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XXII. BIOCHEMICKÝ ZJAZD - Jesseniova lekárska fakulta

XXII. BIOCHEMICKÝ ZJAZD - Jesseniova lekárska fakulta

XXII. BIOCHEMICKÝ ZJAZD - Jesseniova lekárska fakulta

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Posters<br />

29.<br />

THE ROLE OF 14-3-3 PROTEIN IN REGULATION OF GLUCOSE<br />

TraNSPORTER GLUT4 TraNSLOCATION TO ADIPOCYTE PLASMA<br />

MEMBraNE<br />

Lucia Gajdošechová, Miroslava Eckertová, Katarína Kršková and Štefan Zorad<br />

Institute of Experimental Endocrinology, SAS, Bratislava, Slovakia<br />

Basic mechanism of insulin action is translocation of GLUT4 transport vesicles (GTV) from<br />

inner cell compartments to plasma membrane. Defect of this mechanism leads to development<br />

of insulin resistance and diabetes. Beta isoform of 14-3-3 protein binds to Thrphosphorylated<br />

AS160, the substrate of insulin-activated Akt protein kinase, thereby reducing<br />

of AS160 GTP-ase activity and subsequently activating GTV translocation in adipose tissue.<br />

The main purpose of the present study was to evaluate GLUT4 and GLUT1 transporters<br />

protein content in epididymal adipose tissue plasma membranes of young obese Zucker<br />

rats and correlate it with the amount of 14-3-3 protein in fat tisssue total homogenate.<br />

Zucker rats represent a model of obesity and insulin resistance with mild hyperglycemia.<br />

Based on unchanged GLUT1 and elevated GLUT4 content in plasma membrane fraction<br />

of obese animals we assume normal insulin sensitivity with regard to glucose transporter<br />

translocation in adipose tissue of 3-month-old obese Zucker rats. Augmented GLUT4<br />

translocation seems to be due to an enormous increase in 14-3-3 protein which might play<br />

a crucial role in glucose transporter activation. Surprisingly, the serum concentration of<br />

adiponectin was significantly elevated in obese animals despite of decreased mRNA level<br />

in white adipose tissue. The elucidation of 14-3-3 protein regulation, e.g. by adiponectin,<br />

await for further investigation.<br />

Ackowledgement: This work was supported by grant VEGA 2/0162/08.<br />

<strong>XXII</strong>. Biochemistry Congress, Martin<br />

147

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