<i>Lampetra fluviatilis</i>Neurotrophin Homolog, Descendant of a Neurotrophin Ancestor, Discloses the Early Molecular Evolution of Neurotrophins in the Vertebrate Subphylum

Hallböök, Finn; Lundin, Lars‐Gustav; Kullander, Klas

doi:10.1523/jneurosci.18-21-08700.1998

Cited by 57 publications

(54 citation statements)

References 58 publications

(48 reference statements)

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“…In high vertebrates BDNF and NT-4 are the preferred ligands for TrkB whereas NT-3 mainly binds to TrkC (Lewin and Barde, 1996). Interestingly the homologues for both groups of ligands have also been characterized in teleosts (see Hallböök et al, 1998 for references). They include BDNF-like, (Hashimoto and Heinrich, 1997), NT-4 (Götz and Schartl, 1994), and NT-7 (Lai et al, 1998;Nilsson et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

Co-localization of Trk neurotrophin receptors and regulatory peptides in the endocrine cells of the teleostean stomach

et al. 1999

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Recently it has been observed that a subpopulation of gut endocrine cells in vertebrates express Trk-like proteins, suggesting that neurotrophins could regulate the synthesis and storage of amines and peptides of these cells. Nevertheless, the peptides and amines present in the endocrine cells that express Trks have not been characterized. In this study we used immunohistochemistry to investigate the occurrence of Trk-like proteins (TrkA-like, TrkB-like and TrkC-like) and the possible co-localization of these with peptides and/or biogenic amines in the endocrine cells of the stomach of three teleost (bass, gilt-head and scorpionfish). No TrkA-like immunoreactivity (IR) was detected in the stomach of these species, whereas TrkB-like IR and TrkC-like IR were observed in numerous cells of the gastric epithelium. TrkB-like immunoreactive cells were present in all three species examined, and were particularly abundant in the blind sac. Conversely, TrkC-like immunoreactive cells were found only in the bass stomach, apparently co-localized with TrkB-like IR. TrkB-like IR was found co-localized with somatostatin IR in scorpionfish, and with somatostatin and CGRP IR in gilt-head and bass. Gastric endocrine cells expressing 5-HT, glucagon, insulin, met-, leu-enkephalin, substance P, PYY, VIP, CCK, NPY, bombesin and motilin were unreactive for Trk-like proteins. The present results provide direct evidence for the occurrence of Trk-like neurotrophin receptor proteins in a subpopulation of the teleostean gastric endocrine cells and suggest that neurotrophins could regulate, as in neurons, the expression of some neuropeptides such as somatostatin and CGRP. Anat Rec 256: [219][220][221][222][223][224][225][226] 1999.

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Section: Discussionmentioning

confidence: 99%

Co-localization of Trk neurotrophin receptors and regulatory peptides in the endocrine cells of the teleostean stomach

et al. 1999

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“…Mammals seem to be the only vertebrates in which the ear expresses an additional neurotrophin, NT-3, in significant amounts (Pirvola et al, 1997;Hallbook et al, 1998). Our previous data have shown that expression of NT-3 in the basal, high-frequency turn of the cochlea of mammals is followed by a delayed upregulation of BDNF in this turn .…”

Section: The Pattern Of Experimentally Rerouted Fibers Resembles Pattmentioning

confidence: 94%

NT-3 Replacement with Brain-Derived Neurotrophic Factor Redirects Vestibular Nerve Fibers to the Cochlea

Tessarollo¹,

Coppola²,

Fritzsch³

2004

J. Neurosci.

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“…Porcine NPY, p[Leu31,Pro34]NPY, the series of amino terminally truncated pig NPY peptides pNPY , pNPY 13236 , pNPY [18][19][20][21][22][23][24][25][26][27][28][29][30][31][32][33][34][35][36] , pNPY [25][26][27][28][29][30][31][32][33][34][35][36] , pNPY [26][27][28][29][30][31][32][33][34][35][36] , and bovine PP were from Bachem (King of Prussia, PA, USA); p[D-Trp32]NPY was from Peninsula Laboratories Inc. Lamprey peptides were synthesized as described below. BIBP3226 was kindly provided by K. Thomae GmBH, Biberach, Germany.…”

