Title

Authors

Affiliation

Department of Biochemistry, Faculty of Medicine, Northern Border University, Arar-91431, Saudi Arabia

Email

nadeem_kizilbash@yahoo.com; *Corresponding author

Article Type

Hypothesis

Date

Received January 09, 2013; Accepted January 11, 2013; Published February 06, 2013

The structure of a2-m-Globulin fragment (A2-f) is not known.a2-m-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 drug-induced 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 a2-m-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.

Keywords

a2-m-Globulin fragment, Kidney fatty acid binding protein, Chemically-induced nephropathy.

Citation

Hai & Kizilbash,   Bioinformation 9(3): 145-149 (2013)

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.