µ-Crystallin: A thyroid hormone binding protein

µ-Crystallin is a NADPH-regulated thyroid hormone binding protein encoded by the CRYM gene in humans. It is primarily expressed in the brain, muscle, prostate, and kidney, where it binds thyroid hormones, which regulate metabolism and thermogenesis. It also acts as a ketimine reductase in the lysine...

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Autores principales:	Kinney Christian J., Bloch Robert J.
Formato:	article
Lenguaje:	EN
Publicado:	Sciendo 2021
Materias:	crym µ-crystallin mu-crystallin thyroid hormone t3 t4 ketimine reductase Diseases of the endocrine glands. Clinical endocrinology RC648-665
Acceso en línea:	https://doaj.org/article/b8829ecb12ae41ae8e7a6d0f3cf426db
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spelling	oai:doaj.org-article:b8829ecb12ae41ae8e7a6d0f3cf426db2021-12-02T16:41:14Zµ-Crystallin: A thyroid hormone binding protein1336-032910.2478/enr-2021-0011https://doaj.org/article/b8829ecb12ae41ae8e7a6d0f3cf426db2021-04-01T00:00:00Zhttps://doi.org/10.2478/enr-2021-0011https://doaj.org/toc/1336-0329µ-Crystallin is a NADPH-regulated thyroid hormone binding protein encoded by the CRYM gene in humans. It is primarily expressed in the brain, muscle, prostate, and kidney, where it binds thyroid hormones, which regulate metabolism and thermogenesis. It also acts as a ketimine reductase in the lysine degradation pathway when it is not bound to thyroid hormone. Mutations in CRYM can result in non-syndromic deafness, while its aberrant expression, predominantly in the brain but also in other tissues, has been associated with psychiatric, neuromuscular, and inflammatory diseases. CRYM expression is highly variable in human skeletal muscle, with 15% of individuals expressing ≥13 fold more CRYM mRNA than the median level. Ablation of the Crym gene in murine models results in the hypertrophy of fast twitch muscle fibers and an increase in fat mass of mice fed a high fat diet. Overexpression of Crym in mice causes a shift in energy utilization away from glycolysis towards an increase in the catabolism of fat via β-oxidation, with commensurate changes of metabolically involved transcripts and proteins. The history, attributes, functions, and diseases associated with CRYM, an important modulator of metabolism, are reviewed.Kinney Christian J.Bloch Robert J.Sciendoarticlecrymµ-crystallinmu-crystallinthyroid hormonet3t4ketimine reductaseDiseases of the endocrine glands. Clinical endocrinologyRC648-665ENEndocrine Regulations, Vol 55, Iss 2, Pp 89-102 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	crym µ-crystallin mu-crystallin thyroid hormone t3 t4 ketimine reductase Diseases of the endocrine glands. Clinical endocrinology RC648-665
spellingShingle	crym µ-crystallin mu-crystallin thyroid hormone t3 t4 ketimine reductase Diseases of the endocrine glands. Clinical endocrinology RC648-665 Kinney Christian J. Bloch Robert J. µ-Crystallin: A thyroid hormone binding protein
description	µ-Crystallin is a NADPH-regulated thyroid hormone binding protein encoded by the CRYM gene in humans. It is primarily expressed in the brain, muscle, prostate, and kidney, where it binds thyroid hormones, which regulate metabolism and thermogenesis. It also acts as a ketimine reductase in the lysine degradation pathway when it is not bound to thyroid hormone. Mutations in CRYM can result in non-syndromic deafness, while its aberrant expression, predominantly in the brain but also in other tissues, has been associated with psychiatric, neuromuscular, and inflammatory diseases. CRYM expression is highly variable in human skeletal muscle, with 15% of individuals expressing ≥13 fold more CRYM mRNA than the median level. Ablation of the Crym gene in murine models results in the hypertrophy of fast twitch muscle fibers and an increase in fat mass of mice fed a high fat diet. Overexpression of Crym in mice causes a shift in energy utilization away from glycolysis towards an increase in the catabolism of fat via β-oxidation, with commensurate changes of metabolically involved transcripts and proteins. The history, attributes, functions, and diseases associated with CRYM, an important modulator of metabolism, are reviewed.
format	article
author	Kinney Christian J. Bloch Robert J.
author_facet	Kinney Christian J. Bloch Robert J.
author_sort	Kinney Christian J.
title	µ-Crystallin: A thyroid hormone binding protein
title_short	µ-Crystallin: A thyroid hormone binding protein
title_full	µ-Crystallin: A thyroid hormone binding protein
title_fullStr	µ-Crystallin: A thyroid hormone binding protein
title_full_unstemmed	µ-Crystallin: A thyroid hormone binding protein
title_sort	µ-crystallin: a thyroid hormone binding protein
publisher	Sciendo
publishDate	2021
url	https://doaj.org/article/b8829ecb12ae41ae8e7a6d0f3cf426db
work_keys_str_mv	AT kinneychristianj μcrystallinathyroidhormonebindingprotein AT blochrobertj μcrystallinathyroidhormonebindingprotein
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µ-Crystallin: A thyroid hormone binding protein

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