ArticleMolecular biology of the cell2004
Tyrosine phosphatase epsilon is a positive regulator of osteoclast function in vitro and in vivo.
Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
25 citing papers in PubMed, 84 citations in OpenAlex.
- A Multifunctional Therapeutic Strategy Using P7C3 as A Countermeasure Against Bone Loss and Fragility in An Ovariectomized Rat Model of Postmenopausal Osteoporosis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Osteoclast Methods in Protein Phosphatase Research.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Protein tyrosine phosphatases in skeletal development and diseases.Bone research · 2022Review
- Discovery of exercise-related genes and pathway analysis based on comparative genomes of Mongolian originated Abaga and Wushen horse.Open life sciences · 2022Article
- Tuning the Protein Phosphorylation by Receptor Type Protein Tyrosine Phosphatase Epsilon (PTPRE) in Normal and Cancer Cells.Journal of Cancer · 2019Review
- Differential oxidation of protein-tyrosine phosphatases during zebrafish caudal fin regeneration.Scientific reports · 2017Article
- Retinoid X receptors orchestrate osteoclast differentiation and postnatal bone remodeling.The Journal of clinical investigation · 2015Article
- Evidence that homozygous PTPRD gene microdeletion causes trigonocephaly, hearing loss, and intellectual disability.Molecular cytogenetics · 2015Article
- Bone remodeling markers and bone metastases: From cancer research to clinical implications.BoneKEy reports · 2015Review
- Adaptor protein GRB2 promotes Src tyrosine kinase activation and podosomal organization by protein-tyrosine phosphatase ϵ in osteoclasts.The Journal of biological chemistry · 2014Article
- Protein tyrosine phosphatases ε and α perform nonredundant roles in osteoclasts.Molecular biology of the cell · 2014Article
- TULA-2, a novel histidine phosphatase, regulates bone remodeling by modulating osteoclast function.Cellular and molecular life sciences : CMLS · 2013Article
- Genome-Wide Association Identifies TBX5 as Candidate Gene for Osteochondrosis Providing a Functional Link to Cartilage Perfusion as Initial Factor.Frontiers in genetics · 2013Article
- Epidermal growth factor receptor (EGFR)-mediated positive feedback of protein-tyrosine phosphatase epsilon (PTPepsilon) on ERK1/2 and AKT protein pathways is required for survival of human breast cancer cells.The Journal of biological chemistry · 2012Article
- Identification and expression of the family of classical protein-tyrosine phosphatases in zebrafish.PloS one · 2010Article
- Protein tyrosine phosphatase epsilon regulates integrin-mediated podosome stability in osteoclasts by activating Src.Molecular biology of the cell · 2009Article
- Activation of Src kinase by protein-tyrosine phosphatase-PEST in osteoclasts: comparative analysis of the effects of bisphosphonate and protein-tyrosine phosphatase inhibitor on Src activation in vitro.Journal of cellular physiology · 2009Article
- Targeted transgenic expression of an osteoclastic transmembrane protein-tyrosine phosphatase in cells of osteoclastic lineage increases bone resorption and bone loss in male young adult mice.The Journal of biological chemistry · 2009Article
- PTPepsilon has a critical role in signaling transduction pathways and phosphoprotein network topology in red cells.Proteomics · 2008Article
- Podosomes and Invadopodia: Related structures with Common Protein Components that May Promote Breast Cancer Cellular Invasion.Breast cancer : basic and clinical research · 2008Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Protein tyrosine phosphorylation is a major regulator of bone metabolism. Tyrosine phosphatases participate in regulating phosphorylation, but roles of specific phosphatases in bone metabolism are largely unknown. We demonstrate that young (<12 weeks) female mice lacking tyrosine phosphatase epsilon (PTPepsilon) exhibit increased trabecular bone mass due to cell-specific defects in osteoclast function. These defects are manifested in vivo as reduced association of osteoclasts with bone and as reduced serum concentration of C-terminal collagen telopeptides, specific products of osteoclast-mediated bone degradation. Osteoclast-like cells are generated readily from PTPepsilon-deficient bone-marrow precursors. However, cultures of these cells contain few mature, polarized cells and perform poorly in bone resorption assays in vitro. Podosomes, structures by which osteoclasts adhere to matrix, are disorganized and tend to form large clusters in these cells, suggesting that lack of PTPepsilon adversely affects podosomal arrangement in the final stages of osteoclast polarization. The gender and age specificities of the bone phenotype suggest that it is modulated by hormonal status, despite normal serum levels of estrogen and progesterone in affected mice. Stimulation of bone resorption by RANKL and, surprisingly, Src activity and Pyk2 phosphorylation are normal in PTPepsilon-deficient osteoclasts, indicating that loss of PTPepsilon does not cause widespread disruption of these signaling pathways. These results establish PTPepsilon as a phosphatase required for optimal structure, subcellular organization, and function of osteoclasts in vivo and in vitro.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.