On the ontogeny and interactions of glyceraldehyde-3-phosphate dehydrogenase.
The interaction of GAPDH with cellular structure has been studied in the major tissues of the mouse during development. Overall the data provides a clear indication that interactions between GAPDH and cellular structure are appreciable in all major tissues, at least during early stages of development, and an analysis of the isozyme status of the enzyme in both soluble and bound compartments for all tissues at all developmental stages indicates the presence of only a single GAPDH isozyme in the mouse. Possible reasons for the lack of an extensive multiplicity of this enzyme in mammalian tissues (the only tetrameric glycolytic enzyme to display this restriction) and for the large amounts of GAPDH in many cell types are discussed in relation to the large number of proteins that GAPDH interacts with in the cell.
D000818:Animals; D001921:Brain / Q000201:enzymology / Q000254:growth & development; D003599:Cytoskeleton / Q000032:analysis*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000096:biosynthesis* / Q000502:physiology; D006019:Glycolysis; D007527:Isoenzymes / Q000096:biosynthesis* / Q000502:physiology; D007668:Kidney / Q000201:enzymology / Q000254:growth & development; D051379:Mice / Q000254:growth & development* / Q000378:metabolism; D024510:Muscle Development; D009132:Muscles / Q000201:enzymology
D007527:Isoenzymes; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases