Osmotic stress of salmon stimulates upregulation of a cold inducible RNA binding protein (CIRP) similar to that of mammals and amphibians.
Salmon are subjected to hyperosmotic stress during transition from freshwater to the marine environment. A variety of mechanisms have evolved to allow movement of the animal from a hydrating to a dehydrating environment. Using differential assay of mRNA expression, a 1.3 kb transcript was found to be upregulated in branchial lamellae of salmon exposed to hyperosmotic conditions. The transcript contains an open reading frame of 618 nt coding for a 205 amino acid protein with a molecular mass of 21.5 kDa. The putative protein, dubbed salmon glycine-rich RNA binding protein (SGRP), possesses a high degree of identity (>70%) with the cold inducible RNA binding proteins (CIRP) of mammals and amphibians and contains the canonical features of these proteins including a single RNA recognition motif (RRM), high glycine content and conserved flanking motifs. SGRP mRNA was observed to increase in response to hyperosmotic stress of branchial tissue with maximum levels of expression after 48 h of exposure. Transcript also was observed in liver, kidney and heart but was not upregulated significantly by osmotic stress in these tissues. Exposure of isolated lamellae to heat stress and sodium arsenite, known inducers of hsps, did not stimulate accumulation of SGRP transcript. Similarly, inhibition of protein synthesis with cycloheximide and the MAPK and MEK signal transduction pathways with SB202190 and PD98059 failed to alter expression of the gene. Of significance was the absence of an increase in expression of SGRP in response to cold stress (DeltaT = 5 and 12 degrees C for 12 and 24 h). The findings of this research suggest that ectothermic salmon inhabiting boreal waters possess a protein analogous to the CIRPs currently identified in mammals and amphibians. In contrast to the function of CIRPs, SGRP appears to have a more prominent role in adaptation to hyperosmotic conditions rather than cold stress.
Dept of Fisheries, Animal and Veterinary Science, Building #14 East Farm, URI, Kingston, RI 02881, USA.
Feng
F
Pan
Jacques
J
Zarate
Arpita
A
Choudhury
Ryan
R
Rupprecht
Terence M
TM
Bradley
D000595:Amino Acid Sequence; D000663:Amphibians; D000818:Animals; D003001:Cloning, Molecular; D003080:Cold Temperature; D016384:Consensus Sequence; D018076:DNA, Complementary / Q000235:genetics; D005786:Gene Expression Regulation / Q000502:physiology*; D007700:Kinetics; D008322:Mammals; D008969:Molecular Sequence Data; D009994:Osmolar Concentration; D012313:RNA / Q000235:genetics; D016601:RNA-Binding Proteins / Q000235:genetics*; D020317:Salmo salar / Q000235:genetics*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D018076:DNA, Complementary; D016601:RNA-Binding Proteins; D012313:RNA