24 resultados para tegumental proteins


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Journal of Electroanalytical Chemistry 541 (2003) 153-162

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Dissertação apresentada para obtenção do Grau de Doutor em Bioquímica, ramo de Bioquímica-Física, pela Universidade Nova de Lisboa, Faculdade de Ciências e Tecnologia

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Dissertação apresentada para a obtenção do Grau de Doutor em Bioquímica, especialidade de Bioquímica-Física pela Universidade Nova de Lisboa, Faculdade de Ciências e Tecnologia

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Journal of Proteome Research (2006)5: 2720-2726

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Journal of Biological Inorganic Chemistry (2010)15: 271-281

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The S100 proteins are 10-12 kDa EF-hand proteins that act as central regulators in a multitude of cellular processes including cell survival, proliferation, differentiation and motility. Consequently, many S100 proteins are implicated and display marked changes in their expression levels in many types of cancer, neurodegenerative disorders, inflammatory and autoimmune diseases. The structure and function of S100 proteins are modulated by metal ions via Ca2+ binding through EF-hand motifs and binding of Zn2+ and Cu2+ at additional sites, usually at the homodimer interfaces. Ca2+ binding modulates S100 conformational opening and thus promotes and affects the interaction with p53, the receptor for advanced glycation endproducts and Toll-like receptor 4, among many others. Structural plasticity also occurs at the quaternary level, where several S100 proteins self-assemble into multiple oligomeric states, many being functionally relevant. Recently, we have found that the S100A8/A9 proteins are involved in amyloidogenic processes in corpora amylacea of prostate cancer patients, and undergo metal-mediated amyloid oligomerization and fibrillation in vitro. Here we review the unique chemical and structural properties of S100 proteins that underlie the conformational changes resulting in their oligomerization upon metal ion binding and ultimately in functional control. The possibility that S100 proteins have intrinsic amyloid-forming capacity is also addressed, as well as the hypothesis that amyloid self-assemblies may, under particular physiological conditions, affect the S100 functions within the cellular milieu.

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A Thesis submitted at the Faculty Science and Technology of the New University of Lisbon for a degree in Doctor of Philosophy in Biochemistry with specialization in Physical Biochemistry

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Dissertation presented to obtain the Ph.D. degree in Biochemistry

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J Biol Inorg Chem (2011) 16:209–215 DOI 10.1007/s00775-010-0717-z

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J Biol Inorg Chem (2006) 11: 433–444 DOI 10.1007/s00775-006-0090-0

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Dissertação para obtenção do Grau de Doutor em Bioquímica, Especialidade Bioquímica Estrutural

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Dissertation presented to obtain the Ph.D degree in Biochemistry, Engineering and Technological Sciences

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Dissertation presented to obtain the Ph.D degree in Biochemistry.

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Dissertation presented to obtain the Ph.D degree in Biology