Apoptosis regulating gene

Details Apoptosis regulating gene Apoptosis regulating gene

1996-11-22

1998-12-01

Feisee, Lila

Chemistry: molecular biology and microbiology

Vector, per se

435325, 536 231, C12N 1511, C12N 500

Patent

active

058437738

DESCRIPTION:

BRIEF SUMMARY
BACKGROUND OF THE INVENTION

1. Field of the Invention
The present invention is related to a new apoptosis regulating gene, a plasmid containing the same, and a peptide encoded by the same.
Several publications are referenced in this application. Full citation to these references is found at the end of the specification immediately preceding the SEQUENCE LISTING or where the publication is mentioned.
2. Background of the Invention
Living cells are programmed to die spontaneously when they are useless. Such a programmed cell death is called "Apoptosis" and has widely attracted attentions in cell physiological fields.
Apoptosis plays an important role in many physiological processes, such as embryonic development, deletion of self-reactive T-cells (Williams, 1991; Williams and Smith, 1993), and in many diseases such as cancer or neurodegenerative disorders. Apoptosis also plays a critical role in maintaining homeostasis in many adult tissues. It is widely accepted that cell death and cell proliferation are precisely balanced to maintain the proper types of cells or tissues, and disruption of this balance can result in several pathological phenotypes (Williams, 1991).
Apoptosis is regulated by multiple factors, either the appearance of a stimulus such as glucocorticoid hormones for immature thymocyte (Trauth et al., 1989), or the disappearance of a stimulus such as IL-2 withdrawal from mature T lymphocyte (Duke and Cohen, 1986). Alternatively, apoptosis can also be induced by the removal of growth factors from hemopoietic lineage cells and neuronal cells (Williams et al., 1990; Garcia et al., 1992). It has been also that a number of signaling events, including cytosolic Ca.sup.++ increase, cAMP accumulation, activation of protein kinase C and activation of protein tyrosine kinase, regulate apoptotic cell death (McCondey and Orrenus, 1994). Several genes regulating apoptosis in various tissues and circumstances were reported: P53 and Bcl-2 are two of the most studied regulatory genes.
Apoptosis is induced by inactivation of Rb in the lens (Morgenbesser et al., 1994; Williams et al., 1994) and by .gamma.-irradiation in the lymphocytes (Clarke et al., 1993; Lowe et al., 1993), respectively in the presence of tumor suppressor p53. Overexpression of p53 can induce either growth arrest or apoptosis depending on the cell type, whereas loss of p53 function can produce resistance to apoptotic cell death, leading to aggressive tumors (Williams, 1994). Mutation of p53 is associated with the human malignancies, including lung, breast, colorectal, prostate and multiple hemopoietic tumors (Fisher, 1999), revealing a correlation between a perturbation of apoptosis and carcinogenesis.
Bcl-2 is homologous to the C. elegans ced-9 gene, an apoptosis-blocking gene (Hengartner and Horvitz, 1994), and is abundantly expressed in follicular lymphoma that is resulted from the t(14;18) chromosomal translocation (Tsujimoto et al., 1985). It has been known that deaths of a variety of cell types can be prevented by Bcl-2 overexpression, although not all forms of cell death are inhibited (Williams, 1991). Thymocyte overexpressing Bcl-2 were resistant to the induction of apoptosis by glucocorticoid, radiation or anti-CD3 treatments (Sentman et al., 1991; Strasser et al., 1991). Overexpression of Bcl-2 in B cell compartments increases the number of mature resting B cells (Strasser et al., 1991, due to extended cell survival rather than increases proliferation. The action mechanism of the Bcl-2 is not clear yet. Recently, Bcl-2 has been reported to protect apoptosis independent of the inhibition of reactive oxygen species (Jacobson and Raff, 1995; Shimize et al., 1995), which is contradictory to the previous results (Hockenbery et al., 1993).
Several genes with Bcl-2 related sequences have been reported. Bax, 21 kDa protein, was known to have 21% homology to Bcl-2, and inhibits the function of Bcl-2, perhaps by forming Bcl-2-Bax complex (Oltvai et al., 1993). Bcl-x was reported to have a high-level homology to Bcl-2 and like Bcl-2 prevents a

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