Calcitropic peptides: neural perspectives
Identifieur interne : 002896 ( Istex/Corpus ); précédent : 002895; suivant : 002897Calcitropic peptides: neural perspectives
Auteurs : K. L Hull ; K. Fathimani ; P. Sharma ; S. HarveySource :
- Comparative Biochemistry and Physiology, Part C: Comparative Pharmacology and Toxicology [ 0742-8413 ] ; 1998.
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Abstract
In mammals and higher vertebrates, calcitropic peptides are produced by peripheral endocrine glands: the parathyroid gland (PTH), thyroid or ultimobranchial gland (calcitonin) and the anterior pituitary gland (growth hormone and prolactin). These hormones are, however, also found in the neural tissues of lower vertebrates and invertebrates that lack these endocrine organs, suggesting that neural tissue may be an ancestral site of calcitropic peptide synthesis. Indeed, the demonstration of CNS receptors for these calcitropic peptides and their induction of neurological actions suggest that these hormones arose as neuropeptides. Neural and neuroendocrine roles of some of these calcitropic hormones (calcitonin and parathyroid hormone) and related peptides (calcitonin gene related peptide, stanniocalcin and parathyroid hormone related peptide) are thus the focus of this review.
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DOI: 10.1016/S0742-8413(98)00010-3
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ISTEX:EF5514D0383CE8ACFDFAB418F0451B1FAF3B1F13Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Calcitropic peptides: neural perspectives</title><author><name sortKey="Hull, K L" sort="Hull, K L" uniqKey="Hull K" first="K. L" last="Hull">K. L Hull</name><affiliation><mods:affiliation>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</mods:affiliation></affiliation></author><author><name sortKey="Fathimani, K" sort="Fathimani, K" uniqKey="Fathimani K" first="K" last="Fathimani">K. Fathimani</name><affiliation><mods:affiliation>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</mods:affiliation></affiliation></author><author><name sortKey="Sharma, P" sort="Sharma, P" uniqKey="Sharma P" first="P" last="Sharma">P. Sharma</name><affiliation><mods:affiliation>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</mods:affiliation></affiliation></author><author><name sortKey="Harvey, S" sort="Harvey, S" uniqKey="Harvey S" first="S" last="Harvey">S. Harvey</name><affiliation><mods:affiliation>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:EF5514D0383CE8ACFDFAB418F0451B1FAF3B1F13</idno><date when="1998" year="1998">1998</date><idno type="doi">10.1016/S0742-8413(98)00010-3</idno><idno type="url">https://api-v5.istex.fr/document/EF5514D0383CE8ACFDFAB418F0451B1FAF3B1F13/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">002896</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">002896</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Calcitropic peptides: neural perspectives</title><author><name sortKey="Hull, K L" sort="Hull, K L" uniqKey="Hull K" first="K. L" last="Hull">K. L Hull</name><affiliation><mods:affiliation>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</mods:affiliation></affiliation></author><author><name sortKey="Fathimani, K" sort="Fathimani, K" uniqKey="Fathimani K" first="K" last="Fathimani">K. Fathimani</name><affiliation><mods:affiliation>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</mods:affiliation></affiliation></author><author><name sortKey="Sharma, P" sort="Sharma, P" uniqKey="Sharma P" first="P" last="Sharma">P. Sharma</name><affiliation><mods:affiliation>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</mods:affiliation></affiliation></author><author><name sortKey="Harvey, S" sort="Harvey, S" uniqKey="Harvey S" first="S" last="Harvey">S. Harvey</name><affiliation><mods:affiliation>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Comparative Biochemistry and Physiology, Part C: Comparative Pharmacology and Toxicology</title><title level="j" type="abbrev">CBCOLD</title><idno type="ISSN">0742-8413</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1998">1998</date><biblScope unit="volume">119</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="389">389</biblScope><biblScope unit="page" to="410">410</biblScope></imprint><idno type="ISSN">0742-8413</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0742-8413</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Brain</term><term>Calcitonin</term><term>Calcitonin gene-related peptide</term><term>Calcium</term><term>Parathyroid hormone</term><term>Parathyroid hormone related peptide</term><term>Stanniocalcin</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In mammals and higher