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Evolution of PTH assays

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Resumo:PTH metabolism is complex and the circulating forms include the intact 1-84 molecule as well as several carboxyl-terminal fragments. The first generation of PTH assays included several types of competitive assays, with specificities that spanned carboxyl, mid-region and amino-terminal portions of the molecule. The limitations of these assays and the methodological evolution led to the description of 2nd generation non-competitive immunometric assays for PTH in the late 80's, based on the recognition of the PTH molecule by two different antibodies, one directed against de amino-terminal and other against the carboxyl-terminal segments. The observation that in some circumstances "long" carboxyl-terminal segments were also measured by 2nd generation assays led to the development of 3rd generation assays based on amino-terminal specific antibodies that are specific for the first amino acids, measuring only the molecular forms that activate PTH1R. The practical and cost-benefit advantages of these assays are still debatable. The recent observation that carboxyl-terminal fragments of PTH have biological activity via a distinct receptor than PTH1R, points to the future need of more than one assay in order to evaluate parathyroid hormone function.
Autores principais:Vieira,José Gilberto H.
Outros Autores:Kunii,Ilda; Nishida,Sônia
Assunto:Parathyroid hormone assay Radioimmunoassay Immunometric assays Circulating forms of parathyroid hormone
Ano:2006
País:Brasil
Tipo de documento:artigo
Tipo de acesso:acesso aberto
Instituição associada:IBICT
Idioma:inglês
Origem:Oasisbr
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author Vieira,José Gilberto H.
author2 Kunii,Ilda
Nishida,Sônia
author2_role author
author
author_facet Vieira,José Gilberto H.
Kunii,Ilda
Nishida,Sônia
author_role author
country_str BR
creators_json_txt [{\"Person.name\":\"Vieira,José Gilberto H.\"},{\"Person.name\":\"Kunii,Ilda\"},{\"Person.name\":\"Nishida,Sônia\"}]
datacite.creators.creator.creatorName.fl_str_mv Vieira,José Gilberto H.
Kunii,Ilda
Nishida,Sônia
datacite.rights.fl_str_mv http://purl.org/coar/access_right/c_abf2
datacite.subjects.subject.fl_str_mv Parathyroid hormone assay
Radioimmunoassay
Immunometric assays
Circulating forms of parathyroid hormone
datacite.titles.title.fl_str_mv Evolution of PTH assays
dc.creator.none.fl_str_mv Vieira,José Gilberto H.
Kunii,Ilda
Nishida,Sônia
dc.format.none.fl_str_mv text/html
dc.identifier.none.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0004-27302006000400007
dc.language.none.fl_str_mv eng
dc.publisher.none.fl_str_mv Sociedade Brasileira de Endocrinologia e Metabologia
dc.rights.none.fl_str_mv http://purl.org/coar/access_right/c_abf2
dc.source.none.fl_str_mv Arquivos Brasileiros de Endocrinologia & Metabologia v.50 n.4 2006
reponame:Arquivos Brasileiros de Endocrinologia & Metabologia (Online)
instname:Sociedade Brasileira de Endocrinologia e Metabologia (SBEM)
instacron:SBEM
dc.subject.none.fl_str_mv Parathyroid hormone assay
Radioimmunoassay
Immunometric assays
Circulating forms of parathyroid hormone
dc.title.fl_str_mv Evolution of PTH assays
dc.type.none.fl_str_mv http://purl.org/coar/resource_type/c_6501
description PTH metabolism is complex and the circulating forms include the intact 1-84 molecule as well as several carboxyl-terminal fragments. The first generation of PTH assays included several types of competitive assays, with specificities that spanned carboxyl, mid-region and amino-terminal portions of the molecule. The limitations of these assays and the methodological evolution led to the description of 2nd generation non-competitive immunometric assays for PTH in the late 80's, based on the recognition of the PTH molecule by two different antibodies, one directed against de amino-terminal and other against the carboxyl-terminal segments. The observation that in some circumstances "long" carboxyl-terminal segments were also measured by 2nd generation assays led to the development of 3rd generation assays based on amino-terminal specific antibodies that are specific for the first amino acids, measuring only the molecular forms that activate PTH1R. The practical and cost-benefit advantages of these assays are still debatable. The recent observation that carboxyl-terminal fragments of PTH have biological activity via a distinct receptor than PTH1R, points to the future need of more than one assay in order to evaluate parathyroid hormone function.
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person_str_mv Vieira,José Gilberto H.
Kunii,Ilda
Nishida,Sônia
publishDate 2006
publisher.none.fl_str_mv Sociedade Brasileira de Endocrinologia e Metabologia
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spelling Evolution of PTH assaysVieira,José Gilberto H.Kunii,IldaNishida,SôniaParathyroid hormone assayRadioimmunoassayImmunometric assaysCirculating forms of parathyroid hormoneopen accesshttp://purl.org/coar/access_right/c_abf2http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0004-27302006000400007URLhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0004-27302006000400007URLHasVersion2006-08-01PTH metabolism is complex and the circulating forms include the intact 1-84 molecule as well as several carboxyl-terminal fragments. The first generation of PTH assays included several types of competitive assays, with specificities that spanned carboxyl, mid-region and amino-terminal portions of the molecule. The limitations of these assays and the methodological evolution led to the description of 2nd generation non-competitive immunometric assays for PTH in the late 80's, based on the recognition of the PTH molecule by two different antibodies, one directed against de amino-terminal and other against the carboxyl-terminal segments. The observation that in some circumstances "long" carboxyl-terminal segments were also measured by 2nd generation assays led to the development of 3rd generation assays based on amino-terminal specific antibodies that are specific for the first amino acids, measuring only the molecular forms that activate PTH1R. The practical and cost-benefit advantages of these assays are still debatable. The recent observation that carboxyl-terminal fragments of PTH have biological activity via a distinct receptor than PTH1R, points to the future need of more than one assay in order to evaluate parathyroid hormone function.engtext/htmlSociedade Brasileira de Endocrinologia e MetabologiaArquivos Brasileiros de Endocrinologia & Metabologia v.50 n.4 2006reponame:Arquivos Brasileiros de Endocrinologia & Metabologia (Online)instname:Sociedade Brasileira de Endocrinologia e Metabologia (SBEM)instacron:SBEMjournal articlehttp://purl.org/coar/resource_type/c_6501literatureVoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85
spellingShingle Evolution of PTH assays
Vieira,José Gilberto H.
Parathyroid hormone assay
Radioimmunoassay
Immunometric assays
Circulating forms of parathyroid hormone
status SINGLETON
status_str VoR
subject.fl_str_mv Parathyroid hormone assay
Radioimmunoassay
Immunometric assays
Circulating forms of parathyroid hormone
title Evolution of PTH assays
title_full Evolution of PTH assays
title_fullStr Evolution of PTH assays
title_full_unstemmed Evolution of PTH assays
title_short Evolution of PTH assays
title_sort Evolution of PTH assays
topic Parathyroid hormone assay
Radioimmunoassay
Immunometric assays
Circulating forms of parathyroid hormone
topic_facet Parathyroid hormone assay
Radioimmunoassay
Immunometric assays
Circulating forms of parathyroid hormone
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0004-27302006000400007
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