In the brain, all three isoenzyme types [muscle (M), liver (L), and br
ain (C)] of 6-phosphofructo-1-kinase (PFK; EC 2.7.1.11) occur, forming
a complex mixture of home- and heterotetramers. The PFK isoenzyme pat
tern of the different brain cell types is yet unknown. In the present
study, we investigated the distribution of the PFK isoenzyme subunits
in primary and secondary cell cultures and in bulk-isolated cells of r
at brain by means of sodium dodecyl sulfate-polyacrylamide gel electro
phoresis and western blotting. All three PFK isoenzymes are present in
all cell types but in different proportions. The cellular distributio
n of the PFK isoenzymes in situ was studied immunohistochemically with
different polyclonal antisera against purified rat PFKs. The monospec
ific antibody against M-type PFK stained preferentially the perinuclea
r areas of neurons and glial cells. The antibodies that in immunoblots
detected mainly the L-type PFK showed a characteristic staining in on
ly the cytoplasma and the processes of cells, whereas the C-type antib
odies almost homogeneously stained whole cell bodies as well as large
dendrites. Because the PFK isoenzymes differ with respect to their all
osteric properties, their differential distribution in different brain
cells might be of importance for the regulation of brain glycolysis i
n the different cellular compartments of the brain.