,Met(O2)11]SP (BHSarSP), [125I]-neurokinin A (INKA) and [125I]-Bolton-Hunter scyliorhinin II (BHScyII) were used to investigate NK-1, NK-2, and NK-3 sites, in rat submandibular gland, gastric fundus, and brain, respectively. Elongation of the neurokinin A molecule does not appear to influence binding to rat tachykinin NK-1 and NK-2 binding sites. Ranakinin has affinity for the NK-1 and NK-2 site similar to that of substance P and neurokinin A, respectively, but has low affinity for the NK-3 site. Despite its structural similarities to neuropeptide gamma, carassin has only moderate affinity for rat tachykinin binding sites. Possession of an acidic residue at position 4 appears critical for binding to rat NK-2 sites.

Amino Acid Sequence↗
PubMedDate not supplied

Neuroendocrine peptides (NPY, GRP, VIP, somatostatin) from the brain and stomach of the alligator.

Despite the important position of the reptiles in phylogeny, relatively few regulatory peptides from reptilian species have been characterized structurally. Neuropeptide Y was isolated from the brain of the alligator, Alligator mississippiensis, and vasoactive intestinal polypeptide (VIP), gastrin-releasing peptide (GRP), its COOH-terminal decapeptide (GRP-10), and somatostatin-14 were isolated from the alligator stomach. The primary structures of NPY and somatostatin-14 are the same as the corresponding peptides from the human, whereas alligator VIP is identical to chicken VIP. The amino acid sequence of GRP (Ala-Pro-Ala-Pro-Ser-Gly-Gly-Gly-Ser-Ala10-Pro-Leu-Ala-Lys-Ile-Tyr -Pro-Arg-Gly-Ser20-His-Trp-Ala-Val-Gly-His-Leu-Met-NH2) contains an additional residue and six substitutions compared with chicken GRP, but alligator GRP-10 is the same as chicken GRP-10. Bombesin was not detected in the stomach extract. The data confirm that evolutionary pressure to conserve the amino acid sequence of NPY and somatostatin-14 has been very strong but demonstrate that pressure to conserve the complete primary structure of GRP has been less than that for other neuroendocrine peptides. The identity of chicken and alligator VIP is consistent with the known close phylogenetic relationship between crocodilians and birds.

Alligators and Crocodiles↗
PubMedDate not supplied

Isolation and structural characterization of calcitonin gene-related peptide from the brain and intestine of the frog, Rana ridibunda.

Calcitonin gene-related peptide (CGRP) was isolated in a single molecular form from an extract of the whole brain and from the small intestine of the European green frog, Rana ridibunda. The primary structure of the peptide was established as: Ala-Cys-Asn-Thr-Ala-Thr-Cys-Val-Thr-His10-Arg-Leu-Ala-Asp-Phe-Leu- Ser-Arg-Ser-Gly20-Gly-Met-Ala-Lys-Asn-Asn-Phe-Val-Pro-Thr30- Asn-Val-Gly-Ser-Ala-Phe-NH2. Frog CGRP shows only two amino acid substitutions (Val22-->Met and Gly23-->Ala) compared with chicken CGRP, as deduced from the nucleotide sequence of a cloned cDNA. The Asp14 residue, which leads to enhanced biological potency in chicken CGRP, is also present in the frog peptide. The data show that the structure of CGRP has been strongly conserved during evolution of the vertebrates.

Amino Acid Sequence↗