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Ligand binding and signalling pathways of PTH receptors in sea bream (Sparus auratus) enterocytes

2006Journal article Restricted access
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dc.contributor.authorRotllant, J.
dc.contributor.authorGuerreiro, P. M.
dc.contributor.authorRedruello, Begoña
dc.contributor.authorFernandes, H.
dc.contributor.authorApolonia, L.
dc.contributor.authorAnjos, Liliana
dc.contributor.authorCanario, Adelino V. M.
dc.contributor.authorPower, Deborah
dc.date.accessioned2014-05-15T11:16:29Z
dc.date.available2014-05-15T11:16:29Z
dc.date.issued2006
dc.date.updated2014-05-13T09:33:30Z
dc.description.abstractWhole animal studies have indicated that Ca2+ uptake by the gastrointestinal tract is regulated by the action of parathyroid hormone-related peptide (PTHrP) in teleost fish. We have characterised PTH receptors (PTHR) in piscine enterocytes and established, by using aminoterminal PTHrP peptides, the amino acid residues important for receptor activation and for stabilising the ligand/receptor complex. Ligand binding of 125I-(1–35tyr) PTHrP to the membrane fraction of isolated sea bream enterocytes revealed the existence of a single saturable high-affinity receptor (KD=2.59 nM; Bmax=71 fmol/mg protein). Reverse transcription/polymerase chain reaction with specific primers for sea bream PTH1R and PTH3R confirmed the mRNA expression of only the later receptor. Fugu (1–34) PTHrP increased cAMP levels in enterocytes but had no effect on total inositol phosphate accumulation. The aminoterminal peptides (2–34)PTHrP, (3–34)PTHrP and (7–34) PTHrP bound efficiently to the receptor but were severely defective in stimulating cAMP in enterocyte cells indicating that the first six residues of piscine (1–34)PTHrP, although not important for receptor binding, are essential for activation of the adenylate cyclase/phosphokinase A (AC-PKA)-receptor-coupled intracellular signalling pathway. Therefore, PTHrP in teleosts acts on the gastrointestinal tract through PTH3R and the AC-PKA intracellular signalling pathway and might regulate Ca2+ uptake at this site. Ligand-receptor binding and activity throughout the vertebrates appears to be allocated to the same amino acid residues of the amino-terminal domain of the PTHrP molecule.por
dc.identifier.citationRotllant, J.; Guerreiro, P. M.; Redruello, B.; Fernandes, H.; Apolonia, L.; Anjos, L.; Canario, A. V. M.; Power, D. M. Ligand binding and signalling pathways of PTH receptors in sea bream (Sparus auratus) enterocytes, Cell and Tissue Research, 323, 2, 333-341, 2006.por
dc.identifier.doihttp://dx.doi.org/10.1007/s00441-005-0070-7
dc.identifier.issn0302-766X
dc.identifier.otherAUT: ACA00258; DPO00386;
dc.identifier.urihttp://hdl.handle.net/10400.1/3956
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherSpringerpor
dc.subjectParathyroid hormone-related peptide (PTHrP)por
dc.subjectPTHrP receptors (PTH1R, PTH3R)por
dc.subjectEnterocytepor
dc.subjectSea breampor
dc.subjectSparus auratus (Teleostei)por
dc.titleLigand binding and signalling pathways of PTH receptors in sea bream (Sparus auratus) enterocytespor
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage341por
oaire.citation.issue2por
oaire.citation.startPage333por
oaire.citation.titleCell and Tissue Researchpor
oaire.citation.volume323por
person.familyNameGuerreiro da Costa Guerreiro
person.familyNameRedruello
person.familyNameAnjos Guerreiro
person.familyNameCanario
person.familyNamePower
person.givenNamePedro Miguel
person.givenNameBegoña
person.givenNameLiliana Isabel Tomé
person.givenNameAdelino
person.givenNameDeborah Mary
person.identifierA-2539-2009
person.identifierAAK-3800-2020
person.identifier143624
person.identifier.ciencia-id5C13-965D-3148
person.identifier.ciencia-id6D18-2D1C-A45C
person.identifier.ciencia-id1F1E-D3B3-F804
person.identifier.ciencia-id891A-8A44-3CAE
person.identifier.orcid0000-0001-5371-7919
person.identifier.orcid0000-0003-1787-5594
person.identifier.orcid0000-0001-9474-522X
person.identifier.orcid0000-0002-6244-6468
person.identifier.orcid0000-0003-1366-0246
person.identifier.ridC-7942-2009
person.identifier.scopus-author-id8575757700
person.identifier.scopus-author-id56568523700
person.identifier.scopus-author-id7101806760
rcaap.rightsrestrictedAccesspor
rcaap.typearticlepor
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