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1.
Mol Cell Endocrinol ; 518: 110989, 2020 12 01.
Article in English | MEDLINE | ID: mdl-32835784

ABSTRACT

The growth hormone (Gh)/insulin-like growth-factor (Igf)/Igf binding protein (Igfbp) system regulates growth and osmoregulation in salmonid fishes, but how this system interacts with other endocrine systems is largely unknown. Given the well-documented consequences of mounting a glucocorticoid stress response on growth, we hypothesized that cortisol inhibits anabolic processes by modulating the expression of hepatic igfbp mRNAs. Atlantic salmon (Salmo salar) parr were implanted intraperitoneally with cortisol implants (0, 10, and 40 µg g-1 body weight) and sampled after 3 or 14 days. Cortisol elicited a dose-dependent reduction in specific growth rate (SGR) after 14 days. While plasma Gh and Igf1 levels were unchanged, hepatic igf1 mRNA was diminished and hepatic igfbp1b1 and -1b2 were stimulated by the high cortisol dose. Plasma Igf1 was positively correlated with SGR at 14 days. Hepatic gh receptor (ghr), igfbp1a, -2a, -2b1, and -2b2 levels were not impacted by cortisol. Muscle igf2, but not igf1 or ghr, levels were stimulated at 3 days by the high cortisol dose. As both cortisol and the Gh/Igf axis promote seawater (SW) tolerance, and particular igfbps respond to SW exposure, we also assessed whether cortisol coordinates the expression of branchial igfbps and genes associated with ion transport. Cortisol stimulated branchial igfbp5b2 levels in parallel with Na+/K+-ATPase (NKA) activity and nka-α1b, Na+/K+/2Cl--cotransporter 1 (nkcc1), and cystic fibrosis transmembrane regulator 1 (cftr1) mRNA levels. The collective results indicate that cortisol modulates the growth of juvenile salmon via the regulation of hepatic igfbp1s whereas no clear links between cortisol and branchial igfbps previously shown to be salinity-responsive could be established.


Subject(s)
Hydrocortisone/administration & dosage , Insulin-Like Growth Factor Binding Protein 1/genetics , Insulin-Like Growth Factor Binding Protein 2/genetics , Insulin-Like Growth Factor Binding Protein 5/genetics , Liver/metabolism , Salmo salar/growth & development , Animals , Dose-Response Relationship, Drug , Drug Implants/chemistry , Gene Expression Regulation, Developmental/drug effects , Growth Hormone/blood , Hydrocortisone/pharmacology , Injections, Intraperitoneal , Insulin-Like Growth Factor I/genetics , Insulin-Like Growth Factor I/metabolism , Liver/growth & development , Salmo salar/genetics , Seawater/chemistry
2.
J Fish Biol ; 85(4): 1279-96, 2014 Oct.
Article in English | MEDLINE | ID: mdl-25159100

ABSTRACT

Specific growth hormone (GH)-binding protein (Ghbp) was purified from Atlantic salmon Salmo salar and rainbow trout Oncorhynchus mykiss plasma with immunoprecipitation and characterized in cross-linking studies using autoradiography and western blots. The size of the Ghbp was estimated to be c. 53 kDa. A radioimmunoassay was established to measure Ghbp in salmonids, using antibodies specific against the extracellular segment of the S. salar growth hormone receptor 1 (grh1; GenBank AY462105). Plasma Ghbp levels were measured in S. salar smolts in fresh water and after transfer to seawater (SW; experiments 1 and 2), and in post-smolts kept at different salinities (0, 12, 22 and 34) for 3 months (experiment 3). A transient increase in plasma Ghbp, which lasted for 1 month or less, was noted in smolts after transfer to SW. Concomitantly, plasma GH and gill Na(+) -K(+) -ATPase activity increased during smoltification (in experiment 2). No difference in plasma Ghbp was evident between post-smolts kept at different salinities, although the fish kept at salinity 34 had higher plasma GH than the group kept at salinity 22 and higher hepatic ghr1 expression than post-smolts kept at salinity 12. This suggests that plasma Ghbp regulation may respond to salinity changes in the short term. The lack of correlation between Ghbp, plasma GH and hepatic ghr1 expression in the long-term post-smolt experiment indicates that Ghbp levels may be regulated independently of other components of the endocrine GH system in salmonids.


