Abstract
Cytoskeleton controls the stability of transcripts, by mechanisms that involve mRNAs and eEF1A attachment to it. Besides, it plays a key role in protein synthesis and secretion, which seems to be impaired in somatotrophs of hypothyroid rats, whose cytoskeleton is disarranged. This study investigated the: eEF1A and GH mRNA binding to cytoskeleton plus GH mRNA translation rate and GH secretion, in sham-operated and thyroidectomized rats treated with T3 or saline, and killed 30min thereafter. Thyroidectomy reduced: (a) pituitary F-actin content, and eEF1A plus GH mRNA binding to it; (b) GH mRNA recruitment to polysome; and (c) liver IGF-I mRNA expression, indicating that GH mRNA stability and translation rate, as well as GH secretion were impaired. T3 acutely reversed all these changes, which points toward a nongenomic action of T3 on cytoskeleton rearrangement, which might contribute to the increase on GH mRNA translation rate and GH secretion.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actins / metabolism
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Animals
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Body Weight / drug effects
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Cytoskeleton / drug effects
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Cytoskeleton / metabolism
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Gene Expression Regulation / drug effects
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Growth Hormone / genetics*
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Growth Hormone / metabolism*
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Hypothyroidism / genetics*
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Hypothyroidism / pathology
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Insulin-Like Growth Factor I / genetics
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Insulin-Like Growth Factor I / metabolism
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Liver / drug effects
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Liver / metabolism
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Liver / pathology
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Male
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Organ Size / drug effects
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Peptide Elongation Factor 1 / metabolism
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Pituitary Gland / drug effects
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Pituitary Gland / metabolism
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Pituitary Gland / pathology
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Polyribosomes / drug effects
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Polyribosomes / metabolism
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Protein Binding / drug effects
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Protein Biosynthesis / drug effects*
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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Rats
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Rats, Wistar
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Triiodothyronine / pharmacology*
Substances
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Actins
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Peptide Elongation Factor 1
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RNA, Messenger
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Triiodothyronine
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Insulin-Like Growth Factor I
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Growth Hormone