Platelet-derived growth factor receptor

PDGFRplatelet derived growth factor receptorPDGF receptorPDGF-Rreceptors, platelet-derived growth factor(PDGFRPDGF-receptorsPI3K pathwayPlatelet-derived growth factor receptor-likeproteins
Platelet-derived growth factor receptors (PDGF-R) are cell surface tyrosine kinase receptors for members of the platelet-derived growth factor (PDGF) family.wikipedia
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Tyrosine kinase

tyrosine kinasesprotein-tyrosine kinaseprotein tyrosine kinase
The extracellular region of the receptor consists of five immunoglobulin-like domains while the intracellular part is a tyrosine kinase domain.
Sunitinib is an oral tyrosine kinase inhibitor that acts upon vascular endothelial growth factor receptor (VEGFR), platelet-derived growth factor receptor (PDGFR), stem cell factor receptor, and colony-stimulating factor-1 receptor (Burstein et al. 2008)

Receptor tyrosine kinase

receptor tyrosine kinasestyrosine kinase receptortyrosine kinase receptors
Platelet-derived growth factor receptors (PDGF-R) are cell surface tyrosine kinase receptors for members of the platelet-derived growth factor (PDGF) family.

PDGFRA

PDGFR-αPDGFRαPlatelet-derived growth factor receptor A
There are two forms of the PDGF-R, alpha and beta each encoded by a different gene.

PDGFRB

PDGFRβPDGFR-βplatelet-derived growth factor B
There are two forms of the PDGF-R, alpha and beta each encoded by a different gene.

Crenolanib

Crenolanib is an orally bioavailable benzamidazole that selectively and potently inhibits signaling of wild-type and mutant isoforms of class III receptor tyrosine kinases (RTK) FLT3 (FMS-like Tyrosine Kinase 3), PDGFR α (Platelet-Derived Growth Factor Receptor), and PDGFR β.

Imatinib

Gleevecimatinib mesylateSTI571
The FDA has approved imatinib for use in adults with relapsed or refractory Philadelphia chromosome-positive acute lymphoblastic leukemia (Ph+ ALL), myelodysplastic/ myeloproliferative diseases associated with platelet-derived growth factor receptor gene rearrangements, aggressive systemic mastocytosis without or an unknown D816V c-KIT mutation, hypereosinophilic syndrome and/or chronic eosinophilic leukemia who have the FIP1L1-PDGFRα fusion kinase (CHIC2 allele deletion) or FIP1L1-PDGFRα fusion kinase negative or unknown, unresectable, recurrent and/or metastatic dermatofibrosarcoma protuberans.

Platelet-derived growth factor

PDGFplatelet derived growth factorproto-oncogene proteins c-sis
Platelet-derived growth factor receptors (PDGF-R) are cell surface tyrosine kinase receptors for members of the platelet-derived growth factor (PDGF) family.

PDGFA

-A
PDGF subunits -A and -B are important factors regulating cell proliferation, cellular differentiation, cell growth, development and many diseases including cancer.

PDGFB

PDGF-B-BPDGF-BB
PDGF subunits -A and -B are important factors regulating cell proliferation, cellular differentiation, cell growth, development and many diseases including cancer.

Cellular differentiation

differentiationcell differentiationdifferentiate
PDGF subunits -A and -B are important factors regulating cell proliferation, cellular differentiation, cell growth, development and many diseases including cancer.

Cell growth

proliferationcell proliferationgrowth
PDGF subunits -A and -B are important factors regulating cell proliferation, cellular differentiation, cell growth, development and many diseases including cancer.

Morphogenesis

developmentmorphogeneticmorphogenic
PDGF subunits -A and -B are important factors regulating cell proliferation, cellular differentiation, cell growth, development and many diseases including cancer.

Cancer

cancersmalignanciescancerous
PDGF subunits -A and -B are important factors regulating cell proliferation, cellular differentiation, cell growth, development and many diseases including cancer.

Protein dimer

heterodimerdimerhomodimer
The PDGF family consists of PDGF-A, -B, -C and -D, which form either homo- or heterodimers (PDGF-AA, -AB, -BB, -CC, -DD).

Monomer

monomersmonomeric-mer
The four PDGFs are inactive in their monomeric forms.

Extracellular

extracellular spaceextracellular environment[2
The extracellular region of the receptor consists of five immunoglobulin-like domains while the intracellular part is a tyrosine kinase domain.

Receptor (biochemistry)

receptorreceptorscellular receptors
The extracellular region of the receptor consists of five immunoglobulin-like domains while the intracellular part is a tyrosine kinase domain.

Antibody

antibodiesimmunoglobulinimmunoglobulins
The extracellular region of the receptor consists of five immunoglobulin-like domains while the intracellular part is a tyrosine kinase domain.

Activation

bioactivationbioactivatedactivated
Dimerization is a prerequisite for the activation of the kinase.

Kinase

kinaseskinase domainprotein kinase C
Dimerization is a prerequisite for the activation of the kinase. In conjunction with dimerization and kinase activation, the receptor molecules undergo conformational changes, which allow a basal kinase activity to phosphorylate a critical tyrosine residue, thereby "unlocking" the kinase, leading to full enzymatic activity directed toward other tyrosine residues in the receptor molecules as well as other substrates for the kinase.

Phosphorylation

phosphorylatedphosphorylatephosphorylates
Kinase activation is visualized as tyrosine phosphorylation of the receptor molecules, which occurs between the dimerized receptor molecules (transphosphorylation).

Transphosphorylation

Kinase activation is visualized as tyrosine phosphorylation of the receptor molecules, which occurs between the dimerized receptor molecules (transphosphorylation).

Conformational change

conformationchanges conformationchange conformation
In conjunction with dimerization and kinase activation, the receptor molecules undergo conformational changes, which allow a basal kinase activity to phosphorylate a critical tyrosine residue, thereby "unlocking" the kinase, leading to full enzymatic activity directed toward other tyrosine residues in the receptor molecules as well as other substrates for the kinase.

Enzyme

enzymologyenzymesenzymatic
In conjunction with dimerization and kinase activation, the receptor molecules undergo conformational changes, which allow a basal kinase activity to phosphorylate a critical tyrosine residue, thereby "unlocking" the kinase, leading to full enzymatic activity directed toward other tyrosine residues in the receptor molecules as well as other substrates for the kinase.

Substrate (chemistry)

substratessubstratesubstrate specificity
In conjunction with dimerization and kinase activation, the receptor molecules undergo conformational changes, which allow a basal kinase activity to phosphorylate a critical tyrosine residue, thereby "unlocking" the kinase, leading to full enzymatic activity directed toward other tyrosine residues in the receptor molecules as well as other substrates for the kinase.