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The diabetes-induced increase in PDGFRalpha+ cells may be mediated by FOXO3 up-regulation via the inhibition of the PI3K/Akt signaling pathway in STZ-induced diabetic mice.
Constitutive activation of PDGFRalpha leads to expansion of cartilage underlying the coronal sutures, which contribute to suture closure through endochondral ossification, in a process regulated in part by PI3K/AKT (show AKT1 Proteins) signaling.
OLIG2 (show OLIG2 Proteins) modulates growth factor signaling in two distinct populations of glioma stem cells, characterized by expression of either the epidermal growth factor receptor (EGFR (show EGFR Proteins)) or platelet-derived growth factor receptor alpha.
Conditional knockout of Pdgfra in Pdgfra-expressing tissues in mouse embryos at different embryonic days (E9.5 and E10.5) resulted in multiple developmental anomalies of the frontonasal region, the cranium and the abdominal wall musculature. Furthermore, the day at which the Pdgfra is deleted influences the repertoire of the anomalies of the conditional knockout embryos.
FOXA3 (show FOXA3 Proteins) is a marker of the Sertoli cell lineage and of the adult Leydig cell population, and is a regulator of Pdgfra transcription in Leydig cells.
PDGFRalpha and PDGFRbeta are coexpressed in the craniofacial mesenchyme of mid-gestation mouse embryos and that ablation of Pdgfrb (show PDGFRB Proteins) in the neural crest lineage results in increased nasal septum width, delayed palatal shelf development, and subepidermal blebbing.
The results from this study indicate that PDGF (show PDGFA Proteins) signaling is required for fiber hypertrophy, extracellular matrix production, and angiogenesis that occur during muscle growth.
transient middle cerebral-arterial occlusion (MCAO) was introduced into the mice with conditional Pdgfrb (show PDGFRB Proteins)-gene inactivation, including N-PRbeta-KO mice where the Pdgfrb (show PDGFRB Proteins)-gene was mostly inactivated in the brain except that in vascular pericytes
PDGFR alpha has an important role in cranial neural crest cell mitosis within the mandibular processes
PDGF (show PDGFA Proteins) signalling in the dermis and in dermal condensates is dispensable for hair follicle induction and formation.
PDGFRalpha levels are regulated by SMARCB1 (show SMARCB1 Proteins) expression, and assessment of clinical specimens documents the expression of both PDGFRalpha and FGFR1 (show FGFR1 Proteins) in rhabdoid tumor patients.
The downregulation of platelet-derived growth factor receptor-alpha expression may play a causative role in imatinib-induced thrombocytopenia, a common side effect, in the subset of chronic myeloid leukemia (show BCL11A Proteins) patients with platelet-derived growth factor receptor-alpha +68 GA ins (show INS Proteins)/del, +68 GA del/del, and -909C/A genotypes.
Data indicate that co-inhibition of FGFR1 (show FGFR1 Proteins) and HER2 (show ERBB2 Proteins) or PDGFRalpha led to enhanced drug responses.
High PDGFRA expression is associated with pathogenesis of malignant peripheral nerve sheath tumor.
The interaction between CSR1 (show SCARA3 Proteins) and SF3A3 (show SF3A3 Proteins) led to migration of SF3A3 (show SF3A3 Proteins) from nucleus to cytoplasm. The cytoplasmic redistribution of SF3A3 (show SF3A3 Proteins) significantly reduced the splicing efficiency of epidermal growth factor receptor (show EGFR Proteins) and platelet-derived growth factor receptor (show PDGFRL Proteins).
PDGFRa amplification in multiple skin lesions of undifferentiated pleomorphic sarcoma
PDGFRA mutations were associated with gastrointestinal stromal tumors.
The PDGFRA kinase domain structure we report in this study has potential to facilitate development of new agents which can inhibit this kinase, including both its activating and drug-resistant mutations.
BRAF (show BRAF Proteins) mutations are rare events in KIT/PDGFRA wild-type gastrointestinal stromal tumors.
There are two platelet-derived growth factor receptor (PDGFR (show PDGFRB Proteins)) genes (PDGFRA and PDGFRB (show PDGFRB Proteins)), and they reside on chromosome 4 and 5.
This gene encodes a cell surface tyrosine kinase receptor for members of the platelet-derived growth factor family. These growth factors are mitogens for cells of mesenchymal origin. The identity of the growth factor bound to a receptor monomer determines whether the functional receptor is a homodimer or a heterodimer, composed of both platelet-derived growth factor receptor alpha and beta polypeptides. Studies suggest that this gene plays a role in organ development, wound healing, and tumor progression. Mutations in this gene have been associated with idiopathic hypereosinophilic syndrome, somatic and familial gastrointestinal stromal tumors, and a variety of other cancers.
platelet-derived growth factor receptor, alpha polypeptide
, alpha-type platelet-derived growth factor receptor-like
, Alpha platelet-derived growth factor receptor precursor (PDGF-R-alpha)
, CD140 antigen-like family member A
, PDGF alpha chain
, alpha-type platelet-derived growth factor receptor
, platelet-derived growth factor alpha receptor
, platelet-derived growth factor receptor alpha
, alpha platelet-derived growth factor receptor
, CD140a antigen
, PDGFRA/BCR fusion
, platelet-derived growth factor receptor 2
, rearranged-in-hypereosinophilia-platelet derived growth factor receptor alpha fusion protein
, tyrosine kinase PDGFR