Section: Peptides and Nonpeptidic Antagonistsmentioning

confidence: 99%

A neuropeptide Y receptor Y1‐subfamily gene from an agnathan, the European river lamprey

Salaneck

Fredriksson

Larson

et al. 2001

European Journal of Biochemistry

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We report here the isolation and functional expression of a neuropeptide Y (NPY) receptor from the river lamprey, Lampetra fluviatilis. The receptor displays < 50% aminoacid sequence identity to all previously cloned Y1-subfamily receptors including Y1, Y4, and y6 and the teleost subtypes Ya, Yb and Yc. Phylogenetic analyses point to a closer relationship with Y4 and Ya/b/c suggesting that the lamprey receptor could possibly represent a pro-orthologue of some or all of those gnathostome receptors. Our results support the notion that the Y1 subfamily increased in number by genome or large-scale chromosome duplications, one of which may have taken place prior to the divergence of lampreys and gnathostomes whereas the second duplication probably occurred in the gnathostome lineage after this split. Functional expression of the lamprey receptor in a cell line facilitated specific binding of the three endogenous lamprey peptides NPY, peptide YY and peptide MY with picomolar affinities. Binding studies with a large panel of NPY analogues revealed indiscriminate binding properties similar to those of another nonselective Y1-subfamily receptor, zebrafish Ya. RT-PCR detected receptor mRNA in the central nervous system as well as in several peripheral organs suggesting diverse functions. This lamprey receptor is evolutionarily the most distant NPY receptor that clearly belongs to the Y1 subfamily as defined in mammals, which shows that subtypes Y2 and Y5 arose even earlier in evolution.Keywords: NPY; PYY; evolution; gene duplication; G-protein coupled receptor; Lamprey.Neuropeptide Y (NPY), peptide YY (PYY) and pancreatic polypeptide (PP) are closely related 36-amino-acid neuroendocrine peptides found in all tetrapods. NPY and PYY have also been found in nontetrapod gnathostomes as well as agnathans [1]. These peptides have a large number of physiological effects in the nervous system, the circulatory system and the gastrointestinal tract. NPY is most abundant in the nervous system and stimulates food intake, regulates blood pressure and influences release of pituitary peptides [2,3]. PYY and PP are found in the gastrointestinal tract and are released upon food intake. In nontetrapod vertebrates PYY is also present in the central nervous system (CNS) [4,5]. PY, a PYY-like peptide is only found in certain teleost fishes, and appears to have arisen from a fairly recent gene duplication [1,6]. In the river lamprey, Lampetra fluviatilis, the ancestral PYY gene appears to have undergone a separate gene duplication, resulting in peptide YY and peptide MY [4,7].The effects of the NPY family of peptides are relayed by a family of G-protein coupled receptors [8 -10]. Five receptors have been cloned in mammals; Y1, Y2, Y4, Y5 and y6, most of which have high affinities for NPY and PYY. Y4 is the only receptor for which PP has higher affinity than NPY or PYY. The y6 gene still lacks a physiological correlate, hence it is designated with a lower case 'y'. In humans and other primates, the y6 gene is a pseudogene. Sequence comparisons ...

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Lampetra fluviatilisNeurotrophin Homolog, Descendant of a Neurotrophin Ancestor, Discloses the Early Molecular Evolution of Neurotrophins in the Vertebrate Subphylum

Cited by 57 publications

References 58 publications

Co-localization of Trk neurotrophin receptors and regulatory peptides in the endocrine cells of the teleostean stomach

Co-localization of Trk neurotrophin receptors and regulatory peptides in the endocrine cells of the teleostean stomach

NT-3 Replacement with Brain-Derived Neurotrophic Factor Redirects Vestibular Nerve Fibers to the Cochlea

A neuropeptide Y receptor Y1‐subfamily gene from an agnathan, the European river lamprey

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