vertebrates, calcitropic peptides are produced by peripheral endocrine glands: the parathyroid gland (PTH), thyroid or ultimobranchial gland (calcitonin) and the anterior pituitary gland (growth hormone and prolactin). These hormones are, however, also found in the neural tissues of lower vertebrates and invertebrates that lack these endocrine organs, suggesting that neural tissue may be an ancestral site of calcitropic peptide synthesis. Indeed, the demonstration of CNS receptors for these calcitropic peptides and their induction of neurological actions suggest that these hormones arose as neuropeptides. Neural and neuroendocrine roles of some of these calcitropic hormones (calcitonin and parathyroid hormone) and related peptides (calcitonin gene related peptide, stanniocalcin and parathyroid hormone related peptide) are thus the focus of this review.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>K.L Hull</name><affiliations><json:string>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</json:string></affiliations></json:item><json:item><name>K Fathimani</name><affiliations><json:string>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</json:string></affiliations></json:item><json:item><name>P Sharma</name><affiliations><json:string>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</json:string></affiliations></json:item><json:item><name>S Harvey</name><affiliations><json:string>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Parathyroid hormone</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Calcitonin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Parathyroid hormone related peptide</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Calcitonin gene-related peptide</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Stanniocalcin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Calcium</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Brain</value></json:item></subject><language><json:string>eng</json:string></language><originalGenre><json:string>Review article</json:string></originalGenre><abstract>In mammals and higher vertebrates, calcitropic peptides are produced by peripheral endocrine glands: the parathyroid gland (PTH), thyroid or ultimobranchial gland (calcitonin) and the anterior pituitary gland (growth hormone and prolactin). These hormones are, however, also found in the neural tissues of lower vertebrates and invertebrates that lack these endocrine organs, suggesting that neural tissue may be an ancestral site of calcitropic peptide synthesis. Indeed, the demonstration of CNS receptors for these calcitropic peptides and their induction of neurological actions suggest that these hormones arose as neuropeptides. Neural and neuroendocrine roles of some of these calcitropic hormones (calcitonin and parathyroid hormone) and related peptides (calcitonin gene related peptide, stanniocalcin and parathyroid hormone related peptide) are thus the focus of this review.</abstract><qualityIndicators><score>6.452</score><pdfWordCount>14621</pdfWordCount><pdfCharCount>100864</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>22</pdfPageCount><pdfPageSize>552 x 768 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>121</abstractWordCount><abstractCharCount>886</abstractCharCount><keywordCount>7</keywordCount></qualityIndicators><title>Calcitropic peptides: neural perspectives</title><pii><json:string>S0742-8413(98)00010-3</json:string></pii><genre><json:string>review-article</json:string></genre><serie><title>Vertebrate Endocrinology: Fundamentals and Biomedical Implications. Regulation of Calcium and Phosphate</title><language><json:string>unknown</json:string></language><volume>3</volume><pages><first>105</first><last>138</last></pages><editor><json:item><name>PKT Pang</name></json:item><json:item><name>MP Schreibman</name></json:item></editor></serie><host><title>Comparative Biochemistry and Physiology, Part C: Comparative Pharmacology and Toxicology</title><language><json:string>unknown</json:string></language><publicationDate>1998</publicationDate><issn><json:string>0742-8413</json:string></issn><pii><json:string>S0742-8413(00)X0032-1</json:string></pii><volume>119</volume><issue>3</issue><pages><first>389</first><last>410</last></pages><genre><json:string>journal</json:string></genre></host><categories><inist><json:string>sciences appliquees, technologies et medecines</json:string><json:string>sciences biologiques et medicales</json:string><json:string>sciences medicales</json:string><json:string>pathologie osteoarticulaire</json:string></inist></categories><publicationDate>1998</publicationDate><copyrightDate>1998</copyrightDate><doi><json:string>10.1016/S0742-8413(98)00010-3</json:string></doi><id>EF5514D0383CE8ACFDFAB418F0451B1FAF3B1F13</id><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api-v5.istex.fr/document/EF5514D0383CE8ACFDFAB418F0451B1FAF3B1F13/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api-v5.istex.fr/document/EF5514D0383CE8ACFDFAB418F0451B1FAF3B1F13/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api-v5.istex.fr/document/EF5514D0383CE8ACFDFAB418F0451B1FAF3B1F13/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Calcitropic peptides: neural perspectives</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>©1998 Elsevier Science Inc.