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Polyglutamine Domains Are Substrates of Tissue Transglutaminase: Does Transglutaminase Play a Role in Expanded CAG/Poly‐Q Neurodegenerative Diseases?
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1997
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Molecular BiologyNeurochemical BiomarkersSynaptic SignalingNeurobiology Of DiseaseProtein ExpressionDegenerative PathologyPolyglutamine DomainsNeurologyBiochemistryExpanded PolyglutamineLiver PhysiologyInherited Metabolic DiseaseNeurodegenerationCell BiologyTissue TransglutaminaseGuinea Pig LiverNeurodegenerative DiseasesGlutathione S ‐TransferaseNatural SciencesDegenerative DiseaseNeuroscienceCellular BiochemistryMedicine
Abstract: Huntington's disease and six other neurodegenerative diseases are associated with abnormal gene products containing expanded polyglutamine (poly‐Q; Q n ) domains (n ≥ 40). In the present work, we show that glutathione S ‐transferase (GST) fusion proteins containing a small, physiological‐length poly‐Q domain (GSTQ 10 ) or a large, pathological‐length poly‐Q domain (GSTQ 62 ) are excellent substrates of guinea pig liver (tissue) transglutaminase and that both GSTQ 10 and GSTQ 62 are activators of tissue transglutaminase‐catalyzed hydroxaminolysis of N ‐α‐carbobenzoxyglutaminylglycine. The present findings have implications for understanding the pathophysiological mechanisms of expanded CAG/poly‐Q domain diseases.