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ARS Home » Plains Area » Houston, Texas » Children's Nutrition Research Center » Research » Publications at this Location » Publication #166274
Title: PROTEIN KINASE B (PKB) ACTIVATION DECREASES WITH DEVELOPMENT IN SKELETAL MUSCLE OF NEONATAL PIGS

Author
item SURYAWAN, AGUS - BAYLOR COLL OF MEDICINE
item NGUYEN, HANH - BAYLOR COLL OF MEDICINE
item ORELLANA, RENAN - BAYLOR COLL OF MEDICINE
item LIU, CHUN - BAYLOR COLL OF MEDICINE
item Davis, Teresa

Submitted to: Federation of American Societies for Experimental Biology Conference
Publication Type: Abstract Only
Publication Acceptance Date: 3/24/2004
Publication Date: 4/17/2004
Citation: Suryawan, A., Nguyen, H.V., Orellana, R.A., Liu, C.W., Davis. T.A. 2004. Protein kinase B (PKB) activation decreases with development in skeletal muscle of neonatal pigs [abstract]. Federation of American Societies for Experimental Biology Conference. 18(5):A896.

Interpretive Summary: Not needed for an Abstract

Technical Abstract: Postprandial activation of the insulin signaling pathway that leads to translation initiation is enhanced in skeletal muscle of the neonate and decreases with development in parallel with the developmental decline in muscle protein synthesis. Our previous study showed that the activity of PKB, a major insulin signaling component, was higher in 7- than in 26-d-old pigs. To examine possible molecular mechanisms, we determined PKB isoform abundance and phosphorylation state, the abundance of its kinases, and its association with its kinases. The abundances of total PKB, PKBalpha and PKBgamma were higher in muscle of 7- than 26-d-old pigs while PKBbeta abundance was similar. PKB phosphorylation at Thr308 was higher in 7- than 26-d-old pigs and phosphorylation at Ser473 was similar in both age groups. The association of PKB with 3'-phosphoinositide-dependent kinase-1 (PDK-1), a kinase that phosphorylates Thr308, and PDK-1 abundance were higher in 7- than 26-d-old pigs. However, the association of PKB with integrin-linked kinase (ILK), a kinase that potentially phosphorylates Ser473, and ILK abundance were similar in both age groups. Overall, the results suggest that the marked elevation in the abundances of PKBalpha and PDK-1 and the association of PKB.PDK-1 are likely responsible for the enhanced PKB activation in skeletal muscle of neonatal pigs.