Cancer Protein Description
This report provides a detailed description of a selected cancer protein with information collected from various sources, including UniProt, the Wellcome Trust Sanger Institute’s Catalogue of Somatic Mutations in Cancer (COSMIC), and the Atlas of Genetics and Cytogenetics in Oncology and Haematology.
| Protein Name: | BCL2L1 |
| Gene Name: | BCL2L1 |
| Protein Full Name: | Bcl-2-like protein 1 |
| Alias: | Apoptosis regulator Bcl-X; BCL2L; BCL2L1; BCL2-like 1; Bcl-2-like 1 protein; BCLX; Bcl-X; BCLXL; Bcl-xS; BLC2L |
| Mass (Da): | 26049 |
| Number AA: | 233 |
| UniProt ID: | Q07817 |
| Locus ID: | 598 |
| COSMIC ID: | BCL2L1 |
| Gene location on chromosome: | 20q11.21 |
| Cancer protein type: | OP |
| Effect of cancer mutation on protein: | GAIN |
| Effect of active protein on cancer: | PROMOTES |
| Number of cancer specimens: | 20231 |
| Percent of cancer specimens with mutations: | 0.16 |
| Normal role description: | This protein, one of two splice varients, plays an anti-apoptotic role by binding to voltage-dependent anion channnels (VDACs) thereby preventing the release of the caspase activator, CytC, from the mitochondrial membrane. Its splice variant has an opposite role -- one of pro-apoptosis. It has been shown to be over-expressed in: bladder cancer, breast cancer, hepatocellular carcinoma, follicular lymphomas, and in Non-Hodgkin's lymphoma. |
| Commentary on involvement of protein in cancer: | BCL-xL has been shown to inhibit cell death induced by a number of apoptotic stimuli including gamma irradiation, glucocorticoids, and anti-CD3 treatment (Boise et al., 1993; Chao et al., 1995; Chao et al., 1997). Down regulating the basal level of BCL-xL by RNA interference induces apoptosis in aged human fibroblasts without further stress, indicates that Bcl-xL is an important factor in cell-death control in old fibroblasts (Rochette et al., 2008). This was described in other cell type: in hepatocellular carcinoma cells Hepg2 (Lei et al., 2006), in nasopharyngeal carcinoma cells (Liu et al., 2005) or in esophageal cancer cells (Xie et al., 2006). In colorectal carcinoma (CRC) cell lines and in tissue it was shown that Bcl-xL contribute to apoptosis resistance. Same authors demonstrated that CRC cells with reduced Bcl-xL expression were more sensitive towards oxaliplatin- irinotecan, and 5-FU while, Bcl-xL plasmid transfection decreased chemotherapeutic drug-induced apoptosis (Schulze-Bergkamen et al., 2008). In another study using pancreatic, prostate and leukemic cells treated with benzylisothiocyanate Bcl-xL was phosphorylated and in parallel an enhancement of apoptosis (Basu et al., 2008). In HepG2 cells treated with topotecan it was shown that the expression of Bcl-xL was simultaneously down-regulated with the up-regulation of Bcl-xS in cytoplasm, which could explain the induction of apoptosis (Zhang et al., 2008). Bcl-2 and Bcl-xL inhibit apoptosis induced by a variety of agents in MCF-7 cells. MCF-7 cell lines expressing Bcl-xL and Bcl-2 were protected against apoptosis induced by TNFa and doxorubicin (Fiebig et al., 2006). PUMA (19q13.3-q13.4; p53-upregulated modulator of apoptosis) interacts with anti-apoptotic Bcl-2 and Bcl-xL and is dependent on Bax to induce apoptosis. PUMA initiates apoptosis in part by dissociating Bax and Bcl-xL, thereby promoting Bax multimerization and mitochondrial translocation (Ming et al., 2006). |