| First Author | Pixley FJ | Year | 1995 |
| Journal | J Biol Chem | Volume | 270 |
| Issue | 45 | Pages | 27339-47 |
| PubMed ID | 7592997 | Mgi Jnum | J:42332 |
| Mgi Id | MGI:1095611 | Doi | 10.1074/jbc.270.45.27339 |
| Citation | Pixley FJ, et al. (1995) A heteromorphic protein-tyrosine phosphatase, PTP phi, is regulated by CSF-1 in macrophages. J Biol Chem 270(45):27339-47 |
| abstractText | A novel protein-tyrosine phosphatase, PTP phi, was cloned from a murine macrophage cDNA library. As a result of alternative splicing, macrophage PTP phi mRNAs are predicted to encode two membrane-spanning molecules and a cytosolic enzyme with identical catalytic domains. The membrane-spanning forms differ in the juxtamembrane region, while a start codon downstream of this region is utilized in the translation of the putative cytosolic form. Expression of PTP phi mRNA is low and restricted to macrophage cell lines, macrophage-rich tissues, and brain, kidney, and heart. The mRNA in macrophages and heart is approximately 2.8 kilobases (kb). However, a approximately 5.5-kb transcript in brain and kidney indicates a fourth isoform encoding a large extracellular domain. The approximately 5.5-kb PTP phi brain mRNA encodes the mouse homolog of GLEPP1, a recently reported glomerular epithelial protein. The level of expression of the mRNA encoding the cytosolic form was very low, and only the membrane-spanning proteins (43 and 47 kDa) could be detected in macrophages. Following addition of colony stimulating factor-1 to quiescent BAC1.2F5 macrophages, PTP phi mRNA and protein were down-regulated. The restricted expression of the shorter isoforms of PTP phi and their regulation by colony stimulating factor-1 in macrophages suggest that PTP phi may play a role in mononuclear phagocyte survival, proliferation, and/or differentiation. |
