PMID- 9211863
OWN - NLM
STAT- MEDLINE
DCOM- 19970814
LR  - 20220409
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 272
IP  - 28
DP  - 1997 Jul 11
TI  - Phosphorylation and activation of heart 6-phosphofructo-2-kinase by protein 
      kinase B and other protein kinases of the insulin signaling cascades.
PG  - 17269-75
AB  - To understand the insulin-induced activation of 6-phosphofructo-2-kinase (PFK-2) 
      of the bifunctional enzyme PFK-2/fructose-2,6-bisphosphatase in heart, the effect 
      of phosphorylation by protein kinases of the insulin signaling pathways on PFK-2 
      activity was studied. Purified PFK-2/fructose-2, 6-bisphosphatase from bovine 
      heart is a mixture of two isoforms (Mr 58,000 and 54,000 on SDS-polyacrylamide 
      gels). The Mr 54,000 protein is an alternatively spliced form, lacking 
      phosphorylation sites for protein kinases. Recombinant enzymes corresponding to 
      the Mr 58,000 (BH1) and Mr 54,000 (BH3) forms were expressed and used as 
      substrates for phosphorylation. The recombinant BH1 isoform was phosphorylated by 
      p70 ribosomal S6 kinase (p70(s6k)), mitogen-activated protein kinase-activated 
      protein kinase-1, and protein kinase B (PKB), whereas the recombinant BH3 isoform 
      was a poor substrate for these protein kinases. Treatment with all protein 
      kinases activated PFK-2 in the recombinant BH1 preparation. Phosphorylation of 
      the recombinant BH1 isoform correlated with PFK-2 activation and was reversed by 
      treatment with protein phosphatase 2A. All the protein kinases phosphorylated 
      Ser-466 and Ser-483 in the BH1 isoform, but to different extents: p70(s6k) 
      preferentially phosphorylated Ser-466, whereas mitogen-activated protein 
      kinase-activated protein kinase-1 and PKB phosphorylated Ser-466 and Ser-483 to a 
      similar extent. We propose that PKB is part of the insulin signaling cascade for 
      PFK-2 activation in heart.
FAU - Deprez, J
AU  - Deprez J
AD  - Hormone and Metabolic Research Unit, Institute of Cellular and Molecular 
      Pathology and the Louvain University Medical School, Avenue Hippocrate, 75, 1200 
      Brussels, Belgium.
FAU - Vertommen, D
AU  - Vertommen D
FAU - Alessi, D R
AU  - Alessi DR
FAU - Hue, L
AU  - Hue L
FAU - Rider, M H
AU  - Rider MH
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Insulin)
RN  - 0 (Isoenzymes)
RN  - 0 (Proto-Oncogene Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - EC 2.7.- (Protein Kinases)
RN  - EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor))
RN  - EC 2.7.1.105 (Phosphofructokinase-2)
RN  - EC 2.7.11.1 (Protein Serine-Threonine Kinases)
RN  - EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
RN  - EC 2.7.11.1 (Ribosomal Protein S6 Kinases)
RN  - EC 2.7.11.1 (Ribosomal Protein S6 Kinases, 90-kDa)
RN  - EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases)
SB  - IM
MH  - Adenosine Triphosphate/metabolism
MH  - Animals
MH  - Cattle
MH  - Chromatography, High Pressure Liquid
MH  - Cyclic AMP-Dependent Protein Kinases/metabolism
MH  - Enzyme Activation
MH  - Insulin/*physiology
MH  - Isoenzymes/isolation & purification/metabolism
MH  - Kinetics
MH  - Molecular Weight
MH  - Myocardium/*enzymology
MH  - Phosphofructokinase-2
MH  - Phosphorylation
MH  - Phosphotransferases (Alcohol Group Acceptor)/*metabolism
MH  - Protein Kinases/*metabolism
MH  - Protein Serine-Threonine Kinases/metabolism
MH  - Proto-Oncogene Proteins/metabolism
MH  - Proto-Oncogene Proteins c-akt
MH  - Recombinant Proteins/isolation & purification/metabolism
MH  - Ribosomal Protein S6 Kinases
MH  - Ribosomal Protein S6 Kinases, 90-kDa
MH  - *Signal Transduction
EDAT- 1997/07/11 00:00
MHDA- 1997/07/11 00:01
CRDT- 1997/07/11 00:00
PHST- 1997/07/11 00:00 [pubmed]
PHST- 1997/07/11 00:01 [medline]
PHST- 1997/07/11 00:00 [entrez]
AID - S0021-9258(18)39191-9 [pii]
AID - 10.1074/jbc.272.28.17269 [doi]
PST - ppublish
SO  - J Biol Chem. 1997 Jul 11;272(28):17269-75. doi: 10.1074/jbc.272.28.17269.