anticorps APG-2, anticorps HS24/P52, anticorps HSPH2, anticorps RY, anticorps hsp70, anticorps hsp70RY, anticorps CSA, anticorps GRP-75, anticorps GRP75, anticorps HSPA9B, anticorps MOT, anticorps MOT2, anticorps MTHSP75, anticorps PBP74, anticorps Hspa9a, anticorps csa, anticorps grp-75, anticorps grp75, anticorps hspa9, anticorps hspa9b, anticorps mortalin, anticorps mot, anticorps mot2, anticorps pbp74, anticorps mot-2, anticorps mthsp75, anticorps 74kDa, anticorps Csa, anticorps Grp75, anticorps Hsc74, anticorps Hsp74, anticorps Hsp74a, anticorps Mortalin, anticorps Mot-2, anticorps Mot2, anticorps Mthsp70, anticorps Pbp74, anticorps cb740, anticorps crs, anticorps wu:fc14d08, anticorps wu:fc27c10, anticorps wu:fc38a06, anticorps heat shock protein family A (Hsp70) member 4, anticorps heat shock protein family A (Hsp70) member 9, anticorps heat shock protein family A member 9, anticorps heat shock protein family A (Hsp70) member 9 S homeolog, anticorps stress-70 protein, mitochondrial, anticorps heat shock protein 9, anticorps heat shock protein Hsp9, anticorps HSPA4, anticorps HSPA9, anticorps Hspa9, anticorps hspa9.S, anticorps hspa9, anticorps LOC577721, anticorps hsp9
Sujet
Grp75, also known as mortalin, is a member of Hsp70 family of chaperone proteins that is not heat inducible (1, 2). Grp75 is actually induced under conditions of low glucose and other nutritional and environmental stresses. Grp75 resides primarily in the mitochondrial matrix, where it collaborates with Hsp60 in the re-folding of proteins translocated into this organelle (3, 4). Related forms may also be found in the cytosol or on the surface of the extracellular membrane. Other Grp75 functions include its ability to inactivate the tumor suppressor p53 (5). Studies have found that Grp75 is over-expressed in many tumor tissues and immortalized human cell lines, suggesting its role in the tumor formation (6). Grp75 is also implicated in cell aging, as its overexpression appears to prolong the life span of human fibroblasts (7). And finally, like its E. coli homolog DnaK (8), GRP75 possesses a cation-dependent ATPase activity considered central to its function as a chaperone (9, 10).Synonyms: 75 kDa glucose-regulated protein, HSPA9B, Heat shock 70 kDa protein 9, MOT, Mortalin, PBP74, Peptide-binding protein 74, Stress-70 protein