Mitochondrial proteomes of porcine kidney cortex and medulla: foundation for translational proteomics

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11140%2F16%3A10295556" target="_blank" >RIV/00216208:11140/16:10295556 - isvavai.cz</a>

Result on the web

<a href="http://link.springer.com/article/10.1007%2Fs10157-015-1135-x" target="_blank" >http://link.springer.com/article/10.1007%2Fs10157-015-1135-x</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s10157-015-1135-x" target="_blank" >10.1007/s10157-015-1135-x</a>

Result language

angličtina

Original language name

Mitochondrial proteomes of porcine kidney cortex and medulla: foundation for translational proteomics

Original language description

BACKGROUND: Emerging evidence has linked mitochondrial dysfunction to the pathogenesis of many renal disorders, including acute kidney injury, sepsis and even chronic kidney disease. Proteomics is a powerful tool in elucidating the role of mitochondria in renal pathologies. Since the pig is increasingly recognized as a major mammalian model for translational research, the lack of physiological proteome data of large mammals prompted us to examine renal mitochondrial proteome in porcine kidney cortex and medulla METHODS: Kidneys were obtained from six healthy pigs. Mitochondria from cortex and medulla were isolated using differential centrifugation and proteome maps of cortical and medullar mitochondria were constructed using two-dimensional gel electrophoresis (2DE). Protein spots with significant difference between mitochondrial fraction of renal cortex and medulla were identified by mass spectrometry. RESULTS: Proteomic analysis identified 81 protein spots. Of these spots, 41 mitochondrial proteins were statistically different between renal cortex and medulla (p < 0.05). Protein spots containing enzymes of beta oxidation, amino acid metabolism, and gluconeogenesis were predominant in kidney cortex mitochondria. Spots containing tricarboxylic acid cycle enzymes and electron transport system proteins, proteins maintaining metabolite transport and mitochondrial translation were more abundant in medullar mitochondria. CONCLUSION: This study provides the first proteomic profile of porcine kidney cortex and medullar mitochondrial proteome. Different protein expression pattern reflects divergent functional metabolic role of mitochondria in various kidney compartments. Our study could serve as a useful reference for further porcine experiments investigating renal mitochondrial physiology under various pathological states.

Czech name

—

Czech description

—

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EB - Genetics and molecular biology

OECD FORD branch

—

Project

<a href="/en/project/ED2.1.00%2F03.0076" target="_blank" >ED2.1.00/03.0076: Biomedical Centre of the Faculty of Medicine in Pilsen</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2016

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Clinical and Experimental Nephrology

ISSN

1342-1751

e-ISSN

—

Volume of the periodical

20

Issue of the periodical within the volume

1

Country of publishing house

JP - JAPAN

Number of pages

11

Pages from-to

39-49

UT code for WoS article

000370376200005

EID of the result in the Scopus database

2-s2.0-84958679207