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PTPRD rs35929428 might play a role in hepatic lipid accumulation and fibrosis, followed by the development of NAFLD.
Results show the existence of a perturbed PTPRD-STAT3 (show STAT3 Proteins) axis potentially driving malignant progression of Hepatitis C virus-associated liver disease.
Presynaptic differentiation induced by protein tyrosine phosphatase receptor type D (PTPdelta)-leucine rich repeat and fibronectin type III domain containing 5 (SALM5 (show LRFN5 Proteins)) requires the dimeric property of SALM5 (show LRFN5 Proteins).
In the 2:2 heterotetrameric SALM5 (show LRFN5 Proteins)/PTPdelta complex, a SALM5 (show LRFN5 Proteins) dimer bridges two separate PTPdelta molecules.
our study suggested that PTPRD loci are candidate susceptibility regions that have some marker SNPs for GDM in Han Chinese
We investigated the modification of air pollution and diabetes association by a genetic risk score covering 63 T2D genes. Five single variants near GRB14 (show GRB14 Proteins), UBE2E2 (show UBE2E2 Proteins), PTPRD, VPS26A (show VPS26A Proteins) and KCNQ1 (show KCNQ1 Proteins) showed nominally significant interactions with PM10 (P<0.05). Our results suggest that genetic risk for T2D may modify susceptibility to air pollution through alterations in insulin (show INS Proteins) sensitivity
Mutation in PTPRD gene is associated with nodal marginal zone lymphoma.
Low PTPRD expression is associated with Head and Neck Squamous Cell Carcinoma.
The data provide evidence of the high incidence of PTPRD inactivation in laryngeal squamous cell carcinoma, suggesting that deletions and loss-of-function mutations are responsible for PTPRD loss only in a fraction of cases, whereas DNA methylation (show HELLS Proteins) is the dominating mechanism of PTPRD inactivation.
PTPRD polymorphisms might modulate antipsychotic-induced weight gain.
Chondroitin Sulfate Proteoglycans Negatively Modulate Spinal Cord Neural Precursor Cells by Signaling Through LAR (show PTPRF Proteins) and RPTPsigma (show PTPRS Proteins) and Modulation of the Rho/ROCK Pathway.
Ptprd is a tumor suppressor that can promote tumorigenesis in concert with Cdkn2a loss.
We reveal that PTPRD is a bona fide tumor suppressor, pinpoint PTPRD loss as a cause of aberrant STAT3 activation in gliomas, and establish PTPRD loss, in the setting of CDKN2A/p16(INK4A) deletion, as a driver of glioma progression.
RPTP-sigma (show PTPRS Proteins) and RPTP-delta complement each other functionally during mammalian development, and reveal an essential contribution of RPTP-sigma (show PTPRS Proteins) and RPTP-delta to appropriate motoneuron axon targeting during mammalian axonogenesis.
Receptor protein tyrosine phosphatase (show PTPRT Proteins)-delta cooperates with hedgehog (show SHH Proteins)-responsive gene MIM (show MTSS1 Proteins) to induce cytoskeletal remodeling.
PTPRD may be one of a select group of tumor suppressor genes that are inactivated in a wide range of common tumor types.
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an extracellular region, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. The extracellular region of this protein is composed of three Ig-like and eight fibronectin type III-like domains. Studies of the similar genes in chicken and fly suggest the role of this PTP is in promoting neurite growth, and regulating neurons axon guidance. Multiple alternatively spliced transcript variants of this gene have been reported. A related pseudogene has been identified on chromosome 5.
, protein tyrosine phosphatase, receptor type, delta polypeptide
, protein-tyrosine phosphatase delta
, receptor-type tyrosine-protein phosphatase delta
, protein tyrosine phosphatase, receptor type, D
, protein-tyrosine phosphatase delta-b
, protein tyrosine phosphatase, receptor type D S homeolog
, receptor protein tyrosine phosphatase delta