Structural characterization and chromosomal localization of the mouse cDNA and gene encoding the bone tyrosine phosphatase, mOST-PTP

Daniel F. Morrison, Laura J. Mauro

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


Tyrosine kinases and phosphatases are regulators of the steady-state levels of phosphotyrosine proteins and, in this way, are key players in determining the functional state of the cell. As a unique member of the protein tyrosine phosphatase (PTP) superfamily, osteotesticular PTP (OST-PTP) is a receptor protein whose expression is highly regulated during osteoblast differentiation and in response to modulators of bone remodeling such as parathyroid hormone and vitamin D3. To explore the molecular mechanisms and signaling pathways important in the regulation of this gene, we characterized the structural organization of the mouse OST-PTP cDNA and gene and determined its chromosomal localization. The mouse cDNA is ~5.5 kb including 5.1 kb of coding sequence, 315 bp 5' UTR and 102 bp 3' UTR. It is expressed as a single ~5.8 kb transcript in day 8 differentiated MC3T3 osteoblasts. Although highly homologous to the rat OST-PTP cDNA, the mouse cDNA possesses a 74 bp insert in the 5' UTR which contains several potential transcription factor binding sites such as AP-2 and NFκB. The mouse OST-PTP (mOST-PTP) gene is a single copy gene encompassing 35 exons and spanning only 20.65 kb. As such, it is the smallest gene of the characterized receptor PTP genes. This is due to the lack of large introns and the conserved spatial organization of exons which encode specific protein motifs in the mOST-PTP molecule. Sequence analysis of the putative mOST-PTP promoter revealed basal elements as well as many potential cis-acting regulatory elements with relevance to gene regulation in bone. Of particular interest is the single osteoblast specific element known as osteocalcin specific element 2 (OSE2) found at position -1867, as well as numerous VDRE and NFκB sites found throughout the promoter and the 5' UTR. Fluorescence in situ hybridization studies have shown that mOST-PTP localizes to mouse chromosome 1, region F-G which is syntenic to the segment of human chromosome 1q32-33. This characterization of the mOST-PTP cDNA and gene will facilitate future experiments exploring the mechanisms of regulation of this phosphatase during osteogenesis. (C) 2000 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)195-208
Number of pages14
Issue number2
StatePublished - Oct 31 2000

Bibliographical note

Funding Information:
We would like to thank Dr. David Largaespada (Minnesota Cancer Center) and his laboratory for assistance with Southern analysis; Dr. Renny Franceschi (Michigan School of Dentistry) for MC3T3 cells; Ms. Emily Kishel, Ms. Karen T. Umali, Mr. Daniel C. Tranter, Ms. Melanie Townsend and Dr. Nambirajan Sundaram for helpful discussions and technical support; and Drs. David R. Brown, James Mickelson and Howard Towle for critical review of the manuscript. This work was supported in part by National Institutes of Health Grants R55 and R29 (NIAMS/AR-44226) and the Minnesota Medical Foundation.


  • Adhesion molecule
  • Differentiation
  • Genomic organization
  • Germ cells
  • Osteoblast
  • Receptor tyrosine phosphatase

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