</p></availability><date>1998</date></publicationStmt><notesStmt><note type="content">Section title: Review</note><note type="content">Fig. 1: Phylogenetic presence of calcitropic hormones and related peptides. POMC, pro-opio-melanocortin; GH/PRL, growth hormone/prolactin; Vitamin D, [1, 25]dihydroxy vitamin D3; and PTH, parathyroid hormone.</note><note type="content">Fig. 2: Parathyroid hormone (PTH)-immunoreactivity in the peripheral nervous system (PNS). PTH immunoreactivity was determined in the ileum myenteric plexus of the guinea pig and rat as previously described [208].</note><note type="content">Fig. 3: (A) Reverse transcription-polymerase chain reaction analysis of parathyroid hormone (PTH) in the skate brain. RNA from rat parathyroid gland and skate brain was reverse transcribed and amplified in the presence of degenerate primers based on conserved sequences of the cloned mammalian and avian PTH genes. A moiety of expected size was amplified from both tissues (+): this fragment was not observed if the reverse transcription enzyme was omitted from the reverse transcription reaction (−). (B) The addition of the restriction enzyme BstNI to the amplified skate cDNA (+BstNI) resulted in smaller fragments of expected size; identical fragments were generated by the digestion of rat parathyroid gland cDNA (data not shown).</note><note type="content">Fig. 4: Concentrations of brain and parathyroidal PTH mRNA. RNA was extracted from the brains and parathyroid glands of rats (n=7) and PTH mRNA was quantified by Northern analysis as previously described [198]. The abundance of PTH mRNA in the CNS was inversely correlated (r=−0.79) with parathyroidal PTH mRNA (P<0.05).</note><note type="content">Fig. 5: Differential regulation of central and parathyroidal PTH transcripts by hypocalcemia. Rats were fed diets containing normal (normal calcium; 0.4%) or low (low calcium; 0.02%) levels of calcium for 3 weeks. Following sacrifice, RNA was isolated from parathyroid glands and whole brains and PTH mRNA was detected by Northern analysis, as previously described [198]. PTH mRNA was quantified by laser densitometry and expressed (relative to the hybridization of a GAPDH riboprobe to correct for loading error) in arbitrary units (A.U.). The induction of dietary hypocalcemia for 3 weeks significantly (P<0.001) increased PTH mRNA in the parathyroid gland. CNS PTH mRNA was, conversely, significantly (P<0.001) reduced in hypocalcemic rats. *P<0.001.</note><note type="content">Fig. 6: Neuromodulation of a neuroglandular synapse of the pond snail Helisoma by PTH. Helisoma salivary glands contain electrically coupled networks of glandular cells that exhibit a giant excitatory postsynaptic potential (EPSP) in response to action potentials generated by neuron B4. Although superfusion with PTH (10−5 M for 6 min) did not greatly effect action potential duration, it greatly increased the amplitude of the excitatory post synaptic potential (from 6.25 to 7.7 mV).</note><note type="content">Fig. 7: Effects of PTH on intracellular calcium (Ca2+) concentration in Helisoma bucal ganglion B5 neurons. Intracellular calcium concentrations, as determined by Fura 2, are expressed as the fluorescence ratio (340/380). Changes in the ratio (340/380) before and after the application of different PTH fragments are expressed as arbitrary units. *P<0.01.</note><note type="content">Table 1: Calcitonin immunoreactivity in unicellular animals, invertebrates and protovertebrates</note><note type="content">Table 2: Brain: blood PTH ratiosa</note><note type="content">Table 3: Parathyroid hormone immunoreactivity (PTH-IR) in invertebrates and non-tetrapod vertebrates</note><note type="content">Table 4: POMC-derived peptides in unicellular animals and invertebrate neurons</note><note type="content">Table 5:</note><note type="content">Table 6:</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Calcitropic peptides: neural perspectives</title><author xml:id="author-0000"><persName><forename type="first">K.L</forename><surname>Hull</surname></persName><note type="biography">Current address: Department of Biology, Bishop’s University, Lennoxville QC, JIM IZ7, Canada.