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  • 1
    Electronic Resource
    Electronic Resource
    Heat-shock induced proteins present in the cell nucleus of Chironomus tentans salivary gland (1979)
    [s.l.] : Nature Publishing Group
    Nature 281 (1979), S. 501-503 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] At the cytoplasmic level, the heat shock (39 C) response of Chironomus tentans salivary glands is similar to that observed in Drosophila (Fig. la, b). Several new proteins appear (arrows, Fig. Ib) with a major one of molecular weight (MW) about 68,000. (R.M.T. and M.V., in preparation.) This ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/281501a0
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  • 2
    Electronic Resource
    Electronic Resource
    Regulation of heat shock gene induction and expression during Drosophila development (1997)
    Springer
    Cellular and molecular life sciences 53 (1997), S. 104-113 
    Details
    ISSN: 1420-9071
    Keywords: Key words. Small heat shock proteins; Hsp27; Hsp23; gene regulation; development; heat shock response; oogenesis; spermatogenesis; Drosophila melanogaster.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Some heat shock genes are expressed in the absence of stress during embryogenesis and metamorphosis in the fruit fly Drosophila melanogaster. Their functions in these processes are unknown. During development, each of the four members of the small heat shock protein family (Hsp27, Hsp26, Hsp23 and Hsp22), which are coordinately induced in response to a heat stress, shows a specific pattern of expression in diverse tissues and cells. This expression is driven through cell-specific enhancers in the promoter regions of their genes. In addition, some of the Hsps show cell-specific induction by heat shock. Hsp23, for example, is only inducible in a single cell type (cone cells) of the eye ommatidium, while the other small Hsps are inducible in all cells of the eye unit. In germ line tissues such as testes, Hsp23 and 27 are both readily expressed in the absence of stress (albeit in distinct cell lineages) and cannot be further induced by heat shock. Hsp27 is expressed throughout oogenesi s, but its intracellular localization is stage-specific, being nuclear from germarium to stage 6 and cytoplasmic from stage 8 onwards. Finally the small Hsps show tissue-specific post-translational modifications. Thus the function(s) of the small Hsps may be modulated by different cell and developmental stage-specific mechanisms operating either on their expression, their cellular localization or their structure by post-translational modifications.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00000572
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  • 3
    Electronic Resource
    Electronic Resource
    Stage-specific localization of the small heat shock protein Hsp27 during oogenesis in Drosophila melanogaster (1996)
    Springer
    Chromosoma 105 (1996), S. 142-149 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The developmental and heat shock-induced expression of the small heat shock protein Hsp27 was investigated by confocal microscopy of whole-mount immunostained preparations of ovarioles during oogenesis in Drosophila melanogaster. In unstressed flies, Hsp27 was mainly associated with germline nurse cells throughout egg development. A small group of somatic follicle cells also expressed Hsp27 specifically at stages 8 to 10 of oogenesis. Interestingly, this Hsp showed a different intracellular localization depending on the stages of egg chamber development. Thus Hsp27 was localized in the nucleus of nurse cells during the first stages of oogenesis (from germarium to stage 6) whereas it showed a perinuclear and cytoplasmic localization from stage 8. After a heat shock, Hsp27 accumulated in somatic follicle cells surrounding the egg chamber whereas the expression of this small Hsp did not seem to be enhanced in nurse cells. The stage-dependent pattern of intracellular localization of Hsp27 observed in nurse cells of unstressed flies was also observed following heat shock. At late stages of oogenesis, Hsp27 also showed a perinuclear distribution in follicle and nurse cells after heat stress. These observations suggest that different factors may modulate the expression and intracellular distribution of Hsp27. This modulation may be associated with the specific activities occurring in each particular cell type throughout oogenesis during both normal development and under heat shock conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004120050169
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  • 4
    Electronic Resource
    Electronic Resource
    Immunoelectron microscope localization of Mr 90000 heat shock protein and Mr 70000 heat shock cognate protein in the salivary glands of Chironomus thummi (1992)
    Springer
