Bcl 2 Family Members
Mostrando 1-12 de 98 artigos, teses e dissertações.
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1. Morphological and functional characterizations of Schwann cells stimulated with Mycobacterium leprae
Nerve damage, a characteristic of leprosy, is the cause of patient deformities and a consequence of Schwann cells (SC) infection by Mycobacterium leprae. Although function/dysfunction of SC in human diseases like leprosy is difficult to study, many in vitro models, including SC lines derived from rat and/or human Schwannomas, have been employed. ST88-14 is o
Memórias do Instituto Oswaldo Cruz. Publicado em: 2008-06
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2. Avaliação da expressão de genes e proteínas anti- e pró-apoptóticos em pacientes com diabetes mellitus tipo 1 e esclerose múltipla submetidos ao transplante autólogo de células-tronco hematopoéticas / Evaluation of anti and proapoptotic gene and protein expression in type 1 diabetes mellitus and multiple sclerosis patients submitted to autologous hematopoietic stem cell transplantation
Type 1 diabetes mellitus (T1DM) and multiple sclerosis (MS) are inflammatory, organ-specific autoimmune diseases characterized by selective destruction of insulin-producing pancreatic -cells and central nervous system, respectively, by autoreactive B and T cells. Deregulation of apoptotic machinery is supposed to contribute to self-tolerance breakdown and au
Publicado em: 2008
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3. ROLE OF Bcl-2 AND Bcl-XL IN ANGIOGENESIS
(...)Angiogenesis is defined as the development of new capillaries from pre-existing blood vessels. The hypothesis that tumor growth is angiogenesis dependent was proposed by Judah Folkman in 1971, and it has been confirmed by many investigators thereafter. We have shown that vascular endothelial growth factor (VEGF) induces Bcl-2 expression in endothelial c
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 2006
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4. 14-3-3 proteins in apoptosis
The once obscure members of the 14-3-3 protein family play significant roles in the determination of cell fate. By inhibiting the pro-apoptotic BAD (Bcl-2-antagonist of cell death) and the transcription factor FKHRL-1, 14-3-3 displays important anti-apoptotic characteristics. To date, five points of interaction of 14-3-3 with the apoptotic machinery have bee
Brazilian Journal of Medical and Biological Research. Publicado em: 2003-04
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5. Mitochondria, calcium and pro-apoptotic proteins as mediators in cell death signaling
Cellular Ca2+ signals are crucial in the control of most physiological processes, cell injury and programmed cell death through the regulation of a number of Ca2+-dependent enzymes such as phospholipases, proteases, and nucleases. Mitochondria along with the endoplasmic reticulum play pivotal roles in regulating intracellular Ca2+ content. Mitochondria are e
Brazilian Journal of Medical and Biological Research. Publicado em: 2003-02
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6. A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions.
Regulation of the cell death program involves physical interactions between different members of the Bcl-2 family that either promote or suppress apoptosis. The Bcl-2 homolog, Bak, promotes apoptosis and binds anti-apoptotic family members including Bcl-2 and Bcl-xL. We have identified a domain in Bak that is both necessary and sufficient for cytotoxic activ
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7. Conformational Changes in Bcl-2 Pro-survival Proteins Determine Their Capacity to Bind Ligands*
Antagonists of anti-apoptotic Bcl-2 family members hold promise as cancer therapeutics. Apoptosis is triggered when a peptide containing a BH3 motif or a small molecule BH3 peptidomimetic, such as ABT 737, binds to the relevant Bcl-2 family members. ABT-737 is an antagonist of Bcl-2, Bcl-xL, and Bcl-w but not of Mcl-1. Here we describe new structures of muta
American Society for Biochemistry and Molecular Biology.
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8. Bcl-2 family members do not inhibit apoptosis by binding the caspase activator Apaf-1
The Bcl-2 family of proteins regulates apoptosis, the cell death program triggered by activation of certain proteases (caspases). An attractive model for how Bcl-2 and its closest relatives prevent caspase activation is that they bind to and inactivate an adaptor protein required for procaspase processing. That model has been supported by reports that mammal
The National Academy of Sciences.
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9. Epstein-Barr Virus BALF1 Is a BCL-2-Like Antagonist of the Herpesvirus Antiapoptotic BCL-2 Proteins
Cellular BCL-2 family proteins can inhibit or induce programmed cell death in part by counteracting the activity of other BCL-2 family members. All sequenced gammaherpesviruses encode a BCL-2 homologue that potently inhibits apoptosis and apparently escapes some of the regulatory mechanisms that govern the functions of their cellular counterparts. Examples o
American Society for Microbiology.
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10. Interactions among members of the Bcl-2 protein family analyzed with a yeast two-hybrid system.
Interactions of the Bcl-2 protein with itself and other members of the Bcl-2 family, including Bcl-X-L, Bcl-X-S, Mcl-1, and Bax, were explored with a yeast two-hybrid system. Fusion proteins were created by linking Bcl-2 family proteins to a LexA DNA-binding domain or a B42 trans-activation domain. Protein-protein interactions were examined by expression of
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11. A Bcl-2 homolog encoded by Kaposi sarcoma-associated virus, human herpesvirus 8, inhibits apoptosis but does not heterodimerize with Bax or Bak
The Bcl-2 protein family is characterized by the ability to modulate cell death, and members of this family share two highly conserved domains called Bcl-2 homology 1 (BH1) and 2 (BH2) which have been shown to be critical for the death-repressor activity of Bcl-2 and Bcl-xL. Through sequence analysis we identified a novel viral Bcl-2 homolog, designated KSbc
The National Academy of Sciences of the USA.
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12. The BH3 Domain of Bcl-xS Is Required for Inhibition of the Antiapoptotic Function of Bcl-xL
bcl-x is a member of the bcl-2 family of genes. The major protein product, Bcl-xL, is a 233-amino-acid protein which has antiapoptotic properties. In contrast, one of the alternatively spliced transcripts of the bcl-x gene codes for the protein Bcl-xS, which lacks 63 amino acids present in Bcl-xL and has proapoptotic activity. Unlike other proapoptotic Bcl-2
American Society for Microbiology.