Amino acid analogs while inducing heat shock proteins sensitize CHO cells to thermal damage

Li, Gloria C.; Laszlo, Andrei

doi:10.1002/jcp.1041220114

Cited by 97 publications

(52 citation statements)

References 23 publications

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“…HSP70 is the most prominent protein induced by a variety of stress conditions in all cells investigated (Schlesinger, 1990;Pelham, 1990 (Li & Laszlo, 1985;Riabowol et al, 1988;Johnston & Kucey, 1988). Most recently, it has been shown that cells transfected with hsp70 governed by a constitutive promoter were more resistant to heat-shock, directly supporting the above notion (Angelidis et al, 1991;Li et al, 1991).…”

Section: Discussionmentioning

confidence: 86%

Induction of HSP70 is associated with vincristine resistance in heat-shocked 9L rat brain tumour cells

Lee¹,

Lin²,

Chen³

et al. 1992

Br J Cancer

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SummaryThe most prominent cellular changes in heat-shock response are induction of HSPs synthesis and reorganisation of cytoskeleton. Vincristine was used as a tool to evaluate the integrity of microtubules in 9L rat brain tumour cells recovering from heat-shock treatment. Cells treated at 45°C for 15 min and recovered under normal growing condition became resistant to vincristine-inflicted cytotoxicity and microtubule destruction. Among all HSPs, the level of HSP70 and the degree of vincristine resistance are best correlated. HSP70and tubulin were found to be associated with each other as they were co-immunoprecipitated by either anti-HSP70 or anti-p-tubulin monoclonal antibody. The current studies establish for the first time that HSP70can complex with tubulin in cells and this association may stabilise the organisation of microtubules thus protect the heat-treated cells from vincristine damage. These findings are noteworthy in combining hyperthermia and chemotherapy in the management of malignant diseases.Heat-shock proteins (HSPs) are a small set of proteins induced in cells subjected to supraoptimal temperature and other related physiological stresses (Lindquist & Craig, 1988;Schlesinger, 1990;Schlesinger et al., 1990; Morimoto et al., 1990). The synthesis of HSPs is suggested to be related to the development of thermotolerance in cells that survived the initial heat-treatment (Li & Mak, 1985;Hahn & Li, 1990;Black & Subjeck, 1990). The HSPs are highly conservative and usually termed by their apparent molecular weights. Three classes of major HSPs, i.e., HSPl10, 90 and 70 are commonly detected in mammalian cells (Lindquist & Craig, 1988). HSP70 exists as a family in most organisms and has been the most extensively studied. In rodent cells, this family consists of two closely related proteins (>80% homology at the amino acid level) which have been known as the constitutive form of HSP70 (also known as HSC70, designated as HSP72 hereafter because of its slightly higher molecular weight) and the inducible form of HSP70 (designated as the HSP70 hereafter) (Hightower & White, 1981;Lee et al., 1991). HSP72 is slightly heat inducible, constitutively expressed and found at higher levels in growing cells than in resting cells (Pelham, 1986). This protein was found to be multifunctional. It functions as clathrin uncoating ATPase (Chappell et al., 1986;Deluca-Flaherty et al., 1990) and as molecular chaperone that binds to nascent polypeptides and maintains them in unfolded states, to facilitate their intracellular translocation (Deshaies et al., 1988;Chirico et al., 1988) and/or to accelerate their proper folding and oligomerisation (Beckmann et al., 1990;Pelham, 1990). Recently, HSP72 has been shown to be involved the in vivo assembly of microtubules (Gupta, 1990). On the other hand, HSP70 is highly heat inducible and hardly detectable under normal conditions. Its function is suggested to be similar to that of HSP72 because of the high degree of homology between these two proteins (Lindquist & Craig, 1988). In additi...

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Section: Discussionmentioning

confidence: 86%

Induction of HSP70 is associated with vincristine resistance in heat-shocked 9L rat brain tumour cells

Lee¹,

Lin²,

Chen³

et al. 1992

Br J Cancer

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“…(ii) Pretreatment of the cells with sodium arsenite, removal of the metal, and recovery of the cells for 12 h caused most of the 28-kDa protein to remain within the detergent soluble phase after a heat shock treatment. (iii) Pretreatment of the cells with an amino acid analog of proline, azetidine, thereby resulting in the production of nonfunctional HSPs (20,33,39,56), and subsequent heat shock treatment resulted in the protein fractionating within the insoluble pellet, similar to results with the nontolerant cells. However, pretreatment with the analog and then removal of the drug, thereby allowing for production of functional stress proteins (20,39,56), now resulted in significantly more of the protein remaining within the soluble phase after heat shock treatment, similar to the effect with thermotolerant cells.…”

Section: Discussionmentioning

confidence: 97%

Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein.

