Ah. Koeppen et al., THE HETEROGENEOUS DISTRIBUTION OF BRAIN TRANSFERRIN, Journal of neuropathology and experimental neurology, 54(3), 1995, pp. 395-403
Immunocytochemistry with antisera to transferrin has often been used t
o identify oligodendroglia in tissue sections and cultures, but reacti
on product also occurs in blood vessel walls and nerve cells. There is
considerable species variation. Serum transferrin is largely biosynth
esized in the liver, and its established physiological role is the tra
nsport of iron to tissue sites and delivery of the metal to the interi
or of cells that have transferrin receptors on their surfaces. In sect
ions of the central nervous system, the visualization of iron and tran
sferrin generally does not coincide, and transferrin may have importan
ce to normal brain function beyond iron transport. For a comparative a
nalysis of transferrin in rabbit and rat brain, polyclonal antisera we
re raised against purified serum transferrins of these species. The an
tisera were used for transferrin immunocytochemistry on vibratome sect
ions and for immunochemical detection on electroblots. Transferrin imm
unocytochemistry and iron histochemistry were compared. The electropho
retic separation of brain extracts and transfer to nitrocellulose memb
ranes permitted the quantitation of the protein and the study of the c
arbohydrate chains of tissue-bound transferrins by biotinylated lectin
s. An unexpected result in the rabbit was the dense immunocytochemical
reaction product in Bergmann glia and Golgi epithelial cells. Reactio
n in the cytoplasm of oligodendrocytes was relatively faint in this sp
ecies except for some selected white matter tracts, e.g. the inferior
cerebellar peduncles. In sections of rat brain, oligodendrocytes and v
essel wails reacted vigorously in ail locations. Transferrin levels in
rat brain were substantially higher than in rabbit brain. In the rabb
it, maximum transferrin levels occurred in the cerebellum. The combina
tion of lectin affinity chemistry and digestion with neuraminidase rev
ealed the presence of sialylated, mannose-containing, and fucosylated
intracellular brain transferrin in both species. These observations ma
y also be relevant to the recently described neurological syndrome tha
t is associated with carbohydrate deficiency of serum and cerebrospina
l fluid transferrin.