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Liver and muscle hemojuvelin are differently glycosylated

BACKGROUND: Hemojuvelin (HJV) is one of essential components for expression of hepcidin, a hormone which regulates iron transport. HJV is mainly expressed in muscle and liver, and processing of HJV in both tissues is similar. However, hepcidin is expressed in liver but not in muscle and the role of...

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Autores principales: Fujikura, Yuzo, Krijt, Jan, Nečas, Emanuel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3190341/
https://www.ncbi.nlm.nih.gov/pubmed/21936923
http://dx.doi.org/10.1186/1471-2091-12-52
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author Fujikura, Yuzo
Krijt, Jan
Nečas, Emanuel
author_facet Fujikura, Yuzo
Krijt, Jan
Nečas, Emanuel
author_sort Fujikura, Yuzo
collection PubMed
description BACKGROUND: Hemojuvelin (HJV) is one of essential components for expression of hepcidin, a hormone which regulates iron transport. HJV is mainly expressed in muscle and liver, and processing of HJV in both tissues is similar. However, hepcidin is expressed in liver but not in muscle and the role of the muscle HJV is yet to be established. Our preliminary analyses of mouse tissue HJV showed that the apparent molecular masses of HJV peptides are different in liver (50 kDa monomer and 35 and 20 kDa heterodimer fragments) and in muscle (55 kDa monomer and a 34 kDa possible large fragment of heterodimer). One possible explanation is glycosylation which could lead to difference in molecular mass. RESULTS: We investigated glycosylation of HJV in both liver and muscle tissue from mice. PNGase F treatment revealed that the HJV large fragments of liver and muscle were digested to peptides with similar masses, 30 and 31 kDa, respectively, and the liver 20 kDa small fragment of heterodimer was digested to 16 kDa, while the 50 kDa liver and 55 kDa muscle monomers were reduced to 42 and 48 kDa, respectively. Endo H treatment produced distinct digestion profiles of the large fragment: a small fraction of the 35 kDa peptide was reduced to 33 kDa in liver, while the majority of the 34 kDa peptide was digested to 33 kDa and a very small fraction to 31 kDa in muscle. In addition, liver HJV was found to be neuraminidase-sensitive but its muscle counterpart was neuraminidase-resistant. CONCLUSIONS: Our results indicate that different oligosaccharides are attached to liver and muscle HJV peptides, which may contribute to different functions of HJV in the two tissues.
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spelling pubmed-31903412011-10-12 Liver and muscle hemojuvelin are differently glycosylated Fujikura, Yuzo Krijt, Jan Nečas, Emanuel BMC Biochem Research Article BACKGROUND: Hemojuvelin (HJV) is one of essential components for expression of hepcidin, a hormone which regulates iron transport. HJV is mainly expressed in muscle and liver, and processing of HJV in both tissues is similar. However, hepcidin is expressed in liver but not in muscle and the role of the muscle HJV is yet to be established. Our preliminary analyses of mouse tissue HJV showed that the apparent molecular masses of HJV peptides are different in liver (50 kDa monomer and 35 and 20 kDa heterodimer fragments) and in muscle (55 kDa monomer and a 34 kDa possible large fragment of heterodimer). One possible explanation is glycosylation which could lead to difference in molecular mass. RESULTS: We investigated glycosylation of HJV in both liver and muscle tissue from mice. PNGase F treatment revealed that the HJV large fragments of liver and muscle were digested to peptides with similar masses, 30 and 31 kDa, respectively, and the liver 20 kDa small fragment of heterodimer was digested to 16 kDa, while the 50 kDa liver and 55 kDa muscle monomers were reduced to 42 and 48 kDa, respectively. Endo H treatment produced distinct digestion profiles of the large fragment: a small fraction of the 35 kDa peptide was reduced to 33 kDa in liver, while the majority of the 34 kDa peptide was digested to 33 kDa and a very small fraction to 31 kDa in muscle. In addition, liver HJV was found to be neuraminidase-sensitive but its muscle counterpart was neuraminidase-resistant. CONCLUSIONS: Our results indicate that different oligosaccharides are attached to liver and muscle HJV peptides, which may contribute to different functions of HJV in the two tissues. BioMed Central 2011-09-21 /pmc/articles/PMC3190341/ /pubmed/21936923 http://dx.doi.org/10.1186/1471-2091-12-52 Text en Copyright ©2011 Fujikura et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Fujikura, Yuzo
Krijt, Jan
Nečas, Emanuel
Liver and muscle hemojuvelin are differently glycosylated
title Liver and muscle hemojuvelin are differently glycosylated
title_full Liver and muscle hemojuvelin are differently glycosylated
title_fullStr Liver and muscle hemojuvelin are differently glycosylated
title_full_unstemmed Liver and muscle hemojuvelin are differently glycosylated
title_short Liver and muscle hemojuvelin are differently glycosylated
title_sort liver and muscle hemojuvelin are differently glycosylated
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3190341/
https://www.ncbi.nlm.nih.gov/pubmed/21936923
http://dx.doi.org/10.1186/1471-2091-12-52
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