</note><affiliation>Current address: Department of Biology, Bishop’s University, Lennoxville QC, JIM IZ7, Canada.</affiliation><affiliation>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</affiliation></author><author xml:id="author-0001"><persName><forename type="first">K</forename><surname>Fathimani</surname></persName><affiliation>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</affiliation></author><author xml:id="author-0002"><persName><forename type="first">P</forename><surname>Sharma</surname></persName><affiliation>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</affiliation></author><author xml:id="author-0003"><persName><forename type="first">S</forename><surname>Harvey</surname></persName><note type="correspondence"><p>Corresponding author. Tel.: +1 403 4922809.</p></note><affiliation>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</affiliation></author><idno type="istex">EF5514D0383CE8ACFDFAB418F0451B1FAF3B1F13</idno><idno type="DOI">10.1016/S0742-8413(98)00010-3</idno><idno type="PII">S0742-8413(98)00010-3</idno></analytic><monogr><title level="j">Comparative Biochemistry and Physiology, Part C: Comparative Pharmacology and Toxicology</title><title level="j" type="abbrev">CBCOLD</title><idno type="pISSN">0742-8413</idno><idno type="PII">S0742-8413(00)X0032-1</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1998"></date><biblScope unit="volume">119</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="389">389</biblScope><biblScope unit="page" to="410">410</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1998</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>In mammals and higher vertebrates, calcitropic peptides are produced by peripheral endocrine glands: the parathyroid gland (PTH), thyroid or ultimobranchial gland (calcitonin) and the anterior pituitary gland (growth hormone and prolactin). These hormones are, however, also found in the neural tissues of lower vertebrates and invertebrates that lack these endocrine organs, suggesting that neural tissue may be an ancestral site of calcitropic peptide synthesis. Indeed, the demonstration of CNS receptors for these calcitropic peptides and their induction of neurological actions suggest that these hormones arose as neuropeptides. Neural and neuroendocrine roles of some of these calcitropic hormones (calcitonin and parathyroid hormone) and related peptides (calcitonin gene related peptide, stanniocalcin and parathyroid hormone related peptide) are thus the focus of this review.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>Parathyroid hormone</term></item><item><term>Calcitonin</term></item><item><term>Parathyroid hormone related peptide</term></item><item><term>Calcitonin gene-related peptide</term></item><item><term>Stanniocalcin</term></item><item><term>Calcium</term></item><item><term>Brain</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1998">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api-v5.istex.fr/document/EF5514D0383CE8ACFDFAB418F0451B1FAF3B1F13/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: ce:floats; body; tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"><istex:entity SYSTEM="gr1" NDATA="IMAGE" name="gr1"></istex:entity><istex:entity SYSTEM="gr2" NDATA="IMAGE" name="gr2"></istex:entity><istex:entity SYSTEM="gr3" NDATA="IMAGE" name="gr3"></istex:entity><istex:entity SYSTEM="gr4" NDATA="IMAGE" name="gr4"></istex:entity><istex:entity SYSTEM="gr5" NDATA="IMAGE" name="gr5"></istex:entity><istex:entity SYSTEM="gr6" NDATA="IMAGE" name="gr6"></istex:entity><istex:entity SYSTEM="gr7" NDATA="IMAGE" name="gr7"></istex:entity></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="rev" xml:lang="en"><item-info><jid>CBC</jid><aid>2</aid><ce:pii>S0742-8413(98)00010-3</ce:pii><ce:doi>10.1016/S0742-8413(98)00010-3</ce:doi><ce:copyright year="1998" type="full-transfer">Elsevier Science Inc.</ce:copyright></item-info><head><ce:dochead><ce:textfn>Review</ce:textfn></ce:dochead><ce:title>Calcitropic peptides: neural perspectives</ce:title><ce:author-group><ce:author><ce:given-name>K.L</ce:given-name><ce:surname>Hull</ce:surname><ce:cross-ref refid="FN1"><ce:sup>1</ce:sup></ce:cross-ref><ce:cross-ref refid="FN1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>K</ce:given-name><ce:surname>Fathimani</ce:surname></ce:author><ce:author><ce:given-name>P</ce:given-name><ce:surname>Sharma</ce:surname></ce:author><ce:author><ce:given-name>S</ce:given-name><ce:surname>Harvey</ce:surname><ce:cross-ref refid="CORR1">*</ce:cross-ref></ce:author><ce:affiliation><ce:textfn>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</ce:textfn></ce:affiliation><ce:correspondence id="CORR1"><ce:label>*</ce:label><ce:text>Corresponding author. Tel.: +1 403 4922809.