Localization of a human heat-shock HSP 70 gene sequence to chromosome 6 and detection of two other loci by somatic-cell hybrid and restriction fragment length polymorphism analysis

Goate, Alison M.; Cooper, David Neil; Hall, Christine; Leung, Thomas; Solomon, Ellen; Lim, Louis

doi:10.1007/bf00591072

Cited by 62 publications

(36 citation statements)

References 46 publications

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“…A panel of 26 genomic DNA samples was digested with 19 different restriction enzymes to detect RFLPs. Use of the hsp7o probe detected variations in these control samples digested with BgII, PstI and PvuII, as previously reported by Goate et al 4 The DNAs digested with MspI or ScaI were also polymorphic for hsp6O, and the hsp90 probe detected variations in samples digested with Sau961. The frequency of the variable fragments was determined for all polymorphisms (table 1).…”

supporting

confidence: 84%

Human heat shock protein gene polymorphisms and sudden infant death syndrome.

Rahim

Boyd

Patrick

et al. 1996

Archives of Disease in Childhood

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Comparison of the frequency of occurrence of restriction fragment length polymorphisms in control human DNAs and DNAs from infants dying from sudden infant death syndrome has indicated no significant difference in the case of restriction fragment length polymorphisms associated with the heat shock protein genes hsp7O and hsp9O. A highly significant difference was detected, however, in the case of the specific restriction fragment length polymorphisms detected by an hsp6O gene probe in MspI digests. (Arch Dis Child 1996;75:451-452) Keywords: heat shock proteins, restriction fragment length polymorphisms, sudden infant death syndrome, heat shock protein 60.Heat shock proteins play a central part in the normal physiology of cells.' Although they appear to be involved in the acquisition and maintenance of thermotolerance, other major roles include the repair of denatured cell proteins and functions as molecular 'chaperones' in the intracellular transmembrane transport of cellular proteins and in the construction of complex quaternary cellular protein structures. At present the cause of sudden infant death syndrome (SIDS) is unclear. Some deaths have been attributed to fever-like disorders,2 possibly brought on by overwrapping or by a virus infection. A possibility is that infants are susceptible to SIDS because some of the heat shock proteins are not produced or are defective, thus providing inadequate thermal protection. This could arise from defects in the DNA associated with genes encoding critical heat shock proteins. Results and discussion An initial screen of healthy human subjects was undertaken to determine whether sequence probes to the heat shock protein genes, hsp6O, hsp7O, and hsp9O could reveal any restriction fragment length polymorphisms (RFLPs). A panel of 26 genomic DNA samples was digested with 19 different restriction enzymes to detect RFLPs. Use of the hsp7o probe detected variations in these control samples digested with BgII, PstI and PvuII, as previously reported by Goate et al. 4 The DNAs digested with MspI or ScaI were also polymorphic for hsp6O, and the hsp90 probe detected variations in samples digested with Sau961. The frequency of the variable fragments was determined for all polymorphisms (table 1). The RFLPs detected using the hsp60 probe were more complex than those found using the hsp7O probe. With MspI, 16 constant fragments and six variant fragments were detected in 26 individuals. There was one hsp9o associated polymorphism, detected with Sau961 digested DNA. Nine of the fragments were invariant, whereas two others displayed a polymorphism characteristic of a two allele system.To determine if there was any difference in the nature of heat shock protein gene polymorphisms in infants dying from SIDS compared with the controls, 12 DNA samples from SIDS infants were examined with the same 19 restriction enzymes used in the initial screening for heat shock protein polymorphisms. Although the sample size of SIDS DNAs used was small it was sufficiently large to detect frequent...

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supporting

confidence: 84%

Human heat shock protein gene polymorphisms and sudden infant death syndrome.

