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Induction of stress genes by heat-shock in teleost erythrocytes

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:6062614
The eurythermal minnow Fundulus heteroclitus can tolerate rapid temperature changes of more than 20 C. Since heat-shock protein (hsp) synthesis and accumulation confers the transient thermotolerance in many cell types, they examined the heat-shock response of Fundulus for features that may correlate with its adaptability to thermal stress. Erythrocytes, prepared from 20 C acclimated fish, were heated at 40 c. Metabolically labeled (/sup 35/S-methionine) proteins were resolved by 2-d O'Farrell gels. Fundulus synthesize two major hsps of 74 kDa and 76 kDa respectively; each hsp is composed of 3 acidic polypeptides. The pattern of hsp synthesis showed interesting individual variability. Cells of some fish preferentially synthesized either hsp 76 or hsp 74; others synthesized both. While western immunoblots and silver-stained gels indicated that hsps are abundant proteins in unstressed cells, high rates of synthesis were only apparent during heat stress. According to RNA dot-blot analysis, heat-shock mRNA is present in unstressed cells but only increases by 50% following heat stress. Heat-shock RNA of unstressed cells is not translationally active because actinomycin-D inhibits synthesis of hsps. Hsps were synthesized within 15 min of heat stress and continued to be synthesized for more than 6 hours following recovery at 20 C.
Research Organization:
Johns Hopkins Univ., Baltimore, MD
OSTI ID:
6062614
Report Number(s):
CONF-870644-
Conference Information:
Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Journal Volume: 46:6
Country of Publication:
United States
Language:
English