GATA-1 is a gene regulatory protein that is found in red blood cells and contributes to cell-type specific expression of the -globin gene and for the maturation of erythroblasts. Absence of GATA-1 leads to apoptosis and to a block in maturation. GATA-1 upregulates the expression of Bcl-XL and was found to be cleaved in a caspase-dependent manner upon activation of death receptors on the surface of erythroid cells, or alternatively, following deprivation of erythropoietin. Thus, GABA-1 appears to be involved in a complex regulation system determining the red blood cell's fate: differentiation, reversible maturation arrest or death (DeMaria et al., 1999, Nature, 401: 489-93).

Growth Arrest and DNA Damage-inducible genes (gadd genes) are induced following DNA damage. The gadd45 and gadd153 genes in particular are rapidly induced by DNA damaging agents. Induction of human GADD45 by ionizing radiation depends on normal function of p53. GADD45 stimulates DNA excision repair in vitro and inhibits entry of cells into S phase.

A natural flavone compound found in soy with chemopreventive effects, especially in case of breast cancer. Its anticancer effects may include topoisomerase II inhibition, induction of differentiation, inhibition of angiogenesis, inhibition of protein tyrosine kinase activity and apoptosis induction.

gld mutation
gld = generalized lymphoproliferative disease; spontaneous loss-of-function mutation in the FasL gene of mice. Leads to accumulation of lymphocytes.

GPI-anchored Molecule-Like protein (GML) shows a high degree of homology to the family of glycosyl-phosphatidylinositol (GPI)-anchored membrane proteins and was found to be regulated in a p53-dependent manner. Its expression level was correlated with the sensitivity of esophageal cancer cells to anti-cancer drugs and expression of GML enhances apoptosis induced by anti-cancer drugs and gamma-irradiation.

Adapter protein recruited to growth factor receptors (FGF, PDGF) containing SH2 and SH3 domains. Interacts and recruits SOS to the receptor complex.

Like Reaper, Grim encodes for another Drosophila protein with potent apoptotic activity. Together with Reaper and Hid, Grimis localized in the Reaper region and contains the N-terminal RHG motif. Apart from a polyglutamine tract and the RHG motif, the 138 aa of Grim do not exhibit any significant homologies in databank searches. Cell death induced by Grim is preceeded by caspase activation and can be inhibited by caspase inhibitors (reviewed by Abrams JM, Trends Cell Biol., 1999, 9: 435-440).

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