</ce:text></ce:correspondence><ce:footnote id="FN1"><ce:label>1</ce:label><ce:note-para>Current address: Department of Biology, Bishop’s University, Lennoxville QC, JIM IZ7, Canada.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="30" month="5" year="1997"></ce:date-received><ce:date-accepted day="13" month="11" year="1997"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>In mammals and higher vertebrates, calcitropic peptides are produced by peripheral endocrine glands: the parathyroid gland (PTH), thyroid or ultimobranchial gland (calcitonin) and the anterior pituitary gland (growth hormone and prolactin). These hormones are, however, also found in the neural tissues of lower vertebrates and invertebrates that lack these endocrine organs, suggesting that neural tissue may be an ancestral site of calcitropic peptide synthesis. Indeed, the demonstration of CNS receptors for these calcitropic peptides and their induction of neurological actions suggest that these hormones arose as neuropeptides. Neural and neuroendocrine roles of some of these calcitropic hormones (calcitonin and parathyroid hormone) and related peptides (calcitonin gene related peptide, stanniocalcin and parathyroid hormone related peptide) are thus the focus of this review.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Parathyroid hormone</ce:text></ce:keyword><ce:keyword><ce:text>Calcitonin</ce:text></ce:keyword><ce:keyword><ce:text>Parathyroid hormone related peptide</ce:text></ce:keyword><ce:keyword><ce:text>Calcitonin gene-related peptide</ce:text></ce:keyword><ce:keyword><ce:text>Stanniocalcin</ce:text></ce:keyword><ce:keyword><ce:text>Calcium</ce:text></ce:keyword><ce:keyword><ce:text>Brain</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Calcitropic peptides: neural perspectives</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Calcitropic peptides: neural perspectives</title></titleInfo><name type="personal"><namePart type="given">K.L</namePart><namePart type="family">Hull</namePart><affiliation>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</affiliation><description>Current address: Department of Biology, Bishop’s University, Lennoxville QC, JIM IZ7, Canada.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">K</namePart><namePart type="family">Fathimani</namePart><affiliation>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">P</namePart><namePart type="family">Sharma</namePart><affiliation>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">S</namePart><namePart type="family">Harvey</namePart><affiliation>Department of Physiology, University of Alberta, Edmonton AB, T6G 2H7, Canada</affiliation><description>Corresponding author. Tel.: +1 403 4922809.</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="review-article" displayLabel="Review article"></genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1998</dateIssued><copyrightDate encoding="w3cdtf">1998</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">In mammals and higher vertebrates, calcitropic peptides are produced by peripheral endocrine glands: the parathyroid gland (PTH), thyroid or ultimobranchial gland (calcitonin) and the anterior pituitary gland (growth hormone and prolactin). These hormones are, however, also found in the neural tissues of lower vertebrates and invertebrates that lack these endocrine organs, suggesting that neural tissue may be an ancestral site of calcitropic peptide synthesis. Indeed, the demonstration of CNS receptors for these calcitropic peptides and their induction of neurological actions suggest that these hormones arose as neuropeptides. Neural and neuroendocrine roles of some of these calcitropic hormones (calcitonin and parathyroid hormone) and related peptides (calcitonin gene related peptide, stanniocalcin and parathyroid hormone related peptide) are thus the focus of this review.</abstract><note type="content">Section title: Review</note><note type="content">Fig. 1: Phylogenetic presence of calcitropic hormones and related peptides. POMC, pro-opio-melanocortin; GH/PRL, growth hormone/prolactin; Vitamin D, [1, 25]dihydroxy vitamin D3; and PTH, parathyroid hormone.</note><note type="content">Fig. 2: Parathyroid hormone (PTH)-immunoreactivity in the peripheral nervous system (PNS). PTH immunoreactivity was determined in the ileum myenteric plexus of the guinea pig and rat as previously described [208].