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- 저자 : Frangione, (검색결과 2 건)
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Conformation as a Therapeutic Target in the Prionoses and other Neurodegenerative Conditions
Wisniewski, Thomas,Sigurdsson, Einar M.,Aucouturier, Pierre,Frangione, B. 한림대학교 환경·생명과학연구소 2000 국제학술회의 Vol.2000 No.-
Abnormal protein conformation is increasingly being recognized as part of the pathogenesis of numerous neurodegenerative conditions. The common theme in all these diseases is the conversion of a normal cellular and/or circulating protein into an insoluble, aggregated, β-sheet rich form which is deposited in the brain. The aggregated proteins can accumulate extracellularly, often in the form of amyloid, or intracellularly producing inclusion bodies. These deposits are toxic and produce neuronal dysfunction and death. A unique category of the conformational conditions are prion related diseases(or prionoses), where the etiology is thought to be related to conversion of the normal prion protein, PrP□ ,into an infectious and pathogenic form, PrP□. However, the most common of these disorders is Alzheimer's disease(AD) where the central events is thought to be the conversion of normal soluble amyloid(sAβ) into fibrillar Aβin the form of neuritic plaques and congophilic angiopathy. Our growing understanding of the mechanisms involved in this category of disease, raises the possibility of therapeutic approaches based directly on the prevention and reversal of pathologic protein conformations. Possible approaches include synthetic β-sheet breaker peptides, which our preliminary data suggest may be useful for both AD and the prionoses, as well as immunological approaches where an antibody and/or cell mediated response is triggered against the aggregating abnormal protein.
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Conformation as a Therapeutic Target in the Prionoses and other Neurodegenerative Conditions
Wisniewski, Thomas,Sigurdsson, Einar M.,Aucouturier, Pierre,Frangione, B. 한림대학교 환경·생명과학연구소 2000 [일송 국제심포지엄] 노화와 만성퇴행성 신경질환 Vol.- No.3
Abnormal protein conformation is increasingly being recognized as part of the pathogenesis of numerous neurodegenerative conditions. The common theme in all these diseases is the conversion of a normal cellular and/or circulation protein into an insoluble, aggregated, β-sheet rich form which is deposited in the brain. The aggregated proteins can accumulate extracellularly, often in the form of amyloid, or intracellularly producing inclusion bodies. These deposits are toxic and produce neuronal dysfunction and death. A unique category of the conformational conditions are prion related diseases (or prionoses), where the etiology is thought to be related to conversion of the normal prion protein, PrP^c, into an infectious and pathogenic form, PrP^Sc. However, the most common of these disorders is Alzheimer's disease (AD) where the central event is thought to be the conversion of normal soluble amyloid (sAβ) into fibrillar Aβ in the form of neuritic plaques and congophilic angiopathy. Our growing understanding of the mechanisms involved in this category of disease, raises the pathologic protein conformations. Possible approaches include synthetic β-sheet breaker peptides, which our preliminary data suggest may be useful for both AD and the prionoses, as well as immunological approaches where an antibody and/or cell mediated response is triggered against the aggregation abnormal protein.
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