Special evolution of neurohypophysial hormones in cartilaginous fishes: asvatocin and phasvatocin, two oxytocin-like peptides isolated from the spotted dogfish (Scyliorhinus caniculus).

Chauvet, Jacqueline; Rouillé, Yves; Chauveau, Christophe; Chauvet, M.T.; Acher, Roger

doi:10.1073/pnas.91.23.11266

Cited by 21 publications

(8 citation statements)

References 30 publications

(22 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Unlike the evolutionary stable vasopressin lineage, oxytocinlike peptides are very diverse in this primitive group of the vertebrates (7). To none of these peptides has a function been assigned, and they have very poor uterotonic activity in mammals (46). Hence, it will be of interest to examine whether functional receptors exist for these peptides.…”

Section: Discussionmentioning

confidence: 99%

Co-evolution of Ligand-Receptor Pairs in the Vasopressin/Oxytocin Superfamily of Bioactive Peptides

Kesteren¹,

Tensen

Smit³

et al. 1996

Journal of Biological Chemistry

104

View full text Add to dashboard Cite

In order to understand the molecular mechanisms that underlie the co-evolution of related yet functionally distinct peptide-receptor pairs, we study receptors for the vasopressin-related peptide Lys-conopressin in the mollusc Lymnaea stagnalis. In addition to a previously cloned Lys-conopressin receptor (LSCPR1), we have now identified a novel Lys-conopressin receptor subtype, named LSCPR2. The two receptors have a differential distribution in the reproductive organs and the brain, which suggests that they are involved in the control of distinct aspects of reproduction and mediate transmitter-like and/or modulatory effects of Lysconopressin on different types of central neurons. In contrast to LSCPR1, LSCPR2 is maximally activated by both Lys-conopressin and Ile-conopressin, an oxytocinlike synthetic analog of Lys-conopressin. Together with a study of the phylogenetic relationships of Lysconopressin receptors and their vertebrate counterparts, these data suggest that LSCPR2 represents an ancestral receptor to the vasopressin/oxytocin receptor family in the vertebrates. Based on our findings, we provide a theory of the molecular co-evolution of the functionally distinct ligand-receptor pairs of the vasopressin/oxytocin superfamily of bioactive peptides.Peptide receptors form an important subclass of the otherwise diverse superfamily of G protein-coupled 1 receptors that all have a seven-transmembrane segment topology in common (for review, see Ref. 1). This receptor type forms a component of a modular system for the transduction of extracellular signals across the cell membrane and the subsequent conversion of these signals to an intracellular second messenger pathway via the activation of heterotrimeric G proteins (for review, see Ref.2). Molecular evolutionary mechanisms such as gene duplication and subsequent mutation of the resulting genes have resulted in the formation of families of related yet distinct peptides (3) and peptide receptors (4). In the nervous and endocrine systems, many peptide isoforms bind to distinct receptor subtypes that mediate the specific cellular actions that underlie a large variety of behavioral and physiological processes. Peptide-receptor and receptor-effector interactions are of critical importance for peptide function, and many diseases are linked to malfunctions of these interactions (5). However, the great variety in structure of both peptides and receptors has hampered the development of a coherent theory explaining the molecular basis of co-evolution of specifically interacting peptide-receptor pairs. The vasopressin/oxytocin superfamily of peptides and their cognate receptors offer an attractive model for the study of specificity of peptide-receptor interactions and the co-evolution of related peptide-receptor pairs (6). These peptides and receptors occur throughout the entire animal kingdom (for review, see Ref. 7), allowing detailed comparison of their structural features and experimental testing of putative specificity determinants. The peptides of the superfamily are s...

show abstract

Section: Discussionmentioning

confidence: 99%

Co-evolution of Ligand-Receptor Pairs in the Vasopressin/Oxytocin Superfamily of Bioactive Peptides

Kesteren¹,

Tensen

Smit³

et al. 1996

Journal of Biological Chemistry

104

View full text Add to dashboard Cite

show abstract

“…In some groups of vertebrates, more than two peptides have been reported. In the cartilaginous fish, a host of various neutral peptides are present in different species . Amongst tetrapods, the duality of both basic and neutral hormone precursors has been reported in Metatheria .…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning and characterisation of an isotocin paralogue ([V8] isotocin) in catfishes (superorder Ostariophysi): Origin traced likely to the fish‐specific whole genome duplication

Banerjee

Chaube

Joy

2018

J Neuroendocrinology

View full text Add to dashboard Cite

The present study reports the molecular cloning of a previously uncharacterised neurohypophyseal nonapeptide precursor cDNA in two catfish species: Heteropneustes fossilis and Clarias batrachus. The deduced nonapeptide is CYISNCPVG ([V8] isotocin), which has not been reported in any vertebrate till date. Phylogenetic and conserved synteny analyses showed the gene to have originated from the isotocin precursor (pro‐it) gene by fish‐specific whole genome duplication (3R). The two isotocin lineages have been designated as pro‐ita (new gene) and pro‐itb (conventional it gene). All teleost groups may not possess both pro‐ita and pro‐itb and the pattern of losses/retention was found to be lineage‐specific. Quantitative reverse transcriptase‐polymerase chain reaction studies showed the expression of the pro‐ita gene in the brain and ovary of H. fossilis. In situ hybridisation studies localised the pro‐ita transcripts in the nucleus preopticus of the hypothalamus and the follicular layer (theca‐granulosa) of oocytes, comprising tissues in which pro‐itb and vasotocin precursor (pro‐vt) mRNA expression was previously reported. The transcript levels varied with the reproductive stage and a high abundance was found in both brain and ovary during the breeding phase. The substitution of valine in place of isoleucine at the eighth position in Ita may have modified the ligand‐receptor interaction, leading to sub‐functionalisation and the retention of the gene in catfishes.

