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Article: Interferon-γ increases intracellular calcium and inositol phosphates in primary human thyroid cell culture

TitleInterferon-γ increases intracellular calcium and inositol phosphates in primary human thyroid cell culture
Authors
Issue Date1995
PublisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.org
Citation
Endocrinology, 1995, v. 136 n. 11, p. 5028-5033 How to Cite?
AbstractInterferon-γ (IFNγ) is believed to play a role in the pathogenesis of autoimmune thyroid disease, as it is known to exert diverse effects on thyroid metabolism. These include induction of human leukocyte antigen class II expression, inhibition of gene expression of thyroglobulin and thyroid peroxidase, as well as inhibition of cellular proliferation. However, the mechanism of action of IFNγ in thyrocytes has not been clearly defined. We studied the action of IFNγ on the production of inositol phosphates and intracellular Ca2+ mobilization in primary cultures of human thyrocytes using the fluorescent Ca2+ indicator furs-2. IFNγ increased the production of inositol mono-, bis-, and trisphosphates and caused a dose-dependent increase in intracellular Ca2+ ([Ca2+)(i)) at 37 C. Preincubation with 12-O-tetradecanoylphorbol-13-acetate, which activates protein kinase C, resulted in the abolition of the IFNγ response, suggesting that protein Kinase C was involved in a negative feedback loop resulting in inhibition of IFNγ-induced [Ca2+](i) rise. Prior release of intracellularly stored Ca2+ with thapsigargin, the microsomal Ca2+ pump inhibitor, also abolished the response of IFNγ. Mobilization of [Ca2+](i) resulted in Ca2+ entry across the plasma membrane, which could be blocked by La3+ the inorganic Ca2+ antagonist. The tyrosine protein kinase inhibitor, genistein, inhibited the production of inositol phosphates and the elevation of [Ca2+](i) induced by IFNγ, but had no effect on ATP, suggesting that tyrosine protein kinase is involved in the signaling transduction of IFNγ. We conclude that the mobilization of intracellular Ca2+ and the production of inositol phosphates are two important signaling events for the action of IFNγ in human thyrocytes.
Persistent Identifierhttp://hdl.handle.net/10722/48963
ISSN
2015 Impact Factor: 4.159
2015 SCImago Journal Rankings: 2.363
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorKung, AWCen_HK
dc.contributor.authorLau, KSen_HK
dc.contributor.authorWong, NSen_HK
dc.date.accessioned2008-06-12T06:30:52Z-
dc.date.available2008-06-12T06:30:52Z-
dc.date.issued1995en_HK
dc.identifier.citationEndocrinology, 1995, v. 136 n. 11, p. 5028-5033en_HK
dc.identifier.issn0013-7227en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48963-
dc.description.abstractInterferon-γ (IFNγ) is believed to play a role in the pathogenesis of autoimmune thyroid disease, as it is known to exert diverse effects on thyroid metabolism. These include induction of human leukocyte antigen class II expression, inhibition of gene expression of thyroglobulin and thyroid peroxidase, as well as inhibition of cellular proliferation. However, the mechanism of action of IFNγ in thyrocytes has not been clearly defined. We studied the action of IFNγ on the production of inositol phosphates and intracellular Ca2+ mobilization in primary cultures of human thyrocytes using the fluorescent Ca2+ indicator furs-2. IFNγ increased the production of inositol mono-, bis-, and trisphosphates and caused a dose-dependent increase in intracellular Ca2+ ([Ca2+)(i)) at 37 C. Preincubation with 12-O-tetradecanoylphorbol-13-acetate, which activates protein kinase C, resulted in the abolition of the IFNγ response, suggesting that protein Kinase C was involved in a negative feedback loop resulting in inhibition of IFNγ-induced [Ca2+](i) rise. Prior release of intracellularly stored Ca2+ with thapsigargin, the microsomal Ca2+ pump inhibitor, also abolished the response of IFNγ. Mobilization of [Ca2+](i) resulted in Ca2+ entry across the plasma membrane, which could be blocked by La3+ the inorganic Ca2+ antagonist. The tyrosine protein kinase inhibitor, genistein, inhibited the production of inositol phosphates and the elevation of [Ca2+](i) induced by IFNγ, but had no effect on ATP, suggesting that tyrosine protein kinase is involved in the signaling transduction of IFNγ. We conclude that the mobilization of intracellular Ca2+ and the production of inositol phosphates are two important signaling events for the action of IFNγ in human thyrocytes.en_HK
dc.format.extent418 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
dc.publisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.orgen_HK
dc.relation.ispartofEndocrinologyen_HK
dc.rightsEndocrinology. Copyright © The Endocrine Society.en_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subject.meshCalcium - metabolismen_HK
dc.subject.meshInositol Phosphates - metabolismen_HK
dc.subject.meshInterferon Type II - pharmacologyen_HK
dc.subject.meshThyroid Gland - metabolismen_HK
dc.subject.meshAlkaloids - pharmacologyen_HK
dc.titleInterferon-γ increases intracellular calcium and inositol phosphates in primary human thyroid cell cultureen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0013-7227&volume=136&issue=11&spage=5028&epage=5033&date=1995&atitle=Interferon-gamma+increases+intracellular+calcium+and+inositol+phosphates+in+primary+human+thyroid+cell+cultureen_HK
dc.identifier.emailKung, AWC:awckung@hku.hken_HK
dc.identifier.emailWong, NS:nswong@hkucc.hku.hken_HK
dc.identifier.authorityKung, AWC=rp00368en_HK
dc.identifier.authorityWong, NS=rp00340en_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.pmid7588238-
dc.identifier.scopuseid_2-s2.0-0028973299en_HK
dc.identifier.hkuros11139-
dc.identifier.volume136en_HK
dc.identifier.issue11en_HK
dc.identifier.spage5028en_HK
dc.identifier.epage5033en_HK
dc.identifier.isiWOS:A1995TB98300040-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridKung, AWC=7102322339en_HK
dc.identifier.scopusauthoridLau, KS=35205833900en_HK
dc.identifier.scopusauthoridWong, NS=7202836641en_HK

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