Isolation and Characterization of a cDNA Encoding a Xenopus Immunoglobulin Binding Protein, BiP (Grp78)

Miskovic, Dragana; Salter–Cid, Luisa; Ohan, Nicholas; Flajnik, Martin F.; Heikkila, John J.

doi:10.1016/s0305-0491(96)00219-2

Cited by 22 publications

(19 citation statements)

References 37 publications

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“…It has been previously shown that glucosamine can disrupt ER function, cause ER stress, and promote the activation of the unfolded protein response in CHO, Xenopus A6, and L1210 leukemic cells (15)(16)(17). We investigated the capacity of different concentrations of glucose and glucosamine to cause an ER stress response in human cell types that are relevant to atherogenesis, including HASMC and Thp-1, as well as HepG2.…”

Section: Resultsmentioning

confidence: 99%

“…Enhanced hexosamine pathway activity has been implicated in insulin resistance, ␤-cell death, and atherosclerosis (11)(12)(13)(14). One characteristic of glucosamine that has been overlooked with respect to diabetes and atherogenesis is its ability to promote the misfolding of proteins in the endoplasmic reticulum (ER), a condition defined as ER stress (15)(16)(17). We have recently shown that activation of the cellular ER stress response correlates with atherogenic lesion development in hyperhomocysteinemic apolipoprotein E (apoE)-deficient mice (18).…”

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Glucosamine-Induced Endoplasmic Reticulum Dysfunction Is Associated With Accelerated Atherosclerosis in a Hyperglycemic Mouse Model

et al. 2006

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Diabetes is a major independent risk factor for cardiovascular disease and stroke; however, the molecular and cellular mechanisms by which diabetes contributes to the development of vascular disease are not fully understood. Our previous studies demonstrated that endoplasmic reticulum (ER) stress-inducing agents, including homocysteine, promote lipid accumulation and activate inflammatory pathways-the hallmark features of atherosclerosis. We hypothesize that the accumulation of intracellular glucosamine observed in diabetes may also promote atherogenesis via a mechanism that involves ER stress. In support of this theory, we demonstrate that glucosamine can induce ER stress in cell types relevant to the development of atherosclerosis, including human aortic smooth muscle cells, monocytes, and hepatocytes. Furthermore, we show that glucosamine-induced ER stress dysregulates lipid metabolism, leading to the accumulation of cholesterol in cultured cells. To examine the relevance of the ER stress pathway in vivo, we used a streptozotocin-induced hyperglycemic apolipoprotein E-deficient mouse model of atherosclerosis. Using molecular biological and histological techniques, we show that hyperglycemia is associated with tissue-specific ER stress, hepatic steatosis, and accelerated atherosclerosis. This novel mechanism may not only explain how diabetes and hyperglycemia promote atherosclerosis, but also provide a potential new target for therapeutic intervention. Diabetes 55:93-101, 2006

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Section: Resultsmentioning

confidence: 99%

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Glucosamine-Induced Endoplasmic Reticulum Dysfunction Is Associated With Accelerated Atherosclerosis in a Hyperglycemic Mouse Model

et al. 2006

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“…Five Xenopus laevis HSP70 members have been reported, including 2 inducible hsp70 genes, 2 constitutive hsc70 genes and the ER-resident BiP (Ali et al, 1996a;Bienz, 1984a;Miskovic et al, 1997). Hsc70 mRNA was constitutively present throughout Xenopus development, and was detectable globally (Ali et al, 1996a;Lang et al, 2000).…”

Section: Xenopus Hsp70 Developmental Regulationmentioning

confidence: 99%

Examination of the expression of the heat shock protein gene, hsp110, in Xenopus laevis cultured cells and embryos

