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Serum Amyloid A Truncations in Type 2 Diabetes Mellitus
Serum Amyloid A (SAA) is an acute phase protein complex consisting of several abundant isoforms. The N- terminus of SAA is critical to its function in amyloid formation. SAA is frequently truncated, either missing an arginine or an arginine-serine dipeptide, resulting in isoforms that may influence...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4301920/ https://www.ncbi.nlm.nih.gov/pubmed/25607823 http://dx.doi.org/10.1371/journal.pone.0115320 |
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author | Yassine, Hussein N. Trenchevska, Olgica He, Huijuan Borges, Chad R. Nedelkov, Dobrin Mack, Wendy Kono, Naoko Koska, Juraj Reaven, Peter D. Nelson, Randall W. |
author_facet | Yassine, Hussein N. Trenchevska, Olgica He, Huijuan Borges, Chad R. Nedelkov, Dobrin Mack, Wendy Kono, Naoko Koska, Juraj Reaven, Peter D. Nelson, Randall W. |
author_sort | Yassine, Hussein N. |
collection | PubMed |
description | Serum Amyloid A (SAA) is an acute phase protein complex consisting of several abundant isoforms. The N- terminus of SAA is critical to its function in amyloid formation. SAA is frequently truncated, either missing an arginine or an arginine-serine dipeptide, resulting in isoforms that may influence the capacity to form amyloid. However, the relative abundance of truncated SAA in diabetes and chronic kidney disease is not known. METHODS: Using mass spectrometric immunoassay, the abundance of SAA truncations relative to the native variants was examined in plasma of 91 participants with type 2 diabetes and chronic kidney disease and 69 participants without diabetes. RESULTS: The ratio of SAA 1.1 (missing N-terminal arginine) to native SAA 1.1 was lower in diabetics compared to non-diabetics (p = 0.004), and in males compared to females (p<0.001). This ratio was negatively correlated with glycated hemoglobin (r = −0.32, p<0.001) and triglyceride concentrations (r = −0.37, p<0.001), and positively correlated with HDL cholesterol concentrations (r = 0.32, p<0.001). CONCLUSION: The relative abundance of the N-terminal arginine truncation of SAA1.1 is significantly decreased in diabetes and negatively correlates with measures of glycemic and lipid control. |
format | Online Article Text |
id | pubmed-4301920 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-43019202015-01-30 Serum Amyloid A Truncations in Type 2 Diabetes Mellitus Yassine, Hussein N. Trenchevska, Olgica He, Huijuan Borges, Chad R. Nedelkov, Dobrin Mack, Wendy Kono, Naoko Koska, Juraj Reaven, Peter D. Nelson, Randall W. PLoS One Research Article Serum Amyloid A (SAA) is an acute phase protein complex consisting of several abundant isoforms. The N- terminus of SAA is critical to its function in amyloid formation. SAA is frequently truncated, either missing an arginine or an arginine-serine dipeptide, resulting in isoforms that may influence the capacity to form amyloid. However, the relative abundance of truncated SAA in diabetes and chronic kidney disease is not known. METHODS: Using mass spectrometric immunoassay, the abundance of SAA truncations relative to the native variants was examined in plasma of 91 participants with type 2 diabetes and chronic kidney disease and 69 participants without diabetes. RESULTS: The ratio of SAA 1.1 (missing N-terminal arginine) to native SAA 1.1 was lower in diabetics compared to non-diabetics (p = 0.004), and in males compared to females (p<0.001). This ratio was negatively correlated with glycated hemoglobin (r = −0.32, p<0.001) and triglyceride concentrations (r = −0.37, p<0.001), and positively correlated with HDL cholesterol concentrations (r = 0.32, p<0.001). CONCLUSION: The relative abundance of the N-terminal arginine truncation of SAA1.1 is significantly decreased in diabetes and negatively correlates with measures of glycemic and lipid control. Public Library of Science 2015-01-21 /pmc/articles/PMC4301920/ /pubmed/25607823 http://dx.doi.org/10.1371/journal.pone.0115320 Text en https://creativecommons.org/publicdomain/zero/1.0/ This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. |
spellingShingle | Research Article Yassine, Hussein N. Trenchevska, Olgica He, Huijuan Borges, Chad R. Nedelkov, Dobrin Mack, Wendy Kono, Naoko Koska, Juraj Reaven, Peter D. Nelson, Randall W. Serum Amyloid A Truncations in Type 2 Diabetes Mellitus |
title | Serum Amyloid A Truncations in Type 2 Diabetes Mellitus |
title_full | Serum Amyloid A Truncations in Type 2 Diabetes Mellitus |
title_fullStr | Serum Amyloid A Truncations in Type 2 Diabetes Mellitus |
title_full_unstemmed | Serum Amyloid A Truncations in Type 2 Diabetes Mellitus |
title_short | Serum Amyloid A Truncations in Type 2 Diabetes Mellitus |
title_sort | serum amyloid a truncations in type 2 diabetes mellitus |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4301920/ https://www.ncbi.nlm.nih.gov/pubmed/25607823 http://dx.doi.org/10.1371/journal.pone.0115320 |
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