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The structure, biosynthesis, and biological roles of fetuin-A: A review

Fetuin-A is a heterodimeric plasma glycoprotein containing an A-chain of 282 amino acids and a B-chain of 27 amino acid residues linked by a single inter-disulfide bond. It is predominantly expressed in embryonic cells and adult hepatocytes, and to a lesser extent in adipocytes and monocytes. Fetuin...

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Autores principales: Chekol Abebe, Endeshaw, Tilahun Muche, Zelalem, Behaile T/Mariam, Awigchew, Mengie Ayele, Teklie, Mekonnen Agidew, Melaku, Teshome Azezew, Muluken, Abebe Zewde, Edgeit, Asmamaw Dejenie, Tadesse, Asmamaw Mengstie, Misganaw
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9340150/
https://www.ncbi.nlm.nih.gov/pubmed/35923855
http://dx.doi.org/10.3389/fcell.2022.945287
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author Chekol Abebe, Endeshaw
Tilahun Muche, Zelalem
Behaile T/Mariam, Awigchew
Mengie Ayele, Teklie
Mekonnen Agidew, Melaku
Teshome Azezew, Muluken
Abebe Zewde, Edgeit
Asmamaw Dejenie, Tadesse
Asmamaw Mengstie, Misganaw
author_facet Chekol Abebe, Endeshaw
Tilahun Muche, Zelalem
Behaile T/Mariam, Awigchew
Mengie Ayele, Teklie
Mekonnen Agidew, Melaku
Teshome Azezew, Muluken
Abebe Zewde, Edgeit
Asmamaw Dejenie, Tadesse
Asmamaw Mengstie, Misganaw
author_sort Chekol Abebe, Endeshaw
collection PubMed
description Fetuin-A is a heterodimeric plasma glycoprotein containing an A-chain of 282 amino acids and a B-chain of 27 amino acid residues linked by a single inter-disulfide bond. It is predominantly expressed in embryonic cells and adult hepatocytes, and to a lesser extent in adipocytes and monocytes. Fetuin-A binds with a plethora of receptors and exhibits multifaceted physiological and pathological functions. It is involved in the regulation of calcium metabolism, osteogenesis, and the insulin signaling pathway. It also acts as an ectopic calcification inhibitor, protease inhibitor, inflammatory mediator, anti-inflammatory partner, atherogenic factor, and adipogenic factor, among other several moonlighting functions. Fetuin-A has also been demonstrated to play a crucial role in the pathogenesis of several disorders. This review mainly focuses on the structure, synthesis, and biological roles of fetuin-A. Information was gathered manually from various journals via electronic searches using PubMed, Google Scholar, HINARI, and Cochrane Library from inception to 2022. Studies written in English and cohort, case-control, cross-sectional, or experimental studies were considered in the review, otherwise excluded.
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spelling pubmed-93401502022-08-02 The structure, biosynthesis, and biological roles of fetuin-A: A review Chekol Abebe, Endeshaw Tilahun Muche, Zelalem Behaile T/Mariam, Awigchew Mengie Ayele, Teklie Mekonnen Agidew, Melaku Teshome Azezew, Muluken Abebe Zewde, Edgeit Asmamaw Dejenie, Tadesse Asmamaw Mengstie, Misganaw Front Cell Dev Biol Cell and Developmental Biology Fetuin-A is a heterodimeric plasma glycoprotein containing an A-chain of 282 amino acids and a B-chain of 27 amino acid residues linked by a single inter-disulfide bond. It is predominantly expressed in embryonic cells and adult hepatocytes, and to a lesser extent in adipocytes and monocytes. Fetuin-A binds with a plethora of receptors and exhibits multifaceted physiological and pathological functions. It is involved in the regulation of calcium metabolism, osteogenesis, and the insulin signaling pathway. It also acts as an ectopic calcification inhibitor, protease inhibitor, inflammatory mediator, anti-inflammatory partner, atherogenic factor, and adipogenic factor, among other several moonlighting functions. Fetuin-A has also been demonstrated to play a crucial role in the pathogenesis of several disorders. This review mainly focuses on the structure, synthesis, and biological roles of fetuin-A. Information was gathered manually from various journals via electronic searches using PubMed, Google Scholar, HINARI, and Cochrane Library from inception to 2022. Studies written in English and cohort, case-control, cross-sectional, or experimental studies were considered in the review, otherwise excluded. Frontiers Media S.A. 2022-07-18 /pmc/articles/PMC9340150/ /pubmed/35923855 http://dx.doi.org/10.3389/fcell.2022.945287 Text en Copyright © 2022 Chekol Abebe, Tilahun Muche, Behaile T/Mariam, Mengie Ayele, Mekonnen Agidew, Teshome Azezew, Abebe Zewde, Asmamaw Dejenie and Asmamaw Mengstie. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Cell and Developmental Biology
Chekol Abebe, Endeshaw
Tilahun Muche, Zelalem
Behaile T/Mariam, Awigchew
Mengie Ayele, Teklie
Mekonnen Agidew, Melaku
Teshome Azezew, Muluken
Abebe Zewde, Edgeit
Asmamaw Dejenie, Tadesse
Asmamaw Mengstie, Misganaw
The structure, biosynthesis, and biological roles of fetuin-A: A review
title The structure, biosynthesis, and biological roles of fetuin-A: A review
title_full The structure, biosynthesis, and biological roles of fetuin-A: A review
title_fullStr The structure, biosynthesis, and biological roles of fetuin-A: A review
title_full_unstemmed The structure, biosynthesis, and biological roles of fetuin-A: A review
title_short The structure, biosynthesis, and biological roles of fetuin-A: A review
title_sort structure, biosynthesis, and biological roles of fetuin-a: a review
topic Cell and Developmental Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9340150/
https://www.ncbi.nlm.nih.gov/pubmed/35923855
http://dx.doi.org/10.3389/fcell.2022.945287
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