A model for understanding gene regulation during spermatogenesis: the mouse testis Pdha-2 promoter

1995 ◽  
Vol 7 (4) ◽  
pp. 705 ◽  
Author(s):  
RC Iannello ◽  
J Young ◽  
S Sumarsono ◽  
M Tymms ◽  
I Kola
Keyword(s):  
Gene Regulation ◽  
Pyruvate Dehydrogenase ◽  
Current Knowledge ◽  
Pyruvate Dehydrogenase Complex ◽  
Mouse Testis ◽  
Alpha Subunit ◽  
Livestock Industry ◽  
Coordinate Expression ◽  
Complex Process ◽  
Dehydrogenase Complex

Spermatogenesis is a complex process requiring the coordinate expression of a number of testis-specific genes. How these genes are regulated during spermatogenesis is poorly understood. However, the elucidation of these mechanisms has significant implications for both medicine and the primary livestock industry. The delineation of this process is of particular interest and, in this study, Pdha-2, a gene which codes for the murine testis-specific isoform of the E1 alpha subunit of the pyruvate dehydrogenase complex, has been used as a model. This review focuses on current knowledge about its expression and regulation during spermatogenesis.

scholarly journals Studies on the incorporation of [32P]phosphate into pyruvate dehydrogenase in intact rat fat-cells. Effects of insulin

1980 ◽  
Vol 192 (2) ◽  
pp. 469-481 ◽  
Author(s):  
W A Hughes ◽  
R W Brownsey ◽  
R M Denton
Keyword(s):  
Pyruvate Dehydrogenase ◽  
Pyruvate Dehydrogenase Complex ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Subcellular Fractionation ◽  
Alpha Subunit ◽  
Fat Cells ◽  
Phosphorylated Proteins ◽  
Alpha Subunits ◽  
Dehydrogenase Complex

1. Intact rat epididymal fat-cells were incubated with 32Pi, and the intracellular proteins were separated by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. One of the separated bands of phosphorylated proteins had an apparent subunit mol.wt. of 42 000, which is the same as that of the alpha-subunit of the pyruvate dehydrogenase complex. By using a combination of subcellular fractionation, immunoprecipitation with antiserum raised against pyruvate dehydrogenase complex and two-dimensional electrophoresis it was apparent that the incorporation into alpha-subunits accounted for 35–45% of the total incorporation into this band of phosphoproteins. 2. The increase in the initial activity of pyruvate dehydrogenase that follows brief exposure of fat-cells to insulin was shown to be associated with a decrease in the steady-state incorporation of 32P into the alpha-subunits of pyruvate dehydrogenase. 3. Tryptic peptide analysis of pyruvate dehydrogenase [32P]phosphate, labelled in intact fat-cells, indicated that three serine residues on the alpha-subunit were phosphorylated, corresponding to the three sites phosphorylated when purified pig heart pyruvate dehydrogenase was incubated with [gamma-32P]ATP. The relative phosphorylation of all three serine residues appeared to be similar in 32P-labelled alpha-subunits in both control and insulin-treated fat-cells.

The Pyruvate Dehydrogenase Complex as a Target for Gene Therapy

2003 ◽  
Vol 3 (3) ◽  
pp. 239-245 ◽  
Author(s):  
Peter Stacpoole ◽  
Renius Owen ◽  
Terence Flotte
Keyword(s):  
Gene Therapy ◽  
Pyruvate Dehydrogenase ◽  
Pyruvate Dehydrogenase Complex ◽  
Dehydrogenase Complex
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