Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density

Ostman, A., Yang, Q., Tonks, N. K. (October 1994) Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density. Proceedings of the National Academy of Sciences of the United States of America, 91 (21). pp. 9680-9684. ISSN 0027-8424

URL: http://www.ncbi.nlm.nih.gov/pubmed/7937872
DOI: 10.1073/pnas.91.21.9680

Abstract

cDNA encoding a receptor-like protein-tyrosine-phosphatase (PTP) termed DEP-1 was isolated from a HeLa cell library. The cDNA predicts an enzyme consisting of an extracellular segment containing eight fibronectin type III repeats, a single transmembrane segment, and a single intracellular PTP domain. Following expression of DEP-1 cDNA in COS cells a glycoprotein of 180 kDa was detected and PTP activity was demonstrated in immunocomplexes with a C-terminal peptide antiserum. Endogenous DEP-1 was detected in WI-38 human embryonic lung fibroblasts by immunoblotting and immunocomplex PTP assays. Immunoblot analysis of DEP-1 expression in WI-38 cells revealed dramatically increased levels and activity of the PTP in dense cultures relative to sparse cultures. Also, DEP-1 activity, detected in PTP assays of immunocomplexes, was increased is dense cell cultures. In contrast, the expression levels of PTP-1B did not change with cell density. This enhancement of DEP-1 expression with increasing cell density was also observed in another fibroblast cell line, AG1518. The increase in DEP-1 occurs gradually with increasing cell contact and is initiated before saturation cell density is reached. These observations suggest that DEP-1 may contribute to the mechanism of contact inhibition of cell growth.

Item Type: Paper
Uncontrolled Keywords: CONTACT-DEPENDENT INHIBITION NERVOUS-SYSTEM AXONS DROSOPHILA-MELANOGASTER GROWTH GENE PHOSPHOTYROSINE CLONING DOMAIN PHOSPHORYLATION TRANSFORMATION
Subjects: organism description > animal > insect > Drosophila
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein receptor
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein tyrosine phosphatase
CSHL Authors:
Communities: CSHL labs > Tonks lab
Depositing User: Matt Covey
Date: October 1994
Date Deposited: 18 Dec 2013 15:25
Last Modified: 18 Dec 2013 15:25
PMCID: PMC44880
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29066

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