Arrigo¹,

Suhan²,

Welch³

1988

Mol. Cell. Biol.

326

231

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Mammalian cells grown at 37C contain a single low-molecular-weight heat shock (or stress) protein with an apparent mass of 28 kilodaltons (kDa) whose synthesis increases in cells after exposure (6,23,24,26,27,37). The only obvious common property of these proteins from different organisms is their homology to the a-crystallin proteins present ill the lens (24,25,43). Because both the a-crystallins and the low-MW HSPs are isolated as rather large aggregates (i.e., 200 to 800 kDa from normal, nonheated cells) (1-3, 4, 6, 7, 14, 15, 46), we suspect that their observed homology resides in those domains responsible for the self-assembling properties of the proteins.We recently described the characterization and purification of the low-MW HSP from HeLa cells (6). The

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“…일반적으로 동물 세포 나 기관이 스트레스에 노출되면 대부분의 다른 단백질은 합 성이 억제되나, HSPs는 특이적으로 빠르게 합성된다고 한다. HSPs는 세포의 항상성에 중요한 역할을 하며, 고온이나 중금 속, 산화 스트레스 등에 의해 발현량이 증가하며, 원핵․진핵 생물의 모든 세포에서 검출된다 (Craig, 1985;Li and Laszlo, 1985;Lindquist, 1986;Lindquist and Craig, 1988;Young et al, 2001;Powers and Workman, 2007). 특히, HSP-70은 스 트레스에 가장 민감하게 반응하는 열 스트레스 단백질로 닭 에 있어서도 제한급여, 수송, 격리와 같은 스트레스원에 노 출되면 HSP-70 유전자의 발현이 현저하게 상승한다고 한다 (Kamboh et al, 2013;Zulkifli et al, 2014).…”

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Comparison of Stress Response in Diallel Crossed Korean Domestic Chicken Breeds

Cho¹,

Park²,

Choi³

et al. 2016

Korean Journal of Poultry Science

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To establish a new synthetic Korean meat chicken breed, we tested 5×5 diallel cross mating experiment with domestic chicken breeds. Comparing stress responses among diallel crossed chicken breeds, we analyzed telomere length, DNA damage and expressions of heat shock protein genes (HSPs) as the markers of the stress response. The telomere length was measured by quantitative fluorescence in situ hybridization on the nuclei of lymphocytes. The expression levels of HSP-70, HSP-90α and HSP-90β genes were analyzed by quantitative real-time polymerase chain reaction in lymphocytes. The DNA damage rate of lymphocytes was quantified by the comet assay known as the single cell gel electrophoresis. In results, there were significant differences in the values of the stress markers such as telomere length, HSPs and DNA damage rate, and also were significant differences in viabilities and body weights among the 5×5 diallel crossed chicken breeds. The telomere shortening rate, expression values of HSPs and DNA damage rate were significant low in W and Y crossed chickens compare to the others, but GG pure breed showed the highest values in the 25 crossed chickens. Estimating correlation coefficient, the survival rate positively correlated to telomere length, but negatively correlated to the expression levels of HSP-70, HSP-90α, HSP-90β genes and to the value of % DNA in tail as DNA damage rate. The expression levels of HSP-70, HSP-90α and HSP-90β genes of dead chickens had significantly higher than those of survival chickens. According to the results on the stress marker analysis, it would be considered that the crossed breeds had more stress resistant than the pure breeds, and the crossed chickens with a light strain such as W or Y were relatively resistant to stress, but the crossed chickens with a heavy strain such as G, H, F were susceptible to stress.

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Amino acid analogs while inducing heat shock proteins sensitize CHO cells to thermal damage

Cited by 97 publications

References 23 publications

Induction of HSP70 is associated with vincristine resistance in heat-shocked 9L rat brain tumour cells

Induction of HSP70 is associated with vincristine resistance in heat-shocked 9L rat brain tumour cells

Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein.

Comparison of Stress Response in Diallel Crossed Korean Domestic Chicken Breeds

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