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α(2)-µ-Globulin fragment (a2-f) from kidneys of male rats

The structure of α(2)-µ-Globulin fragment (A2-f) is not known.α(2)-µ-Globulin fragment (A2-f) is a 15.5 kDa protein that binds equimolar amount of fatty acids in male rat kidneys. The expression of this protein has been shown to change in response to druginduced and genetic hypertension which sugges...

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Detalles Bibliográficos
Autores principales: Hai, Abdul, Kizilbash, Nadeem A
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3569602/
https://www.ncbi.nlm.nih.gov/pubmed/23422892
http://dx.doi.org/10.6026/97320630009145
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author Hai, Abdul
Kizilbash, Nadeem A
author_facet Hai, Abdul
Kizilbash, Nadeem A
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description The structure of α(2)-µ-Globulin fragment (A2-f) is not known.α(2)-µ-Globulin fragment (A2-f) is a 15.5 kDa protein that binds equimolar amount of fatty acids in male rat kidneys. The expression of this protein has been shown to change in response to druginduced and genetic hypertension which suggests that it plays an important role in renal fatty acid metabolism under pathological conditions as well as normal conditions. A2-f has sequence homology with amino acid 28-178 of α(2)-µ-Globulin (A2U) that is synthesized pre-dominantly in the male rat liver and is present in the urine. It is believed that unusual structural features permit A2-f to be targeted to the proximal tubule cell; to escape lysosomal degradation in liver and to enter the cytosol of proximal tubule cells of the kidneys. Homology modeling has been employed to determine the structural elements of this protein and they have been compared with the published structure of A2U. Results suggest differences between the structure of A2-f and its precursor protein A2U.
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spelling pubmed-35696022013-02-19 α(2)-µ-Globulin fragment (a2-f) from kidneys of male rats Hai, Abdul Kizilbash, Nadeem A Bioinformation Hypothesis The structure of α(2)-µ-Globulin fragment (A2-f) is not known.α(2)-µ-Globulin fragment (A2-f) is a 15.5 kDa protein that binds equimolar amount of fatty acids in male rat kidneys. The expression of this protein has been shown to change in response to druginduced and genetic hypertension which suggests that it plays an important role in renal fatty acid metabolism under pathological conditions as well as normal conditions. A2-f has sequence homology with amino acid 28-178 of α(2)-µ-Globulin (A2U) that is synthesized pre-dominantly in the male rat liver and is present in the urine. It is believed that unusual structural features permit A2-f to be targeted to the proximal tubule cell; to escape lysosomal degradation in liver and to enter the cytosol of proximal tubule cells of the kidneys. Homology modeling has been employed to determine the structural elements of this protein and they have been compared with the published structure of A2U. Results suggest differences between the structure of A2-f and its precursor protein A2U. Biomedical Informatics 2013-02-06 /pmc/articles/PMC3569602/ /pubmed/23422892 http://dx.doi.org/10.6026/97320630009145 Text en © 2013 Biomedical Informatics This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
spellingShingle Hypothesis
Hai, Abdul
Kizilbash, Nadeem A
α(2)-µ-Globulin fragment (a2-f) from kidneys of male rats
title α(2)-µ-Globulin fragment (a2-f) from kidneys of male rats
title_full α(2)-µ-Globulin fragment (a2-f) from kidneys of male rats
title_fullStr α(2)-µ-Globulin fragment (a2-f) from kidneys of male rats
title_full_unstemmed α(2)-µ-Globulin fragment (a2-f) from kidneys of male rats
title_short α(2)-µ-Globulin fragment (a2-f) from kidneys of male rats
title_sort α(2)-µ-globulin fragment (a2-f) from kidneys of male rats
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3569602/
https://www.ncbi.nlm.nih.gov/pubmed/23422892
http://dx.doi.org/10.6026/97320630009145
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