</note><note type="content">Fig. 3: (A) Reverse transcription-polymerase chain reaction analysis of parathyroid hormone (PTH) in the skate brain. RNA from rat parathyroid gland and skate brain was reverse transcribed and amplified in the presence of degenerate primers based on conserved sequences of the cloned mammalian and avian PTH genes. A moiety of expected size was amplified from both tissues (+): this fragment was not observed if the reverse transcription enzyme was omitted from the reverse transcription reaction (−). (B) The addition of the restriction enzyme BstNI to the amplified skate cDNA (+BstNI) resulted in smaller fragments of expected size; identical fragments were generated by the digestion of rat parathyroid gland cDNA (data not shown).</note><note type="content">Fig. 4: Concentrations of brain and parathyroidal PTH mRNA. RNA was extracted from the brains and parathyroid glands of rats (n=7) and PTH mRNA was quantified by Northern analysis as previously described [198]. The abundance of PTH mRNA in the CNS was inversely correlated (r=−0.79) with parathyroidal PTH mRNA (P<0.05).</note><note type="content">Fig. 5: Differential regulation of central and parathyroidal PTH transcripts by hypocalcemia. Rats were fed diets containing normal (normal calcium; 0.4%) or low (low calcium; 0.02%) levels of calcium for 3 weeks. Following sacrifice, RNA was isolated from parathyroid glands and whole brains and PTH mRNA was detected by Northern analysis, as previously described [198]. PTH mRNA was quantified by laser densitometry and expressed (relative to the hybridization of a GAPDH riboprobe to correct for loading error) in arbitrary units (A.U.). The induction of dietary hypocalcemia for 3 weeks significantly (P<0.001) increased PTH mRNA in the parathyroid gland. CNS PTH mRNA was, conversely, significantly (P<0.001) reduced in hypocalcemic rats. *P<0.001.</note><note type="content">Fig. 6: Neuromodulation of a neuroglandular synapse of the pond snail Helisoma by PTH. Helisoma salivary glands contain electrically coupled networks of glandular cells that exhibit a giant excitatory postsynaptic potential (EPSP) in response to action potentials generated by neuron B4. Although superfusion with PTH (10−5 M for 6 min) did not greatly effect action potential duration, it greatly increased the amplitude of the excitatory post synaptic potential (from 6.25 to 7.7 mV).</note><note type="content">Fig. 7: Effects of PTH on intracellular calcium (Ca2+) concentration in Helisoma bucal ganglion B5 neurons. Intracellular calcium concentrations, as determined by Fura 2, are expressed as the fluorescence ratio (340/380). Changes in the ratio (340/380) before and after the application of different PTH fragments are expressed as arbitrary units. *P<0.01.</note><note type="content">Table 1: Calcitonin immunoreactivity in unicellular animals, invertebrates and protovertebrates</note><note type="content">Table 2: Brain: blood PTH ratiosa</note><note type="content">Table 3: Parathyroid hormone immunoreactivity (PTH-IR) in invertebrates and non-tetrapod vertebrates</note><note type="content">Table 4: POMC-derived peptides in unicellular animals and invertebrate neurons</note><note type="content">Table 5: </note><note type="content">Table 6: </note><subject lang="en"><genre>Keywords</genre><topic>Parathyroid hormone</topic><topic>Calcitonin</topic><topic>Parathyroid hormone related peptide</topic><topic>Calcitonin gene-related peptide</topic><topic>Stanniocalcin</topic><topic>Calcium</topic><topic>Brain</topic></subject><relatedItem type="host"><titleInfo><title>Comparative Biochemistry and Physiology, Part C: Comparative Pharmacology and Toxicology</title></titleInfo><titleInfo type="abbreviated"><title>CBCOLD</title></titleInfo><genre type="journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">199806</dateIssued></originInfo><identifier type="ISSN">0742-8413</identifier><identifier type="PII">S0742-8413(00)X0032-1</identifier><part><date>199806</date><detail type="volume"><number>119</number><caption>vol.</caption></detail><detail type="issue"><number>3</number><caption>no.</caption></detail><extent unit="issue pages"><start>217</start><end>416</end></extent><extent unit="pages"><start>389</start><end>410</end></extent></part></relatedItem><identifier type="istex">EF5514D0383CE8ACFDFAB418F0451B1FAF3B1F13</identifier><identifier type="DOI">10.1016/S0742-8413(98)00010-3</identifier><identifier type="PII">S0742-8413(98)00010-3</identifier><accessCondition type="use and reproduction" contentType="copyright">©1998 Elsevier Science Inc.</accessCondition><recordInfo><recordContentSource>ELSEVIER</recordContentSource><recordOrigin>Elsevier Science Inc., ©1998</recordOrigin></recordInfo></mods></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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