Expression and Phosphorylation of BiP/GRP78, a Molecular Chaperone in the Endoplasmic Reticulum, during the Differentiation of a Mouse Myeloblastic Cell Line.

Nakai, Asami; Kawatani, Toshio; Ohi, Shinji; Kawasaki, Hironaka; Yoshimori, Tamotsu; Tashiro, Yutaka; Miyata, Yoshihiko; Yahara, Ichiro; Satoh, Mamoru; Nagata, Kazuhiro

doi:10.1247/csf.20.33

Cited by 22 publications

(14 citation statements)

References 30 publications

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“…Misra et al (50) showed that insulin-induced increases in protein synthesis in murine peritoneal macrophages led to UPR induction, including GRP78 and XBP-1 up-regulation. Further, differentiation of the mouse myeloblastic cell line M1 via interleukin-6 was accompanied by GRP78 up-regulation (51).…”

Section: Discussionmentioning

confidence: 96%

Induction of the unfolded protein response after monocyte to macrophage differentiation augments cell survival in early atherosclerotic lesions

et al. 2010

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Endoplasmic reticulum (ER) stress causes macrophage cell death within advanced atherosclerotic lesions, thereby contributing to necrotic core formation and increasing the risk of atherothrombotic disease. However, unlike in advanced lesions, the appearance of dead/apoptotic macrophages in early lesions is less prominent. Given that activation of the unfolded protein response (UPR) is detected in early lesion-resident macrophages and can enhance cell survival against ER stress, we investigated whether UPR activation occurs after monocyte to macrophage differentiation and confers a cytoprotective advantage to the macrophage. Human peripheral blood monocytes were treated with monocyte colony-stimulating factor to induce macrophage differentiation, as assessed by changes in ultrastructure and scavenger receptor expression. UPR markers, including GRP78, GRP94, and spliced XBP-1, were induced after macrophage differentiation and occurred after a significant increase in de novo protein synthesis. UPR activation after differentiation reduced macrophage cell death by ER stress-inducing agents. Further, GRP78 overexpression in macrophages was sufficient to reduce ER stress-induced cell death. Consistent with these in vitro findings, UPR activation was observed in viable lesion-resident macrophages from human carotid arteries and from the aortas of apoE(-/-) mice. However, no evidence of apoptosis was observed in early lesion-resident macrophages from the aortas of apoE(-/-) mice. Thus, our findings that UPR activation occurs during macrophage differentiation and is cytoprotective against ER stress-inducing agents suggest an important cellular mechanism for macrophage survival within early atherosclerotic lesions.

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Section: Discussionmentioning

confidence: 96%

Induction of the unfolded protein response after monocyte to macrophage differentiation augments cell survival in early atherosclerotic lesions

et al. 2010

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“…With respect to GRPs, the GRP78 promoter is active in both differentiated and undifferentiated mouse embryonal carcinoma cells (Kim et al 1990). Furthermore, levels of both GRP78 and GRP94 increase when M1 cells are induced to differentiate into macrophage-like cells (Nakai et al 1995).…”

Section: Discussionmentioning

confidence: 99%

Glucose-regulated protein 78 (GRP78) is elevated in embryonic mouse heart and induced following hypoglycemic stress

Barnes

Smoak

2000

Anatomy and Embryology

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This study investigates the distribution and heart levels of glucose regulated protein (GRP) 78 during normal development and in response to hypoglycemia in the mouse. Results demonstrate that GRP78 is strongly expressed with in the heart, neural tube, gut endoderm, somites, and surface ectoderm of mouse embryos during early organogenesis, and GRP78 staining remains prominent in the heart from gestational days 9.5 through 13.5. Cardiac myocytes are the primary site of GRP78 expression within the heart. GRP78 levels are highest in the heart during early organogenesis and levels decrease significantly by the fetal period. GRP78 expression is increased after 24 h of hypoglycemia in the early organogenesis-stage heart. Considering the tissue specific pattern of GRP expression and changes during development of the heart, GRPs may play significant roles in the normal differentiation and development of cardiac tissue. GRP induction may also be involved in hypoglycemia-induced cardiac dysmorphogenesis.

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“…A decrease in mtHSP70 is important for the induced differentiation of HL-60 promyelocytic leukaemia cells (Xu et al 1999). By contrast, other studies showed an increase in Hsp70 (GRP78/Bip) during differentiation (Nakai et al 1995). In addition, Cotrupi & Maier (2004) have also suggested that cells in microgravity express Hsp70 in order to maintain their proliferative potential.…”

Section: Proteins With Decreased Expressionmentioning

confidence: 94%

Proteomic analysis of human osteoprogenitor response to disordered nanotopography

Kantawong

Burchmore

Gadegaard

et al. 2008

J. R. Soc. Interface.

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Previous studies have shown that microgroove-initiated contact guidance can induce bone formation in osteoprogenitor cells (OPGs) and produce changes in the cell proteome. For proteomic analysis, differential in-gel electrophoresis (DIGE) can be used as a powerful diagnostic method to provide comparable data between the proteomic profiles of cells cultured in different conditions. This study focuses on the response of OPGs to a novel nanoscale pit topography with osteoinductive properties compared with planar controls. Disordered nearsquare nanopits with 120 nm diameter and 100 nm depth with an average 300 nm centreto-centre spacing (300 nm spaced pits in square pattern, but with G50 nm disorder) were fabricated on 1!1 cm 2 polycaprolactone sheets. Human OPGs were seeded onto the test materials. DIGE analysis revealed changes in the expression of a number of distinct proteins, including upregulation of actin isoforms, beta-galectin1, vimentin and procollagen-proline, 2-oxoglutarate 4-dioxygenase and prolyl 4-hydroxylase. Downregulation of enolase, caldesmon, zyxin, GRASP55, Hsp70 (BiP/GRP78), RNH1, cathepsin D and Hsp27 was also observed. The differences in cell morphology and mineralization are also reported using histochemical techniques.

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Expression and Phosphorylation of BiP/GRP78, a Molecular Chaperone in the Endoplasmic Reticulum, during the Differentiation of a Mouse Myeloblastic Cell Line.

Cited by 22 publications

References 30 publications

Induction of the unfolded protein response after monocyte to macrophage differentiation augments cell survival in early atherosclerotic lesions

Induction of the unfolded protein response after monocyte to macrophage differentiation augments cell survival in early atherosclerotic lesions

Glucose-regulated protein 78 (GRP78) is elevated in embryonic mouse heart and induced following hypoglycemic stress

Proteomic analysis of human osteoprogenitor response to disordered nanotopography

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