Endoplasmic Reticulum Stress Proteins Block Oxidant-induced Ca2+ Increases and Cell Death

Liu, Hong; Miller, Elizabeth M.; Water, Bob van de; Stevens, James

doi:10.1074/jbc.273.21.12858

Cited by 186 publications

(169 citation statements)

References 62 publications

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“…It follows that by blocking or minimizing ER stress, it may be possible to attenuate the induction of lipid biosynthesis. In support of this concept, we observed that stable overexpression of GRP78/BiP, which protects cells from agents or conditions known to cause ER stress (39,40), inhibits homocysteine-induced expression of genes involved in cholesterol biosynthesis in cultured human cells.…”

Section: Figure 11mentioning

confidence: 58%

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Homocysteine-induced endoplasmic reticulum stress causes dysregulation of the cholesterol and triglyceride biosynthetic pathways

et al. 2001

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Section: Figure 11mentioning

confidence: 58%

“…Overexpression of GRP78/BiP has been reported to protect cells from ER stress (39,40). Stably transfected cells overexpressing GRP78/BiP were generated to assess whether blocking homocysteine-induced ER stress attenuated the expression of SREBP-1 and IPP isomerase.…”

Section: Induction Of Ipp Isomerase Gene Expression By Er Stressmentioning

confidence: 99%

Homocysteine-induced endoplasmic reticulum stress causes dysregulation of the cholesterol and triglyceride biosynthetic pathways

et al. 2001

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“…Moreover, since studies have shown that increased expression of ER stress proteins prevents Ca 2 ϩ depletion from the ER and protects against cellular damage and death (Lievremont et al 1997;Liu et al 1997Liu et al , 1998Yu et al 1999), it is possible that an elevation of these proteins in this subgroup of patients may have been an attempt to compen-sate for these neuropathologic changes in this patient group. Indeed, several recent studies are suggestive of cellular loss and glial changes in cortical regions of patients with MDD, which may be correlated with severity of illness (Ongur et al 1998;Rajkowska et al 1999).…”

Section: Discussionmentioning

confidence: 99%

Increased Temporal Cortex ER Stress Proteins in Depressed Subjects Who Died by Suicide

Bown

Wang

MacQueen

et al. 2000

Neuropsychopharmacology

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Regulation of ER stress proteins, such as the 78-kilodalton glucose regulated protein (GRP78) by chronic treatment with mood stabilizing drugs suggests that this family of proteins may be involved in the pathophysiology of mood disorders. Indeed, increased levels of GRP78, GRP94, and calreticulin, a third member of the ERCurrent theories of the pathophysiology of mood disorders suggest that prolonged increases in glucocorticoid levels, likely the result of prolonged environmental stress, lead to biochemical changes in cortical and limbic neurons that leave individuals vulnerable to depression (Duman et al. 1997). A number of studies have found evidence of neuronal atrophy and loss of hippocampal neurons in response to stress (Magarinos et al. 1996;Uno et al. 1989;Sapolsky et al. 1985), and a report of reduced hippocampal volumes in elderly patients with histories of depression suggests that analogous processes may occur in individuals with depression (Sheline et al. 1996). Some models of mood disorders (Hyman and Nestler 1996; Post 1992) have attempted to incorporate the notion of compensatory processes into an understanding of the pathophysiologic changes that occur in patients with mood disorders, but few studies have tested these notions empirically (Post 1992). Part of the difficulty has been identifying neuroprotective mechanisms that may be of relevance for mood disorders.Recently, we found that treatment with the mood stabilizing drugs, valproate and carbamazepine, increased expression of the 78-kilodalton glucose-regulated protein (GRP78) . GRP78 is a member of the ER stress protein family that includes GRP94 and calreticulin, all of which function as Ca 2 ϩ binding proteins and molecular chaperones to assist in the regulation of protein folding (Gething 1997). These proteins have neuroprotective properties, are induced by seizures and ischemic damage, and may be involved in Alzheimer's disease pathology (Yu et al. 1999;Lowenstein et al. 1994;Hamos et al. 1991).Increased expression of ER stress proteins by mood stabilizing drugs suggest that these proteins may be in- METHODS Postmortem brain tissue was obtained from the StanleyFoundation Neuropathology Consortium (4 groups of n ϭ 15 age-and sex-matched subjects, i.e., subjects with bipolar disorder (BD), subjects with Major Depressive Disorder (MDD), subjects with schizophrenia (SCZ), and non-psychiatric, non-neurologic comparison subjects) (Johnston et al. 1997). Details on dissection and clinical characteristics have been previously published (Dowlatshahi et al. 1998(Dowlatshahi et al. , 1999. Briefly, all medical records for psychiatric cases were reviewed by two psychiatrists. Diagnosis was determined according to DSM-IV criteria. If there was disagreement about the diagnosis, a third psychiatrist read the records. If a diagnosis could not be established, a family member was then interviewed. All interviewed relatives were first degree except for two (one aunt and one father-in-law). Similarly, a clinical interview was performed with a family member...

