Please use this identifier to cite or link to this item:
Full metadata record
DC FieldValueLanguage
dc.typeArtigo de periódicopt_BR
dc.titleExpression Of Calcium-buffering Proteins In Rat Intrinsic Laryngeal Muscles.pt_BR
dc.contributor.authorFerretti, Renatopt_BR
dc.contributor.authorMarques, Maria Juliapt_BR
dc.contributor.authorKhurana, Tejvir Spt_BR
dc.contributor.authorSanto Neto, Humbertopt_BR
unicamp.authorMaria Julia Marques, Departamento de Biologia Estrutural e Funcional, Instituto de Biologia, Universidade Estadual de Campinas, Campinas São Paulo, Brazil.pt_BR
unicamp.authorHumberto Santo Neto, Departamento de Biologia Estrutural e Funcional, Instituto de Biologia, Universidade Estadual de Campinas, Campinas São Paulo, Brazil Ferretti, Departamento de Anatomia, Instituto de Biociencias de Botucatu, Universidade Estadual Paulista, Botucatu São Paulo, S Khurana, Department of Physiology, Perelman School of Medicine and Pennsylvania Muscle Institute, University of Pennsylvania, Philadelphia,
dc.subjectLaryngeal Musclespt_BR
dc.subjectStore‐operated Calcium Entrypt_BR
dc.description.abstractIntrinsic laryngeal muscles (ILM) are highly specialized muscles involved in phonation and airway protection, with unique properties that allow them to perform extremely rapid contractions and to escape from damage in muscle dystrophy. Due to that, they may differ from limb muscles in several physiological aspects. Because a better ability to handle intracellular calcium has been suggested to explain ILM unique properties, we hypothesized that the profile of the proteins that regulate calcium levels in ILM is different from that in a limb muscle. Calcium-related proteins were analyzed in the ILM, cricothyroid (CT), and tibialis anterior (TA) muscles from male Sprague-Dawley rats (8 weeks of age) using quantitative PCR and western blotting. Higher expression of key Ca(2+) regulatory proteins was detected in ILM compared to TA, such as the sarcoplasmic reticulum (SR) Ca(2+)-reuptake proteins (Sercas 1 and 2), the Na(+)/Ca(2+) exchanger, phospholamban, and the Ca(2+)-binding protein calsequestrin. Parvalbumin, calmodulin and the ATPase, Ca(2+)-transporting, and plasma membrane 1 were also expressed at higher levels in ILM compared to TA. The store-operated calcium entry channel molecule was decreased in ILM compared to the limb muscle and the voltage-dependent L-type and ryanodine receptor were expressed at similar levels in ILM and TA. These results show that ILM have a calcium regulation system profile suggestive of a better ability to handle calcium changes in comparison to limb muscles, and this may provide a mechanistic insight for their unique pathophysiological properties.en
dc.relation.ispartofPhysiological Reportspt_BR
dc.relation.ispartofabbreviationPhysiol Reppt_BR
dc.identifier.citationPhysiological Reports. v. 3, n. 6, 2015-Jun.pt_BR
dc.description.provenanceMade available in DSpace on 2016-05-23T19:42:06Z (GMT). No. of bitstreams: 1 pmed_26109185.pdf: 541377 bytes, checksum: 35982ddc3a3b6d91f3cd97a977010c0b (MD5) Previous issue date: 2015en
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File SizeFormat 
pmed_26109185.pdf528.69 kBAdobe PDFView/Open

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.