[Glucose regulated protein 78 kD].
One of the most important chaperones located on endoplasmic reticulum, GRP78, referred as BiP (immunoglobulin heavy chain binding protein), belongs to heat shock protein 70 family. GRP78 exists conservatively among a wide variety of biological species, and acts as a central regulator of endoplasmic reticulum (ER) functions, participating in ER protein folding and assembly process, and maintaining ER Ca2+ homeostasis, unfolded protein response and specific anti-apoptotic actions. Specific regulatory cis-elements such as ER stress response element (ERSE) and cAMP response element (CRE) were identified on the promoter of GRP78. Dynamic epigenetic interactions between specific transcription factors such as AFT6 and regulatory elements in GRP78 gene promoter might contribute to human GRP78 constitutive or inducible transcription, resulting from some physiological and pathological stresses. Recently, cellular relationship between GRP78 expression and hepatic steatosis, cancer and nervous system diseases in human was underwent further clinical and biochemical research, which will benefit to human beings.
Wu
Yi-Yuan
YY
Department of Biochemistry and Molecular Biology, Peking University Health Science Center, Beijing 100191, China.
Yang
Ye-Peng
YP
Li
Zai-Quan
ZQ
D000818:Animals; D004721:Endoplasmic Reticulum / Q000235:genetics / Q000378:metabolism; D000091342:Endoplasmic Reticulum Chaperone BiP; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D018832:Molecular Chaperones
D000091342:Endoplasmic Reticulum Chaperone BiP; D018840:HSP70 Heat-Shock Proteins; C000717247:HSPA5 protein, human; D006360:Heat-Shock Proteins; D008565:Membrane Proteins; D018832:Molecular Chaperones; C018551:glucose-regulated proteins