Rahim

Boyd

Patrick

et al. 1996

Archives of Disease in Childhood

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“…For example, the hsp70 gene locus in humans is located in the MHC class III region of chromosome 6 (Goate et al 1987), supporting the idea that the chaperones have a dual role to mediate external stress signals and prevent the accumulation of intracellular protein damage. It is therefore interesting to speculate whether the transcellular signaling molecules that regulate the HSR and other cell stress responses between different tissues to regulate the PN correspond conceptually or functionally to endocrine, paracrine, or immune signals.…”

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confidence: 76%

Organismal proteostasis: role of cell-nonautonomous regulation and transcellular chaperone signaling

Oosten-Hawle

Morimoto

2014

Genes Dev.

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Protein quality control is essential in all organisms and regulated by the proteostasis network (PN) and cell stress response pathways that maintain a functional proteome to promote cellular health. In this review, we describe how metazoans employ multiple modes of cell-nonautonomous signaling across tissues to integrate and transmit the heat-shock response (HSR) for balanced expression of molecular chaperones. The HSR and other cell stress responses such as the unfolded protein response (UPR) can function autonomously in single-cell eukaryotes and tissue culture cells; however, within the context of a multicellular animal, the PN is regulated by cell-nonautonomous signaling through specific sensory neurons and by the process of transcellular chaperone signaling. These newly identified forms of stress signaling control the PN between neurons and nonneuronal somatic tissues to achieve balanced tissue expression of chaperones in response to environmental stress and to ensure that metastable aggregation-prone proteins expressed within any single tissue do not generate local proteotoxic risk. Transcellular chaperone signaling leads to the compensatory expression of chaperones in other somatic tissues of the animal, perhaps preventing the spread of proteotoxic damage. Thus, communication between subcellular compartments and across different cells and tissues maintains proteostasis when challenged by acute stress and upon chronic expression of metastable proteins. We propose that transcellular chaperone signaling provides a critical control step for the PN to maintain cellular and organismal health span.

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“…The differences between these alleles originate at positions -110 and +120 (Milner and Campbell, 1992;Cascino et al, 1993a andCascino et al, 1993b). The pst I restriction site, located on chromosome 6, lies within the hsp70-2 gene (Goate et al, 1987;Milner and Campbell, 1990). This is the polymorphic site used in analysing variations in the hsp70-2 gene by Pst I enzyme digests and restriction fragment length polymorphism (RFLP) analysis.…”

mentioning

confidence: 99%

“…This is the polymorphic site used in analysing variations in the hsp70-2 gene by Pst I enzyme digests and restriction fragment length polymorphism (RFLP) analysis. Two fragments with lengths of 8.5 kb and 9.0 kb represent hsp70-2 (L allele) and hsp70-2 (U allele) respectively (Goate et al, 1987;Favatier et al, 1997). In addition to this, a two-allele polymorphism exists within the 3′-untranslated region (3′utr) where each allele is represented by a 183 bp and a 188 bp fragment respectively.…”

mentioning

confidence: 99%

Hsp70 Induction and hsp70 Gene polymorphisms as Indicators of acclimatization under hyperthermic conditions

Kresfelder

Claassen

Cronjé

2006

Journal of Thermal Biology

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The possibility of using Hsp70 and hsp70 gene polymorphisms as markers of acclimatization was investigated. Volunteers (22) were subjected to an acclimatization regimen and blood analysed for Hsp70 (Hsp72) and hsp70 polymorphisms before and after a heat tolerance test. Physiological parameters denoting acclimatization, or not, were correlated to levels of Hsp70 and combination of hsp70 genes. Only individuals that acclimatized had decreased basal Hsp70 levels and increased ability to induce Hsp70 together with a specific hsp70 genotype combination. We propose that Hsp70 levels (basal vs. induced) with the genotype combination have the potential to be used as markers of acclimatization. Article Outline

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Localization of a human heat-shock HSP 70 gene sequence to chromosome 6 and detection of two other loci by somatic-cell hybrid and restriction fragment length polymorphism analysis

Cited by 62 publications

References 46 publications

Human heat shock protein gene polymorphisms and sudden infant death syndrome.

Human heat shock protein gene polymorphisms and sudden infant death syndrome.

Organismal proteostasis: role of cell-nonautonomous regulation and transcellular chaperone signaling

Hsp70 Induction and hsp70 Gene polymorphisms as Indicators of acclimatization under hyperthermic conditions

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