show abstract

“…In addition to AVT, the European lesserspotted dogfish Scyliorhinus canicula also has the oxytocinlike peptides, phasvatocin and asvatocin, which occur in roughly equal molar amounts in the pituitary (13). AVT is also present in the pituitary in a proportional amount that is lower by about a factor of 20 (13). This low pituitary level was thought to reflect a permanent secretion of AVT (2).…”

mentioning

confidence: 99%

“…It has been characterized in all elasmobranchs examined to date (1,2). In addition to AVT, the European lesserspotted dogfish Scyliorhinus canicula also has the oxytocinlike peptides, phasvatocin and asvatocin, which occur in roughly equal molar amounts in the pituitary (13). AVT is also present in the pituitary in a proportional amount that is lower by about a factor of 20 (13).…”

mentioning

confidence: 99%

Development of an in situ perfused kidney preparation for elasmobranch fish: action of arginine vasotocin

Wells

Anderson

Hazon

2002

American Journal of Physiology-Regulatory, Integrative and Comp

View full text Add to dashboard Cite

Development of an in situ perfused kidney preparation for elasmobranch fish: action of arginine vasotocin. Am J Physiol Regulatory Integrative Comp Physiol 282: R1636-R1642, 2002 10.1152/ajpregu.00810.2000.-Acclimation of the European lesser-spotted dogfish Scyliorhinus canicula to reduced environmental salinity [85-70% seawater (SW)] induced a significant diuresis in addition to a significant decrease in plasma osmolality in vivo. The threshold for this diuresis was determined to be 85% SW. Therefore, S. canicula acclimated to 85% SW was selected for further study as a diuretic model in the development of an in situ perfused kidney preparation. The renal role of arginine vasotocin (AVT) in the in situ perfused trunk preparation was investigated. In SW, perfusion of 10 Ϫ9 and 10 Ϫ10 M AVT resulted in a glomerular antidiuresis and decreases in tubular transport maxima for glucose and perfusate flow. In 85% SW, 10 Ϫ10 M AVT had no significant effect on these renal parameters with the exception of transport maxima for glucose and perfusate flow. Tubular parameters remained unchanged by either 10 Ϫ9 or 10 Ϫ10 M AVT. The results demonstrate that the perfused kidney preparation was a viable tool for the investigation of renal parameters in elasmobranch fish and that AVT induced a glomerular antidiuresis.antidiuresis; seawater; Scyliorhinus canicula; dogfish; neurohypophysial hormones MARINE ELASMOBRANCHS MAINTAIN their plasma isoosmotic or slightly hyperosmotic to that of the surrounding environment, primarily due to the retention of urea (22). Plasma sodium and chloride concentrations are generally higher than those found in marine teleosts, but the fish still face a continuous influx of NaCl across semipermeable membranes, particularly the gills (18,20). Due to the plasma iso/hyperosmolality, some influx of water will occur and urea will be lost to the environment across permeable surfaces, along a concentration gradient. Elasmobranchs are not capable of producing a hyperosmotic urine with respect to body fluids, and the kidneys are not the major site of NaCl excretion (17). It appears that renal retention of urea may be a more important function for the kidney in elasmobranch fish (7).Arginine vasotocin (AVT), a homologue of arginine vasopressin (AVP) in mammals, is the major neurohypophysial peptide in lower vertebrates. It has been characterized in all elasmobranchs examined to date (1, 2). In addition to AVT, the European lesserspotted dogfish Scyliorhinus canicula also has the oxytocinlike peptides, phasvatocin and asvatocin, which occur in roughly equal molar amounts in the pituitary (13). AVT is also present in the pituitary in a proportional amount that is lower by about a factor of 20 (13). This low pituitary level was thought to reflect a permanent secretion of AVT (2). Although accurate levels of AVT have been measured in teleosts, the presence of additional neurohypophysial peptides in elasmobranchs and the potential for these to cross-react with the antiserum have meant that it has not been possible at...

show abstract

Special evolution of neurohypophysial hormones in cartilaginous fishes: asvatocin and phasvatocin, two oxytocin-like peptides isolated from the spotted dogfish (Scyliorhinus caniculus).

Cited by 21 publications

References 30 publications

Co-evolution of Ligand-Receptor Pairs in the Vasopressin/Oxytocin Superfamily of Bioactive Peptides

Co-evolution of Ligand-Receptor Pairs in the Vasopressin/Oxytocin Superfamily of Bioactive Peptides

Molecular cloning and characterisation of an isotocin paralogue ([V8] isotocin) in catfishes (superorder Ostariophysi): Origin traced likely to the fish‐specific whole genome duplication

Development of an in situ perfused kidney preparation for elasmobranch fish: action of arginine vasotocin

Contact Info

Product

Resources

About