Splice isoforms of ubiquitous 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase in human brain.
In human brain we were able to demonstrate sequence diversity of the ubiquitous 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2). Six different isoforms of PFK-2/FBPase-2, two of which are identical with the ubiquitous PFK-2/FBPase-2 and the inducible PFK-2, respectively, could be identified. The heterogeneity of human brain PFK-2/FBPase-2 isoforms is generated by alternative splicing. Three hitherto unrecognized exons were detected. The multiple PFK-2/FBPase-2 transcripts encode proteins which differ with respect to their length and to the amino acid composition of the carboxyl-termini. The isoform pattern of ubiquitous PFK-2/FBPase-2 is more complex in human brain than in skeletal muscle and liver.
Institute of Biochemistry, School of Medicine, University of Leipzig, Liebigstrasse 16, Leipzig, 04103, Germany.
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Eschrich
D017398:Alternative Splicing; D000818:Animals; D001483:Base Sequence; D001921:Brain / Q000201:enzymology*; D001923:Brain Chemistry / Q000235:genetics; D005091:Exons / Q000235:genetics; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D007438:Introns / Q000235:genetics; D008969:Molecular Sequence Data; D025481:Phosphofructokinase-2; D010744:Phosphoric Monoester Hydrolases / Q000235:genetics*; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000235:genetics*; D051381:Rats
D017853:Phosphotransferases (Alcohol Group Acceptor); D025481:Phosphofructokinase-2; D010744:Phosphoric Monoester Hydrolases