Evolution of PTH assays

Detalhes bibliográficos
Autor(a) principal: Vieira,José Gilberto H.
Data de Publicação: 2006
Outros Autores: Kunii,Ilda, Nishida,Sônia
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Arquivos Brasileiros de Endocrinologia & Metabologia (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0004-27302006000400007
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.
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spelling Evolution of PTH assaysParathyroid hormone assayRadioimmunoassayImmunometric assaysCirculating forms of parathyroid hormonePTH 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.Sociedade Brasileira de Endocrinologia e Metabologia2006-08-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0004-27302006000400007Arquivos Brasileiros de Endocrinologia & Metabologia v.50 n.4 2006reponame:Arquivos Brasileiros de Endocrinologia & Metabologia (Online)instname:Sociedade Brasileira de Endocrinologia e Metabologia (SBEM)instacron:SBEM10.1590/S0004-27302006000400007info:eu-repo/semantics/openAccessVieira,José Gilberto H.Kunii,IldaNishida,Sôniaeng2006-11-14T00:00:00Zoai:scielo:S0004-27302006000400007Revistahttps://www.aem-sbem.com/ONGhttps://old.scielo.br/oai/scielo-oai.php||abem-editoria@endocrino.org.br1677-94870004-2730opendoar:2006-11-14T00:00Arquivos Brasileiros de Endocrinologia & Metabologia (Online) - Sociedade Brasileira de Endocrinologia e Metabologia (SBEM)false
dc.title.none.fl_str_mv Evolution of PTH assays
title Evolution of PTH assays
spellingShingle Evolution of PTH assays
Vieira,José Gilberto H.
Parathyroid hormone assay
Radioimmunoassay
Immunometric assays
Circulating forms of parathyroid hormone
title_short Evolution of PTH assays
title_full Evolution of PTH assays
title_fullStr Evolution of PTH assays
title_full_unstemmed Evolution of PTH assays
title_sort Evolution of PTH assays
author Vieira,José Gilberto H.
author_facet Vieira,José Gilberto H.
Kunii,Ilda
Nishida,Sônia
author_role author
author2 Kunii,Ilda
Nishida,Sônia
author2_role author
author
dc.contributor.author.fl_str_mv Vieira,José Gilberto H.
Kunii,Ilda
Nishida,Sônia
dc.subject.por.fl_str_mv Parathyroid hormone assay
Radioimmunoassay
Immunometric assays
Circulating forms of parathyroid hormone
topic Parathyroid hormone assay
Radioimmunoassay
Immunometric assays
Circulating forms of parathyroid hormone
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.
publishDate 2006
dc.date.none.fl_str_mv 2006-08-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0004-27302006000400007
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0004-27302006000400007
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0004-27302006000400007
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
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dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Sociedade Brasileira de Endocrinologia e Metabologia
publisher.none.fl_str_mv Sociedade Brasileira de Endocrinologia e Metabologia
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
instname_str Sociedade Brasileira de Endocrinologia e Metabologia (SBEM)
instacron_str SBEM
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reponame_str Arquivos Brasileiros de Endocrinologia & Metabologia (Online)
collection Arquivos Brasileiros de Endocrinologia & Metabologia (Online)
repository.name.fl_str_mv Arquivos Brasileiros de Endocrinologia & Metabologia (Online) - Sociedade Brasileira de Endocrinologia e Metabologia (SBEM)
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