Subject(s)
Carrier Proteins/blood , Salmo salar/blood , Acclimatization/physiology , Amino Acid Sequence , Animals , Base Sequence , Fish Proteins/blood , Gills/enzymology , Molecular Sequence Data , Radioimmunoassay , Recombinant Proteins/blood , Seawater , Sodium-Potassium-Exchanging ATPase/metabolism
3.
Comp Biochem Physiol C Toxicol Pharmacol ; 130(4): 447-59, 2001 Dec.
Article in English | MEDLINE | ID: mdl-11738632

ABSTRACT

The thyroid hormones (THs), thyroxine (T(4)) and triiodothyronine (T(3)) are products of the thyroid gland in all vertebrates. Their role in early development and metamorphosis is well established in mammals and amphibians, respectively, and recently several studies in fish have highlighted the importance of THs during flatfish metamorphosis. THs are present in high quantities in fish eggs and are presumably of maternal origin. During embryogenesis the concentration of T(4) and T(3) in the eggs decrease until endogenous production starts. Thyroid hormone receptors (TR) have been isolated from several teleosts and in common with tetrapods two receptor isoforms have been identified, TR alpha and TR beta. Both the receptors are expressed in early embryos and larvae of the Japanese flounder (Paralichthys olivaceus), zebrafish (Danio rerio) and seabream (Sparus aurata) although a different temporal pattern is apparent. The role of THs and TRs in fish embryogenesis, larval development and during metamorphosis will be discussed.


Subject(s)
Embryo, Nonmammalian/physiology , Fishes/growth & development , Thyroxine/physiology , Triiodothyronine/physiology , Amino Acid Sequence , Animals , Fishes/physiology , Larva/physiology , Metamorphosis, Biological/physiology , Molecular Sequence Data , Receptors, Thyroid Hormone/genetics , Receptors, Thyroid Hormone/physiology , Sequence Alignment , Thyroxine/metabolism , Triiodothyronine/metabolism
4.
Nat Genet ; 17(1): 84-7, 1997 Sep.
Article in English | MEDLINE | ID: mdl-9288103

ABSTRACT

Essential tremor (ET), the most common movement disorder in humans, appears to be inherited as an autosomal dominant trait in many families. The familial form is called familial essential tremor (FET), which seems similar to sporadic essential tremor. ET is a cause of substantial disability, particularly in the elderly. The prevalence of Parkinson's disease and dystonia may be increased in families with ET, but other movement disorders are seldom encountered in these families. Here we report the results of a genome-wide scan for FET genes in 16 Icelandic families with 75 affected individuals, in whom FET was apparently inherited as a dominant trait. The scan, which was performed with a 10-cM framework map, revealed one locus on chromosome 3q13 to which FET mapped with a genome-wide significance when the data were analysed either parametrically, assuming an autosomal dominant model (lod score = 3.71), or non-parametrically (NPL Z score = 4.70, p < 6.4 x 10(-6).


Subject(s)
Chromosomes, Human, Pair 3 , Tremor/genetics , Chromosome Mapping , Female , Genetic Linkage , Genetic Markers , Genome, Human , Genotype , Humans , Iceland , Lod Score , Male
5.
Fish Physiol Biochem ; 15(5): 395-400, 1996 Nov.
Article in English | MEDLINE | ID: mdl-24194299

ABSTRACT

The Atlantic salmon (Salmo salar) stress response was examined by measuring plasma cortisol, glucose and chloride in fish after water level reduction within rearing tanks. Maximum plasma cortisol levels (366±43 (SD) nM and 534±280 nM for Groups 1 and 2, respectively) were observed 20 min after application of the stressor. Cortisol levels were down to control levels 24 h later. The pattern for cortisol changes observed within these two groups were comparable. Plasma glucose and chloride concentrations did not change significantly in either of the experimental groups. The fish in group 2 were then repeatedly subjected to the same stressor every third day. After the fifth exposure to the stressor, blood was obtained from fish at times corresponding to sampling after the first exposure. Their maximum plasma cortisol level only reached 223 (±96) nM, and was down to prestress levels within 2 h. Plasma glucose and chloride concentrations did not change significantly in this second experiment. This challenge test revealed an acute primary response in Atlantic salmon without any apparent harmful secondary responses, that may thus serve as a standardized reference stressor using other fish groups under comparable conditions.

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