Heat Shock Proteins in Branchial Tissue in Atlantic Salmon (Salmo salar)

Lamellae isolated from gill arches of Atlantic salmon were incubated in 15, 25 and 21°c. Five heat shock or stress proteins (hsps) with molecular weights of 54, 71, 72, 82 and 87 kDal appeared after incubation at 25° c. At 21°c all five proteins were induced in greater quantity and an additional pro...

Full description

Bibliographic Details
Main Author: Allen, Jennifer L.
Format: Text
Language:unknown
Published: DigitalCommons@URI 1993
Subjects:
Online Access:https://digitalcommons.uri.edu/theses/1095
https://doi.org/10.23860/thesis-allen-jennifer-1993
https://digitalcommons.uri.edu/context/theses/article/2103/viewcontent/thesis_allen_jennifer_1993.pdf
id ftunivrhodeislan:oai:digitalcommons.uri.edu:theses-2103
record_format openpolar
spelling ftunivrhodeislan:oai:digitalcommons.uri.edu:theses-2103 2023-07-30T04:02:25+02:00 Heat Shock Proteins in Branchial Tissue in Atlantic Salmon (Salmo salar) Allen, Jennifer L. 1993-01-01T08:00:00Z application/pdf https://digitalcommons.uri.edu/theses/1095 https://doi.org/10.23860/thesis-allen-jennifer-1993 https://digitalcommons.uri.edu/context/theses/article/2103/viewcontent/thesis_allen_jennifer_1993.pdf unknown DigitalCommons@URI https://digitalcommons.uri.edu/theses/1095 doi:10.23860/thesis-allen-jennifer-1993 https://digitalcommons.uri.edu/context/theses/article/2103/viewcontent/thesis_allen_jennifer_1993.pdf Open Access Master's Theses text 1993 ftunivrhodeislan https://doi.org/10.23860/thesis-allen-jennifer-1993 2023-07-17T18:55:50Z Lamellae isolated from gill arches of Atlantic salmon were incubated in 15, 25 and 21°c. Five heat shock or stress proteins (hsps) with molecular weights of 54, 71, 72, 82 and 87 kDal appeared after incubation at 25° c. At 21°c all five proteins were induced in greater quantity and an additional protein of 67 kDal was observed. The time 0 required for the induction of hsps at 25° c was determined by labeling the gills in vitro for one hour after intervals of up to four hours of heat shock. All five proteins were apparent after one hour of heat shock and maximal by two hours. The lamallae continued to synthesize hsps throughout the four hours. Stress proteins were not induced in lamallae exposed to 25 to 300 uM of sodium arsenite or 50 to 500 mM sodium chloride. Although viability was high under these conditions, overall protein synthesis was suppressed. Lamellae proteins induced by heat shock at 25°c were incubated with monoclonal and polyclonal antibodies to hsps 60, 70 and 90. Only the antibodies to constitutive/inducible hsp 70 and the polyclonal antibody to hsp 70 exhibited different degrees of binding in control and shocked samples. October and January fish were subjected to osmotic shock in vivo by transfer from freshwater to 27 ppt and 35 ppt seawater. Five stress proteins with molecular weights of 39, 40, 41, 54, and 82 kDal were induced in non-smelting fish in October upon transfer to 27 ppt for 48 hours. Fish reared under a constant daylight photoperiod did not exhibit induction of hsps when transferred to 27 ppt seawater in January. Text Atlantic salmon Salmo salar University of Rhode Island: DigitalCommons@URI
institution Open Polar
collection University of Rhode Island: DigitalCommons@URI
op_collection_id ftunivrhodeislan
language unknown
description Lamellae isolated from gill arches of Atlantic salmon were incubated in 15, 25 and 21°c. Five heat shock or stress proteins (hsps) with molecular weights of 54, 71, 72, 82 and 87 kDal appeared after incubation at 25° c. At 21°c all five proteins were induced in greater quantity and an additional protein of 67 kDal was observed. The time 0 required for the induction of hsps at 25° c was determined by labeling the gills in vitro for one hour after intervals of up to four hours of heat shock. All five proteins were apparent after one hour of heat shock and maximal by two hours. The lamallae continued to synthesize hsps throughout the four hours. Stress proteins were not induced in lamallae exposed to 25 to 300 uM of sodium arsenite or 50 to 500 mM sodium chloride. Although viability was high under these conditions, overall protein synthesis was suppressed. Lamellae proteins induced by heat shock at 25°c were incubated with monoclonal and polyclonal antibodies to hsps 60, 70 and 90. Only the antibodies to constitutive/inducible hsp 70 and the polyclonal antibody to hsp 70 exhibited different degrees of binding in control and shocked samples. October and January fish were subjected to osmotic shock in vivo by transfer from freshwater to 27 ppt and 35 ppt seawater. Five stress proteins with molecular weights of 39, 40, 41, 54, and 82 kDal were induced in non-smelting fish in October upon transfer to 27 ppt for 48 hours. Fish reared under a constant daylight photoperiod did not exhibit induction of hsps when transferred to 27 ppt seawater in January.
format Text
author Allen, Jennifer L.
spellingShingle Allen, Jennifer L.
Heat Shock Proteins in Branchial Tissue in Atlantic Salmon (Salmo salar)
author_facet Allen, Jennifer L.
author_sort Allen, Jennifer L.
title Heat Shock Proteins in Branchial Tissue in Atlantic Salmon (Salmo salar)
title_short Heat Shock Proteins in Branchial Tissue in Atlantic Salmon (Salmo salar)
title_full Heat Shock Proteins in Branchial Tissue in Atlantic Salmon (Salmo salar)
title_fullStr Heat Shock Proteins in Branchial Tissue in Atlantic Salmon (Salmo salar)
title_full_unstemmed Heat Shock Proteins in Branchial Tissue in Atlantic Salmon (Salmo salar)
title_sort heat shock proteins in branchial tissue in atlantic salmon (salmo salar)
publisher DigitalCommons@URI
publishDate 1993
url https://digitalcommons.uri.edu/theses/1095
https://doi.org/10.23860/thesis-allen-jennifer-1993
https://digitalcommons.uri.edu/context/theses/article/2103/viewcontent/thesis_allen_jennifer_1993.pdf
genre Atlantic salmon
Salmo salar
genre_facet Atlantic salmon
Salmo salar
op_source Open Access Master's Theses
op_relation https://digitalcommons.uri.edu/theses/1095
doi:10.23860/thesis-allen-jennifer-1993
https://digitalcommons.uri.edu/context/theses/article/2103/viewcontent/thesis_allen_jennifer_1993.pdf
op_doi https://doi.org/10.23860/thesis-allen-jennifer-1993
_version_ 1772813215038701568