    Chromosoma 102 (1992), S. 50-59 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The Mr 90000 heat shock protein (hsp 90) and one of the Mr 70000 heat shock cognate proteins (hsc 70) were localized by immunoelectron microscopy in salavary gland cells of normal and heat-shocked larvae of Chironomus thummi using polyclonal antibodies raised against Drosophila proteins. Immunoblotting after separation of proteins by gel electrophoresis shows that these antibodies cross-react with the corresponding proteins of Chironomus. Hsp 90 was localized both in the cytoplasm and in the nucleus, where it is associated with intrachromosomal and extrachromosomal ribonucleoprotein (RNP) fibrils, as well as with the peripheral region of compact chromatin. After heat shock the concentration of hsp 90 increases in the nucleus. This increase is prevented by actinomycin D administration during the heat shock. Hsp 90 is associated with the chromatin of puffs repressed by heat shock and with the RNP fibrils of actively transcribing heat shock puffs. Hsc 70 is mainly found in RNP fibrils and in the periphery of compact chromatin. During heat shock the concentration of hsc 70 decreases in the cytoplasm while it becomes more abundant in association with chromatin and intrachromosomal and extrachromosomal RNP fibrils. These results suggest a translocation of the existing protein from the cytoplasm toward the nucleus. They are supported by observations of the effect of heat shock carried out in the presence of actinomycin D.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00352290
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  • 5
    Electronic Resource
    Electronic Resource
    Hepatocellular carcinoma despite long-term survival in chronic tyrosinaemia I (2000)
    Springer
    Journal of inherited metabolic disease 23 (2000), S. 791-804 
    Details
    ISSN: 1573-2665
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Tyrosinaemia I (fumarylacetoacetate hydrolase deficiency) is an autosomal recessive inborn error of tyrosine metabolism that produces liver failure in infancy or a more chronic course of liver disease with cirrhosis, often complicated by hepatocellular carcinoma, in childhood or early adolescence. We studied a 37-year-old woman with tyrosinaemia I whose severe liver disease in infancy and rickets during childhood resolved with dietary therapy. From 14 years of age she resumed an unrestricted diet with the continued presence of the biochemical features of tyrosinaemia, yet maintained normal liver function. In adult years she accumulated only small amounts of succinylacetone. Despite this evolution to a mild biochemical and clinical phenotype, she eventually developed hepatocellular carcinoma. Her fumarylacetoacetate hydrolase genotype consists of a splice mutation, IVS6−1g〉t, and a novel missense mutation, Q279R. Studies of resected liver demonstrated the absence of hydrolytic activity and of immunological expression of fumarylacetoacetate hydrolase in liver tumour. In nontumoral areas, however, 53% of normal hydrolytic activity and immunologically present fumarylacetoacetate hydrolase was found. This case demonstrates the high risk of liver cancer in tyrosinaemia I even in a seemingly favourable biological environment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026756501669
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  • 6
    Electronic Resource
    Electronic Resource
    Hsp 78: A prominent heat shock protein of the lepidopteran Choristoneura fumiferana that is immunologically unrelated to members of the major Hsp families (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 39-53 
    Details
    ISSN: 0739-4462
    Keywords: spruce budworm ; Cf1 cells ; heat shock response ; lepidopteran cells ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Cultured cells of the spruce budworm (Choristoneura fumiferana) respond to heat shock with the new and/or enhanced synthesis of six proteins with Mrs of 84,000, 78,000, 70,000, 68,000, 21,000, and 14,000, as measured by one- and two-dimensional PAGE. The most prominent hsp of these cells is a 78,000 Da protein which is maximally induced at 39°C and which consists of three isoforms with different pl. Hsp 78 is found in the detergent-soluble cytosolic fraction of cell lysates. In vitro translation of RNA extracted from cultured cells and from larvae shows that the induction of hsp 78 is regulated mainly at the transcriptional level. Hsp 78 does not cross-react with a variety of antibodies made to members of the hsp 70 and hsp 83 families. In particular, antibodies to hsp 70 that do cross-react with a 70 kDa protein of C. fumiferana do not cross-react with hsp 78. Homologous 75-78 kDa hsps are also present in heat-shocked cells from other lepidopterans (Spodoptera frugiperda and Bombyx mori). Cf1 cells exposed to elevated levels of arsenite or cadmium respond with the new and/or enhanced synthesis of only two of their hsps (hsp 84 and hsp 70); hsp 78 is not induced by these treatments. The data suggest that hsp 78 of C. fumiferana represents a new family of hsps unique to lepidopterans. © 1994 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940250105
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