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“…Recently, it has been shown that a variety of toxic insults, including calcium ionophores, inhibitors of glycosylation, chemical toxicants, and oxidative stress, can cause ER stress and ultimately lead to cell death. [31][32][33][34][35][36][37][38][39] We found that significant ER stress and resultant apoptosis occurred in cells expressing mutated COMP compared with wild-type COMP and discuss the significance of this in PSACH.…”

mentioning

confidence: 99%

Mutation (D472Y) in the Type 3 Repeat Domain of Cartilage Oligomeric Matrix Protein Affects Its Early Vesicle Trafficking in Endoplasmic Reticulum and Induces Apoptosis

Hashimoto

Tomiyama

Yamano

et al. 2003

The American Journal of Pathology

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Cartilage oligomeric matrix protein (COMP) is a large pentameric extracellular glycoprotein found in cartilage, tendon, and synovium, and plays structural roles in cartilage as the fifth member of the thrombospondin family. Familial mutations in type 3 repeats of COMP are known to cause pseudoachondroplasia (PSACH) and multiple epiphyseal dysplasia (EDM1). Although such mutations induce enlarged rough endoplasmic reticulum (rER) as a morphological change, the metabolic trafficking of mutated COMP remains unclear. In transfected COS7 cells, wild-type COMP was rapidly secreted into culture medium, while the great majority of COMP with the type 3 repeats mutation (D472Y) remained in the cells and a small portion of mutated COMP was secreted. This finding was followed up with a confocal study with an antibody specific to COMP, which demonstrated mutated COMP tightly associated with abnormally enlarged rER. Phosphorylated eIF2␣, an ER stress protein, was expressed as a pathological reaction in virtually all COS7 cells expressing mutated but not wild-type COMP. Moreover, COS7 cells expressing mutated COMP exhibited significantly more apoptotic reaction than those expressing wild-type COMP. Pathological accumulation of COMP in rER and apoptosis in COS7 cells that were induced by the mutation (D472Y) in COMP imply that COMP mutations play a role in the pathogenesis of PSACH. (Am J

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Endoplasmic Reticulum Stress Proteins Block Oxidant-induced Ca2+ Increases and Cell Death

Cited by 186 publications

References 62 publications

Homocysteine-induced endoplasmic reticulum stress causes dysregulation of the cholesterol and triglyceride biosynthetic pathways

Homocysteine-induced endoplasmic reticulum stress causes dysregulation of the cholesterol and triglyceride biosynthetic pathways

Increased Temporal Cortex ER Stress Proteins in Depressed Subjects Who Died by Suicide

Mutation (D472Y) in the Type 3 Repeat Domain of Cartilage Oligomeric Matrix Protein Affects Its Early Vesicle Trafficking in Endoplasmic Reticulum and Induces Apoptosis

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