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Molecular cloning, characterization, and chromosomal localization of a
novel protein-tyrosine phosphatase, HPTP eta
H Honda, J Inazawa, J Nishida, Y Yazaki and H Hirai
Department of Molecular Biology, Jichi Medical School, Tochigi-ken, Japan.
Protein-tyrosine phosphatases (PTPases) are considered to play an important
role in signal transduction. We previously identified partial sequences of
three novel PTPases in a human leukemic cell line. F-36P. We describe here
cloning, characterization, and chromosomal localization of one of the newly
identified PTPases, termed as HPTP eta (human protein-tyrosine phosphatase
eta). The deduced amino acid sequence was composed of an extracellular
region homologous to fibronectin type III repeats, a transmembrane region,
and a cytoplasmic region containing a single PTPase-like domain. Based on
its primary structure, this clone belongs to type-III receptor-type
PTPases. The PTPase-like domain showed PTPase activity when expressed in
Escherichia coli. Antibody against the extracellular region detected a
protein of 220 to 250 kD in human hematopoietic cell lines expressing HPTP
eta mRNA. The antibody also recognized a protein of approximately the same
molecular weight in COS cells transfected with HPTP eta cDNA, indicating
that the antibody specifically recognized HPTP eta gene product and that
the cloned cDNA contained full-length coding region. The chromosomal
localization determined by fluorescence in situ hybridization showed that
the HPTP eta gene was located at chromosome 11p11.2 on the short arm of
chromosome 11, which is frequently lost or deleted in human carcinomas.
Volume 84,
Issue 12,
pp. 4186-4194,
12/15/1994
Copyright © 1994 by The American Society of Hematology
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