title: Heat shock proteins in porcine ovary: synthesis, accumulation and regulation by stress and hormones.
abstract: The present studies aimed to understand the interrelationships between stress, hormones and heat shock proteins (HSPs) in the ovary. We examined (1) whether HSP70.2, HSP72 and HSP105/110 can be produced and accumulated in porcine ovarian tissue, (2) whether these HSPs could be indicators of stress, i.e. whether two kinds of stress (high temperatures and malnutrition/serum deprivation) can affect them, and (3) whether some hormonal regulators of ovarian functions (insulin-like growth factor (IGF)-I, leptin and follicle-stimulating hormone (FSH)) can affect these HSPs and response of ovaries to HSP-related stress. We analysed the expression of HSP70.2, HSP72 and HSP105/110 mRNA (by using real-time reverse transcriptase polymerase chain reaction) in porcine ovarian granulosa cells, as well as the accumulation of HSP70 protein (by using sodium dodecyl sulphate polyacrylamide gel electrophoresis-Western) in either whole ovarian follicles and granulose cells cultured at normal (37.5°C) or high (41.5°C) temperature, with and without serum and with and without IGF-I, leptin and FSH. Expression of mRNA for HSP70.2, HSP72 and HSP105/110 in ovarian granulosa cells and accumulation of HSP70 protein in whole ovarian follicles and granulosa cells were demonstrated. In all the groups, addition of either IGF-I, leptin and FSH reduced the expression of HSP70.2, HSP72 and HSP105/110 mRNA. Both high temperature, serum deprivation and their combination resulted in increase in mRNAs for all three analysed HSPs. Additions of either IGF-I, leptin and FSH prevented the stimulatory effect of both high temperature and serum deprivation on the transcription of HSP70.2, HSP72 and HSP105/110. In contrast, high temperature reduced accumulation of peptide HSP70 in both ovarian follicles and granulosa cell. Serum deprivation promoted accumulation of HSP70 in granulosa cells, but not in ovarian follicles. Addition of IGF-I, leptin and FSH was able to alter accumulation of HSP70 in both follicles and granulosa cells. The present observations suggest (1) that HSPs can be synthesised in ovarian follicular granulosa cells; (2) that hormones (IGF-I, leptin and FSH) can inhibit, whilst stressors (both high temperature and malnutrition/serum deprivation) can stimulate transcription of HSP70.2, HSP72 and HSP105/110 genes, whilst heat stress, but not malnutrition, can promote depletion of HSP70 in ovarian cells, and (3) that hormones (IGF-I, leptin and FSH) can prevent stress-related changes in HSPs. The application of HSPs as indicators and mediators of stress and hormones on ovarian functions, as well as use of hormones and HSPs as anti-stressor molecules, are discussed.
authors.affiliation: Animal Production Research Centre Nitra, Luzianky near Nitra, Slovakia. sirotkin@cvzv.sk
authors.forename: Alexander V
authors.initials: AV
authors.lastname: Sirotkin
authors.forename: Miroslav
authors.initials: M
authors.lastname: Bauer
mesh_terms: D000818:Animals; D005260:Female; D005640:Follicle Stimulating Hormone / Q000378:metabolism*; D005508:Food Deprivation / Q000502:physiology; D006107:Granulosa Cells / Q000378:metabolism / Q000502:physiology; D050957:HSP110 Heat-Shock Proteins / Q000378:metabolism / Q000502:physiology; D050884:HSP72 Heat-Shock Proteins / Q000378:metabolism / Q000502:physiology; D006360:Heat-Shock Proteins / Q000096:biosynthesis / Q000378:metabolism*; D007334:Insulin-Like Growth Factor I / Q000378:metabolism*; D020738:Leptin / Q000378:metabolism*; D006080:Ovarian Follicle / Q000378:metabolism / Q000502:physiology; D010053:Ovary / Q000378:metabolism* / Q000502:physiology; D013312:Stress, Physiological; D013552:Swine; D013696:Temperature
chemical_list: D050957:HSP110 Heat-Shock Proteins; D050884:HSP72 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D020738:Leptin; D007334:Insulin-Like Growth Factor I; D005640:Follicle Stimulating Hormone