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Updated: Aug 10, 2026

Skeletal Phenotype Analysis of a Conditional Stat3 Deletion Mouse Model
Published on: July 3, 2020
Identification of a hormonally regulated protein tyrosine phosphatase associated with bone and testicular
L J Mauro1, E A Olmsted, B M Skrobacz
1Department of Biological Chemistry, University of Michigan, Ann Arbor 48109.
Abstract:
Absence of the tyrosine kinase activity of c-src and c-fms results in impairment of bone remodeling. Such dysfunction underscores the importance of tyrosine phosphorylation, yet the role of protein tyrosine phosphatases in bone metabolism remains unexamined. We have isolated the cDNA for a novel receptor-like tyrosine phosphatase expressed in bone and testis named osteotesticular protein tyrosine phosphatase (OST-PTP). The deduced 1711-residue protein possesses an extracellular domain with 10 fibronectin type III repeats and a cytoplasmic region with two catalytic domains. In primary rat osteoblasts, the 5.8-kilobase OST-PTP transcript is up-regulated in differentiating cultures and down-regulated in late stage mineralizing cultures. In addition, a presumed alternate transcript of 4.8-5.0 kilobases, which may lack PTP domains, is present in proliferating osteoblasts, but not detectable at other stages. Parathyroid hormone, a modulator of bone function, as well as cyclic AMP analogues, increase OST-PTP mRNA 5-8-fold in UMR 106 cells. In situ hybridization of adult rat testis revealed stage-specific expression of OST-PTP. OST-PTP may function in signaling pathways during bone remodeling, as well as serve a broader role in cell interactions associated with differentiation in bone and testis.
Insights
Researchers identified a novel protein tyrosine phosphatase, OST-PTP, crucial for bone remodeling. Its expression in osteoblasts and response to hormones suggest a key role in bone metabolism and cell differentiation.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Tyrosine kinase activity of c-src and c-fms is vital for bone remodeling.
- The role of protein tyrosine phosphatases (PTPs) in bone metabolism is largely unexamined.
- PTPs are critical regulators of cellular signaling pathways.
Purpose of the Study:
- To identify and characterize novel PTPs involved in bone metabolism.
- To investigate the expression pattern and regulation of a newly discovered PTP in bone cells.
- To explore the potential function of this PTP in bone remodeling and differentiation.
Main Methods:
- Isolation and characterization of the cDNA for a novel receptor-like tyrosine phosphatase, OST-PTP.
- Analysis of OST-PTP mRNA expression in primary rat osteoblasts during differentiation and mineralization.
- Investigation of OST-PTP regulation by parathyroid hormone and cyclic AMP analogues in UMR 106 cells.
- In situ hybridization to determine OST-PTP expression in adult rat testis.
Main Results:
- A novel receptor-like tyrosine phosphatase, OST-PTP, was isolated and characterized.
- OST-PTP mRNA is upregulated during osteoblast differentiation and downregulated during late-stage mineralization.
- A shorter OST-PTP transcript variant, potentially lacking PTP domains, is present in proliferating osteoblasts.
- Parathyroid hormone and cyclic AMP analogues significantly increase OST-PTP mRNA levels in UMR 106 cells.
- Stage-specific expression of OST-PTP was observed in the adult rat testis.
Conclusions:
- OST-PTP is a novel PTP expressed in bone and testis with a potential role in bone remodeling.
- OST-PTP expression is dynamically regulated during osteoblast differentiation and mineralization.
- OST-PTP may be involved in signaling pathways regulating bone cell function and differentiation.
- OST-PTP may also play a role in cell interactions during differentiation in both bone and testis.
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