Evolutionary implications of the cDNA sequence of the single lactate dehydrogenase of a lamprey.

Stock, David W.; Whitt, Gregory S.

doi:10.1073/pnas.89.5.1799

Cited by 19 publications

(10 citation statements)

References 49 publications

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“…A second round of gene duplication involved Ldh-B and gave rise to Ldh-B and Ldh-C . Several phylogenetic studies support this hypothesis of an original Ldh-A and Ldh-B gene duplication followed by more recent and independent origins of the Ldh-C genes in teleost fish, Xenopus laevis , pigeon and mammals [7,10,13]. A second school of thought suggests that the primordial vertebrate LDH was an LDH-C like enzyme.…”

Section: Discussionmentioning

confidence: 97%

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D- and L-lactate dehydrogenases during invertebrate evolution

et al. 2008

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BackgroundThe L-lactate and D-lactate dehydrogenases, which are involved in the reduction of pyruvate to L(-)-lactate and D(+)-lactate, belong to evolutionarily unrelated enzyme families. The genes encoding L-LDH have been used as a model for gene duplication due to the multiple paralogs found in eubacteria, archaebacteria, and eukaryotes. Phylogenetic studies have suggested that several gene duplication events led to the main isozymes of this gene family in chordates, but little is known about the evolution of L-Ldh in invertebrates. While most invertebrates preferentially oxidize L-lactic acid, several species of mollusks, a few arthropods and polychaetes were found to have exclusively D-LDH enzymatic activity. Therefore, it has been suggested that L-LDH and D-LDH are mutually exclusive. However, recent characterization of putative mammalian D-LDH with significant similarity to yeast proteins showing D-LDH activity suggests that at least mammals have the two naturally occurring forms of LDH specific to L- and D-lactate. This study describes the phylogenetic relationships of invertebrate L-LDH and D-LDH with special emphasis on crustaceans, and discusses gene duplication events during the evolution of L-Ldh.ResultsOur phylogenetic analyses of L-LDH in vertebrates are consistent with the general view that the main isozymes (LDH-A, LDH-B and LDH-C) evolved through a series of gene duplications after the vertebrates diverged from tunicates. We report several gene duplication events in the crustacean, Daphnia pulex, and the leech, Helobdella robusta. Several amino acid sequences with strong similarity to putative mammalian D-LDH and to yeast DLD1 with D-LDH activity were found in both vertebrates and invertebrates.ConclusionThe presence of both L-Ldh and D-Ldh genes in several chordates and invertebrates suggests that the two enzymatic forms are not necessarily mutually exclusive. Although, the evolution of L-Ldh has been punctuated by multiple events of gene duplication in both vertebrates and invertebrates, a shared evolutionary history of this gene in the two groups is apparent. Moreover, the high degree of sequence similarity among D-LDH amino acid sequences suggests that they share a common evolutionary history.

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Section: Discussionmentioning

confidence: 97%

“…For this reason the Ldh gene family has been used as a model for gene duplication in vertebrate evolution [8,10]. It is generally accepted that the Ldh genes of jawed vertebrates arose as a series of gene duplications in early vertebrate evolution, after the divergence of vertebrates from tunicates.…”

Section: Discussionmentioning

confidence: 99%

D- and L-lactate dehydrogenases during invertebrate evolution

et al. 2008

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“…Furthermore, sequence comparisons will help to elucidate evolutionary changes in the peptide-receptor interactions. The lampreys are a crucial class to study as they diverged from other vertebrates prior to a proposed large genome duplication event in the gnathostome lineage [36][37][38]. Secondly, the European river lamprey, L. fluviatilis, has already been well established as a model organism for neurobiological purposes [25].…”

Section: Discussionmentioning

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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“…We also investigated by histochemistry the distribution of LDH in imaginal leg discs before (third instar larval discs) and during leg morphogenesis (prepupal discs). Little staining is found in larval discs [Tsujibo et al, 1986], B [Sakai et al, 1987], and C [Millan et al, 1989]; LAMPR, lamprey [Stock and Whitt, 1992]; CELEG, the nematode, C. elegans [Tsoi and Li, 1994]; BACST, the bacterium B. stearothermophilus [Barstow et al, 1986]. Amino acids in the active site are shown in bold [Holbrook et al, 1975;Eventoff et al, 1977;Grau et al, 1981;Li et al, 1983].…”

Section: Developmental Expression Of Imp-l3 and Ldh Activitymentioning

confidence: 98%