PDGF-D, a new protease-activated growth factor

@article{Larochelle2001PDGFDAN,
  title={PDGF-D, a new protease-activated growth factor},
  author={William J. Larochelle and Michael E. Jeffers and William F. McDonald and Rajeev A. Chillakuru and Neill A. Giese and Nathalie Andrienne Lokker and Carol M. Sullivan and Ferenc L. Boldog and Meijia Yang and Corine Vernet and Catherine E. Burgess and Elma R. Fernandes and Lisa L. Deegler and Beth Rittman and Juliette Shimkets and Richard A. Shimkets and Jonathan Rothberg and Henri S. Lichenstein},
  journal={Nature Cell Biology},
  year={2001},
  volume={3},
  pages={517-521}
}
Platelet-derived growth factor (PDGF) has been directly implicated in developmental and physiological processes, as well as in human cancer, fibrotic diseases and arteriosclerosis. The PDGF family currently consists of at least three gene products, PDGF-A, PDGF-B and PDGF-C, which selectively signal through two PDGF receptors (PDGFRs) to regulate diverse cellular functions. After two decades of searching, PDGF-A and B were the only ligands identified for PDGFRs. Recently, however, database… 
PDGF-D is a specific, protease-activated ligand for the PDGF β-receptor
TLDR
PDGF-DD is the first known PDGFR-β-specific ligand, and its unique receptor specificity indicates that it may be important for development and pathophysiology in several organs.
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TLDR
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A Potential Oncogenic Activity of Platelet-Derived Growth Factor D in Prostate Cancer Progression
TLDR
It is shown that LNCaP cells auto-activate latent PDGF DD into the active PDGF domain, which can induce phosphorylation of the β-PDGF receptor and stimulates L NCaP cell proliferation in an autocrine manner, demonstrating a potential oncogenic activity of PDGFDD in the development and/or progression of prostate cancer.
Novel PDGF family members: PDGF-C and PDGF-D.
Factor D in Prostate Cancer Progression A Potential Oncogenic Activity of Platelet-Derived Growth Updated
TLDR
It is shown that LNCaP cells auto-activate latent PDGF DD into the active PDGF domain, which can induce phosphorylation of the -PDGF receptor and stimulates L NCaP cell proliferation in an autocrine manner, demonstrating a potential oncogenic activity of PDGFDD in the development and/or progression of prostate cancer.
Neuropilin 1 binds platelet-derived growth factor ( PDGF )-D and is a co-receptor in PDGF-D / PDGF receptor β signaling
TLDR
It is demonstrated that NRP1 can act as a co-receptor for PDGF-D in PDGFRβ signaling, possibly implicated in intercellular communication in the vascular wall.
Exploring the role of PDGF-D in health and disease
TLDR
The PDGF-D knockout mouse strain is presented, and the expression and function is characterized in vivo, in both physiological conditions and in the tumor setting, and evidence that paracrine PD GF-D signaling from the vasculature induces the production of factors from a rare PDGFRβ-expressing tumor cell subpopulation, thereby contributing to tumor growth is presented.
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References

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PDGF-D is a specific, protease-activated ligand for the PDGF β-receptor
TLDR
PDGF-DD is the first known PDGFR-β-specific ligand, and its unique receptor specificity indicates that it may be important for development and pathophysiology in several organs.
PDGF-C is a new protease-activated ligand for the PDGF α-receptor
TLDR
A new PDGF, PDGF-C, is identified, which binds to and activates the PDGF α-receptor and is activated by proteolysis and induces proliferation of fibroblasts when overexpressed in transgenic mice.
Mechanism of action and in vivo role of platelet-derived growth factor.
TLDR
Structural and functional properties of PDGF and PDGF receptors, the mechanism whereby PDGF exerts its cellular effects, and the role ofPDGF in normal and diseased tissues are discussed.
Functional Importance of Platelet-derived Growth Factor (PDGF) Receptor Extracellular Immunoglobulin-like Domains
The biological effects of platelet-derived growth factor (PDGF) are mediated by α- and β-PDGF receptors (PDGFR), which have an intracellular tyrosine kinase domain and an extracellular region
A novel mechanism regulating growth factor association with the cell surface: identification of a PDGF retention domain.
TLDR
It is demonstrated that this PDGF-A domain also acts as a retention sequence under conditions that inhibit its proteolytic cleavage, which establishes a new mechanism for stable growth factor presentation at the cell surface.
Sera and conditioned media contain different isoforms of platelet-derived growth factor (PDGF) which bind to different classes of PDGF receptor.
TLDR
The existence of isoform-specific PDGF receptors and the large variation in PDGF isoform composition dependent upon source may provide an important mechanism through which the effects of PDGF can be targeted to different cell types and/or toward eliciting different cell responses.
cDNA cloning and expression of the human A-type platelet-derived growth factor (PDGF) receptor establishes structural similarity to the B-type PDGF receptor.
TLDR
The primary structure of the human A-type receptor for platelet-derived growth factor (PDGF) has been determined and the expression of a protein specifically recognized by an antiserum previously shown to react with the PDGF A- type receptor was shown to display high-affinity binding of all three 125I-labeled dimeric forms ofPDGF A and B chains.
Isolation of a novel receptor cDNA establishes the existence of two PDGF receptor genes.
TLDR
The existence of genes encoding two PDGF receptors that interact in a distinct manner with three different PDGF isoforms likely confers considerable regulatory flexibility in the functional responses to PDGF.
Abnormal kidney development and hematological disorders in PDGF beta-receptor mutant mice.
TLDR
Results indicate that whereas the beta receptor is essential in certain cell types during embryonic development, its broader role may be masked because of compensation by the alpha-subunit.
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