Cold Shock Induces the Synthesis of Stress Proteins in Human Keratinocytes

Holland, D.B.; Roberts, S. Gillian; Wood, Edward J.; Cunliffe, W.J.

doi:10.1111/1523-1747.ep12363791

Cited by 59 publications

(30 citation statements)

References 17 publications

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“…Although cultured human keratinocytes have been shown to respond to physical and chemical stresses by the induction of a 90-kD protein (Maytin et al 1990;Edwards et al 1991;Holland et al 1993), we observed that the stress of the wound healing conditions induced only a slight expression in basal and low suprabasal cells of the TE. In agreement with our results, no major difference is found in the level of expression of Hsp90 between oral lichen planus and normal mucosa (Bramanti et al 1995).…”

Section: Discussionmentioning

confidence: 60%

Expression of Heat Shock Proteins in Mouse Skin During Wound Healing

Laplante

Moulin

Auger

et al. 1998

J Histochem Cytochem.

160

114

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SUMMARYWound healing conditions generate a stressful environment for the cells involved in the regeneration process and are therefore postulated to influence the expression of heat shock proteins (Hsps). We have examined the expression of four Hsps (Hsp27, Hsp60, Hsp70 and Hsp90) and a keratin (keratin 6) by immunohistochemistry during cutaneous wound repair from Day 1 to Day 21 after wounding in the mouse. Hsps were constitutively expressed in normal mouse epidermis and their patterns of expression were modified during the healing process. The changes were not directly linked to the time course of the healing process but rather were dependent on the location of cells in the regenerating epidermis. In the thickened epidermis, Hsp60 was induced in basal and low suprabasal cells, Hsp70 showed a reduced expression, and Hsp90 and Hsp27 preserved a suprabasal pattern with an induction in basal and low suprabasal cells. All Hsps had a uniform pattern of expression in the migrating epithelial tongue. These observations suggest that the expression of Hsps in the neoepidermis is related to the proliferation, the migration, and the differentiation states of keratinocytes within the wound. (J Histochem Cytochem 46:1291-1301, 1998)

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Section: Discussionmentioning

confidence: 60%

Expression of Heat Shock Proteins in Mouse Skin During Wound Healing

Laplante

Moulin

Auger

et al. 1998

J Histochem Cytochem.

160

114

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“…It has been proven that it is an active response and cells synthesize specific cold inducible proteins (Kondo et al 1992;Holland et al 1993;Jones and Inouye 1994;Derry et al 1995;Nishiyama et al 1997a, b;Kaufmann et al 1999;Danno et al 2000;Sonna et al 2002;Dresios et al 2005;Yoon et al 2006;Baik et al 2006;Al-Fageeh et al 2006). A change in the phosphorylation patterns at the tyrosine residues of two proteins (~180 and 80 kDa) was also observed following reduction of the culture temperature providing further proof that there is an active signalling response to mild hypothermia in CHO (Kaufmann et al 1999).…”

Section: The Use Of Cell Cycle Arrest To Increase Recombinant Proteinmentioning

confidence: 88%

Proliferation control strategies to improve productivity and survival during CHO based production culture

2007

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Chinese Hamster Ovary cells are the primary system for the production of recombinant proteins for therapeutic use. Protein productivity is directly proportional to viable biomass, viability and culture longevity of the producer cells and a number of approaches have been taken to optimise these parameters. Cell cycle arrest, particularly in G1 phase, typically using reduced temperature cultivation and nutritional control have been used to enhance productivity in production cultures by prolonging the production phase, but the mechanism by which these approaches work is still not fully understood. In this article, we analyse the public literature on proliferation control approaches as they apply to production cell lines with particular reference to what is known about the mechanisms behind each approach.

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“…Evidence of a cold-induced cellular stress response has included reports of induction of HSPs on rewarming (47,60,65), phosphorylation of p38 MAP kinase during hypothermia (39), and translocation of ␤-crystallin from the nucleus to the cytoplasm (14). Cold-induced apoptosis occurs and appears to be sensitive to both the minimum temperature achieved and the duration of the exposure.…”

Section: Cellular Responses To Coldmentioning

confidence: 99%

Invited Review: Effects of heat and cold stress on mammalian gene expression

Sonna

Fujita

Gaffin

et al. 2002

Journal of Applied Physiology

547

409

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This review examines the effects of thermal stress on gene expression, with special emphasis on changes in the expression of genes other than heat shock proteins (HSPs). There are ∼50 genes not traditionally considered to be HSPs that have been shown, by conventional techniques, to change expression as a result of heat stress, and there are <20 genes (including HSPs) that have been shown to be affected by cold. These numbers will likely become much larger as gene chip array and proteomic technologies are applied to the study of the cell stress response. Several mechanisms have been identified by which gene expression may be altered by heat and cold stress. The similarities and differences between the cellular responses to heat and cold may yield key insights into how cells, and by extension tissues and organisms, survive and adapt to stress.

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Cold Shock Induces the Synthesis of Stress Proteins in Human Keratinocytes

Cited by 59 publications

References 17 publications

Expression of Heat Shock Proteins in Mouse Skin During Wound Healing

Expression of Heat Shock Proteins in Mouse Skin During Wound Healing

Proliferation control strategies to improve productivity and survival during CHO based production culture

Invited Review: Effects of heat and cold stress on mammalian gene expression

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