A comparative survey of the RF-amide peptide superfamily (Record no. 3019041)

MARC details
000 -LEADER
fixed length control field 04587naaaa2200361uu 4500
001 - CONTROL NUMBER
control field https://directory.doabooks.org/handle/20.500.12854/43629
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20220714193858.0
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
International Standard Book Number 978-2-88919-729-3
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
International Standard Book Number 9782889197309
024 7# - OTHER STANDARD IDENTIFIER
Standard number or code 10.3389/978-2-88919-729-3
Terms of availability doi
041 0# - LANGUAGE CODE
Language code of text/sound track or separate title English
042 ## - AUTHENTICATION CODE
Authentication code dc
100 1# - MAIN ENTRY--PERSONAL NAME
Personal name Karine Rousseau
Relator code auth
9 (RLIN) 1620327
245 10 - TITLE STATEMENT
Title A comparative survey of the RF-amide peptide superfamily
260 ## - PUBLICATION, DISTRIBUTION, ETC. (IMPRINT)
Name of publisher, distributor, etc Frontiers Media SA
Date of publication, distribution, etc 2015
300 ## - PHYSICAL DESCRIPTION
Extent 1 electronic resource (160 p.)
506 0# - RESTRICTIONS ON ACCESS NOTE
Terms governing access Open Access
Source of term star
Standardized terminology for access restriction Unrestricted online access
520 ## - SUMMARY, ETC.
Summary, etc The discovery, twelve years ago, that the RF-amide peptide kisspeptin, acting via GPR54, is essential for the onset of puberty and reproduction, has been a major breakthrough in reproductive physiology. It has also put in front of the spotlights RF-amide peptides and allowed to revive research on this superfamily. The first member of this family to be characterized, in 1977, was the cardioexcitatory peptide, FMRFamide, isolated from the ganglia of the clam Macrocallista nimbosa. Since then, a large number of these peptides, designated after their C-terminal arginine (R) and amidated phenylalaline (F) residues, have been identified in representative species of all major phyla. By means of phylogenetic analyses, the superfamily of RFamide peptides has been divided into five families in vertebrates: kisspeptin, QFRP (including 26RFa), LPXRFa (including GnIH and RFRP), PQRFa (including NPFF) and PrRP. Recent data reveal that SIFamide-type neuropeptides in protostomian invertebrates and SALMFamide-type neuropeptides in deuterostomian invertebrates share a common evolutionary origin with vertebrate LPXRFa and PQRFa. Interestingly, in invertebrates as in vertebrates, multiple genes, as well as multiple mature peptides, are often present in a single species, questioning the need for such diversity in term of function. Comparative studies on non-mammalian vertebrates and invertebrates allow major advances in the knowledge of the evolutionary history of the RF-amide peptide superfamily. Such phylogenetical studies also contribute to improve classification and nomenclature of both peptides and receptors. RF-amide peptides from different families have major evolutionary conserved roles in the control of reproduction, but also of food intake, metabolism, energy expenditure, cardiovascular function, nociception and stress. They are also involved in the integration of environmental signals, notably the photoperiod, to regulate reproduction. For instance, in most vertebrate species and especially in seasonal mammals, kisspeptin and GnIH/RFRP have complementary but opposite effects in the control of reproductive function. In addition, recent data show cross-activities between the members of the RF-amide peptide superfamily and their receptors. For example, PrRP, kisspeptin and 26RFa are able to modulate nociception via NPFF receptors. Comparative studies have the potential to reveal novel regulatory mechanisms that could give a better comprehension of physiological functions and lead to new therapeutic treatments for related human pathologies. Thus, kisspeptin antagonists have been developed as novel tools for treatment of hormone-dependent disorders of reproduction such as precocious puberty and endometriosis or kisspeptin agonists for treatment of infertility, in humans. Studies on lower vertebrate models can also contribute to the discovery of new roles of these peptides, as seen recently with kisspeptin being involved in the early development of the medaka. This research topic will aim at gathering major advances achieved through comparative studies in (mammalian and non-mammalian) vertebrates and invertebrates, in the knowledge of RF-amide peptides in term of evolutionary history and physiological roles.
540 ## - TERMS GOVERNING USE AND REPRODUCTION NOTE
Terms governing use and reproduction Creative Commons
-- https://creativecommons.org/licenses/by/4.0/
-- cc
-- https://creativecommons.org/licenses/by/4.0/
546 ## - LANGUAGE NOTE
Language note English
653 ## - INDEX TERM--UNCONTROLLED
Uncontrolled term Kisspeptin
653 ## - INDEX TERM--UNCONTROLLED
Uncontrolled term GPCRs
653 ## - INDEX TERM--UNCONTROLLED
Uncontrolled term PrRP
653 ## - INDEX TERM--UNCONTROLLED
Uncontrolled term NPFF
653 ## - INDEX TERM--UNCONTROLLED
Uncontrolled term GnIH
653 ## - INDEX TERM--UNCONTROLLED
Uncontrolled term RF-amide peptides
653 ## - INDEX TERM--UNCONTROLLED
Uncontrolled term evolution
653 ## - INDEX TERM--UNCONTROLLED
Uncontrolled term QRFP
700 1# - ADDED ENTRY--PERSONAL NAME
Personal name Hubert Vaudry
Relator code auth
9 (RLIN) 1570542
700 1# - ADDED ENTRY--PERSONAL NAME
Personal name Sylvie Dufour
Relator code auth
9 (RLIN) 1620328
856 40 - ELECTRONIC LOCATION AND ACCESS
Host name www.oapen.org
Uniform Resource Identifier <a href="http://journal.frontiersin.org/researchtopic/2324/a-comparative-survey-of-the-rf-amide-peptide-superfamily">http://journal.frontiersin.org/researchtopic/2324/a-comparative-survey-of-the-rf-amide-peptide-superfamily</a>
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Public note DOAB: download the publication
856 40 - ELECTRONIC LOCATION AND ACCESS
Host name www.oapen.org
Uniform Resource Identifier <a href="https://directory.doabooks.org/handle/20.500.12854/43629">https://directory.doabooks.org/handle/20.500.12854/43629</a>
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Public note DOAB: description of the publication
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