Gauley

Heikkila

2006

Comparative Biochemistry and Physiology Part A: Molecular &

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Prokaryotic and eukaryotic organisms respond to various stressors with the production of heat shock proteins (HSPs). HSP110 is a large molecular mass HSP that is constitutively expressed in most adult mammalian tissues. In the present study, we have examined for the first time the expression of the hsp110 gene in Xenopus laevis cultured cells and embryos. The Xenopus hsp110 cDNA encodes an 854 amino acid protein, which shares 74% identity with mice and humans. In Xenopus A6 kidney epithelial cells hsp110 mRNA was detected constitutively and was heat inducible. Enhanced hsp110 mRNA levels were detected within 1 h, and remained elevated for at least 6 h. A similar accumulation of hsp70 mRNA was observed, but only in response to stress. Treatment of A6 cells with sodium arsenite and cadmium chloride also induced hsp110 and hsp70 mRNA accumulation. However, while ethanol treatment resulted in the accumulation of hsp70 mRNA no effect was seen for hsp110.Similarly, HSP110 and HSP70 protein increased after a 2 h heat shock and 12 h sodium arsenite treatment. The elevation in HSP110 and HSP70 protein in response to heat was detectable for up to 6 h. Recent studies with mice suggest an important role for HSP110 during development. Analysis of Xenopus embryos revealed that hsp110 mRNA was present in unfertilized eggs, indicating that it is a maternal mRNA, unlike the hsp70 message which was only detectable in response to heat shock. Heat shock-induced hsp110 mRNA accumulation was developmentally regulated, similar to hsp70, since it was not detectable until after the midblastula stage of development. Enhanced hsp110 mRNA accumulation was evident with heat shock at the blastula stage, and levels continued to increase reaching a maximum at the late tailbud stage. Message for the small heat shock protein, hsp27, was not detectable until the early tailbud stage, indicating that this hsp was not present maternally and was developmentally regulated. In situ hybridization analysis revealed that hsp110 mRNA was present in control embryos in the lens placode, spinal cord and somites, but increased upon heat shock in the anterior and posterior region, the lens placode, as well as in the somites and spinal cord. A similar iv distribution was observed for the hsp27 message, although it was not detectable until the early tailbud stage in control or heat-shocked embryos. The intracellular localization of HSP110 protein in response to stress was also investigated. HSP110 was detected predominantly in the cytoplasm in either a diffuse pattern or in long spindle-shaped fibres. Additionally, HSP110 was present in the nucleus. In heat shocked Xenopus A6 cells, HSP110 localized in distinct patterns surrounding the nucleus and was enhanced in the nucleus after prolonged heat stress. Sodium arsenite-treated cells displayed a similar pattern in which HSP110 localized on opposite ends of the nucleus. In contrast, in response to stress HSP30 was homogeneously distributed in the cytoplasm, moving into the nucleus only upon intense stress. ...

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“…development (Wang and Lindquist 1998) or the blastula stage of snail and sea urchin embryogenesis (Giudice 1989;Boon-Niermeijer 1991). Our laboratory and others have examined the developmental regulation of hsp70 gene expression during early embryogenesis of the frog, Xenopus laevis, in which 2 inducible hsp70 genes, 2 constitutive hsc70 genes, and one Bip gene have been described (Bienz 1984a(Bienz , 1984bAli et al 1996aAli et al , 1996bMiskovic et al 1997). X laevis hsp70 genes are not heat shock inducible until after the midblastula transition (MBT), which signals the onset of zygotic genome activation, even though HSF is detectable and heat activatable in cleavage-stage embryos (Bienz 1984a;Heikkila et al 1985Heikkila et al , 1987Heikkila et al , 1997Heikkila 1988, 1989;Ovsenek and Heikkila 1990;Ali et al 1996a).…”

Section: Introductionmentioning

confidence: 99%

Stress-induced, tissue-specific enrichment of hsp70 mRNA accumulation in Xenopus laevis embryos

Lang

Miskovic²,

Lo³

et al. 2000

Cell Stress Chaper

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In this study, we have employed whole-mount, in situ hybridization to study the spatial pattern of hsc70 and hsp70 mRNA accumulation in normal and heat shocked embryos during Xenopus laevis development. Our findings revealed that hsc70 mRNA was constitutively present in a global fashion throughout the embryo and was not heat inducible. Accumulation of hsp70 mRNA, however, was detected only in heat shocked embryos. Furthermore, hsp70 mRNA accumulation was enriched in a tissue-specific manner in X laevis tailbud embryos within 15 minutes of a 33ЊC heat shock. Abundant levels of heat shock-induced hsp70 mRNA were detected in the head region, including the lens placode, the cement gland, and in the somitic region and proctodeum. Preferential heat-induced accumulation of hsp70 mRNA was first detected at a heat shock temperature of 30ЊC. Placement of embryos at 22ЊC after a 1-hour, 33ЊC heat shock resulted in decreased hsp70 mRNA with time, but the message persisted in selected tissues, including the lens placode and somites. Treatment of tailbud embryos with either sodium arsenite or zinc chloride induced a tissuespecific enrichment of hsp70 mRNA in the lens placode and somitic region. These studies reveal the complex nature of the heat shock response in different embryonic tissues and suggest the presence of regulatory mechanisms that lead to a stressor-induced, tissue-specific enrichment of hsp70 mRNA.

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Isolation and Characterization of a cDNA Encoding a Xenopus Immunoglobulin Binding Protein, BiP (Grp78)

Cited by 22 publications

References 37 publications

Glucosamine-Induced Endoplasmic Reticulum Dysfunction Is Associated With Accelerated Atherosclerosis in a Hyperglycemic Mouse Model

Glucosamine-Induced Endoplasmic Reticulum Dysfunction Is Associated With Accelerated Atherosclerosis in a Hyperglycemic Mouse Model

Examination of the expression of the heat shock protein gene, hsp110, in Xenopus laevis cultured cells and embryos

Stress-induced, tissue-specific enrichment of hsp70 mRNA accumulation in Xenopus laevis embryos

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