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Blood, Vol. 94 No. 7 (October 1), 1999:
pp. 2403-2413
PTPROt: An Alternatively Spliced and Developmentally Regulated
B-Lymphoid Phosphatase That Promotes G0/G1 Arrest
Ricardo C.T. Aguiar,
Yoshihiro Yakushijin,
Samir Kharbanda,
Sanjay Tiwari,
Gordon J. Freeman, and
Margaret A. Shipp
From the Department of Adult Oncology, Dana-Farber Cancer Institute,
Harvard Medical School, Boston, MA.
Protein tyrosine phosphatases (PTP) regulate the
proliferation, differentiation, and viability of lymphocytes by
modulating their signaling pathways. By using the differential display
assay, we have cloned a putative receptor-type PTP, which is
predominantly expressed in B-lymphoid tissues (lymph nodes and spleen).
This PTP, termed PTPROt (truncated), is a tissue-specific
alternatively-spliced form of a human epithelial PTP, PTPRO
(PTPU2/GLEPP1). Whereas the epithelial PTPRO includes an  800-amino
acid extracellular domain, the major (3 kb) PTPROt cDNA predicts a
unique 5' untranslated region and truncated (8 amino acids)
extracellular domain with a conserved transmembrane region and single
catalytic domain. PTPROt cDNAs encode functional ~47-kD and ~43-kD
PTPs, which are most abundant in normal naive quiescent B cells and
decreased or absent in germinal center B cells and germinal
center-derived diffuse large B-cell lymphomas. Because PTPROt was
predominantly expressed in naive quiescent B cells, the enzyme's
effects on cell-cycle progression were examined. When multiple stable
PTPROt sense, antisense, and vector only B-cell transfectants were
grown in reduced serum and synchronized with nocodazole, PTPROt sense clones exhibited markedly increased G0/G1 arrest. Taken together, these
data implicate PTPROt in the growth control of specific B-cell subpopulations.
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