Ks. Fang et al., CHARACTERIZATION OF CHICKEN PROTEIN-TYROSINE-PHOSPHATASE-ALPHA AND ITS EXPRESSION IN THE CENTRAL-NERVOUS-SYSTEM, Molecular brain research, 37(1-2), 1996, pp. 1-14
Protein tyrosine phosphorylation and dephosphorylation are important i
n cell proliferation, differentiation and functioning of the central n
ervous system. We have identified a cDNA clone encoding a new transmem
brane protein tyrosine phosphatase from a chicken brain cDNA library.
The predicted amino acid sequence contains two phosphatase tandem repe
ats in the intracellular domain and multiple glycosylation sites in th
e extracellular domain. Since its intracellular domain shares 94% iden
tity with human PTP alpha, we call it chicken PTP alpha (ChPTP alpha).
Antibodies specific to ChPTP alpha recognize two major protein bands
at 130 and 85 kDa in immunoblot and immunoprecipitation. ChPTP alpha t
ranscript and protein are found in many tissues, but they are particul
arly abundant in brain. To gain insight into the function of PTP alpha
s, we investigated the cell-type specific localization of ChPTP alpha
in cerebellum by in situ hybridization and immunostaining. Throughout
development, the level of ChPTP alpha remains similar from embryonic
day 7 to post-hatching day 14, but the abundance and distribution of c
ells expressing this protein vary systematically through this period.
During development, ChPTP alpha appears in pre-migratory and migrating
granule cells, and in Bergmann glia and their radial processes. By 2-
weeks after hatching, ChPTP alpha disappears from all cells of the cer
ebellum except Bergmann glia. Our data, which show for the first time
the temporal and spacial distribution of a PTP alpha, suggest that the
se transmembrane phosphatases are important in the differentiation and
function of Bergmann glia and in the migration of granule cells, and
thereby play a role in development of the cerebellum.