Coexpression of the genes for platelet-derived growth factor B-chain receptor and macrophage colony-stimulating factor 1 receptor during monocytic differentiation.

Pantazis, Panayotis; Kharbanda, Surender; Goustin, Anton Scott; T, Galanopoulos; Küfe, Donald

doi:10.1073/pnas.88.6.2481

Cited by 12 publications

(4 citation statements)

References 34 publications

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“…Several observations suggest that PDGFRβ signaling could play a role in hematopoietic cell proliferation. First, low level expression of PDGFRβ has been observed in murine myeloblastic, mast and multipotential cell lines (de Parseval et al ., 1993) and during the differentiation of primary monocytes and of cell lines THP1 and HL60 (Pantazis et al ., 1991; Inaba et al ., 1993). Second, PDGF treatment in several of these situations has been shown to induce a mitogenic response in both immature and mature cells (de Parseval et al ., 1993; Inaba et al ., 1993).…”

Section: Discussionmentioning

confidence: 99%

A domain of TEL conserved in a subset of ETS proteins defines a specific oligomerization interface essential to the mitogenic properties of the TEL-PDGFRbeta oncoprotein

1997

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TEL is a novel member of the ETS family of transcriptional regulators which is frequently involved in human leukemias as the result of specific chromosomal translocations. We show here by co-immunoprecipitation and GST chromatography analyses that TEL and TEL-derived fusion proteins form homotypic oligomers in vitro and in vivo. Deletion mutagenesis identifies the TEL oligomerization domain as a 65 amino acid region which is conserved in a subset of the ETS proteins including ETS-1, ETS-2, FLI-1, ERG-2 and GABP alpha in vertebrates and PNTP2, YAN and ELG in Drosophila. TEL-induced oligomerization is shown to be essential for the constitutive activation of the protein kinase activity and mitogenic properties of TEL-platelet derived growth factor receptor beta (PDGFR beta), a fusion oncoprotein characteristic of the leukemic cells of chronic myelomonocytic leukemia harboring a t(5;12) chromosomal translocation. Swapping experiments in which the TEL oligomerization domain was exchanged by the homologous domains of representative vertebrate ETS proteins including ETS-1, ERG-2 and GABP alpha show that oligomerization is a specific property of the TEL amino-terminal conserved domain. These results indicate that the amino-terminal domain conserved in a subset of the ETS proteins has evolved to generate a specialized protein-protein interaction interface which is likely to be an important determinant of their specificity as transcriptional regulators.

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Section: Discussionmentioning

confidence: 99%

A domain of TEL conserved in a subset of ETS proteins defines a specific oligomerization interface essential to the mitogenic properties of the TEL-PDGFRbeta oncoprotein

1997

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“…The PDGF competitor for the blots probed with Anti-A was PDGF-AA; for the blots probed with anti-PDGF, PDGF-AB was the competitor. isolated human blood monocytes, Pantazis et al (38) reported expression and production of PDGFR-13 in phorbol estertreated monocytic leukemia cell lines. Perhaps foreign body activation of macrophages induces expression of PDGFR-13 in a similar manner as phorbol ester.…”

Section: Discussionmentioning

confidence: 99%

Regional expression of the platelet-derived growth factor and its receptors in a primate graft model of vessel wall assembly.

Kraiss¹,

Raines²,

Wilcox³

et al. 1993

J. Clin. Invest.

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Healing baboon polytetrafluoroethylene grafts express PDGF mRNA in the neointima. Perfusates of graft segments also contain PDGF-like mitogenic activity. To extend these findings, we studied the expression and regional distribution of the PDGF protein isoforms and their receptors in this prosthetic graft model. By immunohistochemistry, as well as ELISA and Western blot analysis of tissue extracts, both PDGF-A and PDGF-B were identified in macrophages within the interstices of the synthetic material. In contrast, the neointima contained predominantly PDGF-A localized to the endothelial surface and the immediate subjacent smooth muscle cell layers. Tissue extracts of neointima and graft material were mitogenic for baboon aortic smooth muscle cells in culture; nearly all of this proliferative activity was blocked by a neutralizing anti-PDGIF antibody. PDGF receptor,8-subunit mRNA and protein were easily detectable in the neointima and graft material. PDGF receptor a-subunit mRNA was also observed in the graft matrix and at lower levels in the neointima. This pattern of ligand and receptor expression further implicates locally produced PDGF as a regulator of neointimal smooth muscle cell growth in this model. The coexpression of ligand and receptor in the macrophage-rich matrix also suggests that PDGF may participate in the foreign body response. (J. Clin. Invest. 1993. 92:338-348.)

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“…The expression of PDGFRa is specifically detected in subtypes of mesenchymal precursor cells located in the lung, skin, and intestine, whereas PDGFRb is expressed in pericytes and vascular smooth muscle cells (36). Other cells expressing PDGFRa are human platelets, mouse megakaryocytes, and rat liver endothelial cells (52)(53)(54); PDGFRb is expressed in mouse capillary endothelial cells (55), T cells, and macrophages (35,(56)(57)(58). Cultured monocytes (59) and natural killer (NK) cells (60) also express PDGFRb.…”

Section: Pdgf Receptorsmentioning

confidence: 99%

Platelet-Derived Growth Factor Signaling in the Lung. From Lung Development and Disease to Clinical Studies

Noskovičová

Petřek²,

Eickelberg³

et al. 2015

Am J Respir Cell Mol Biol

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Platelet-derived growth factors (PDGFs) and their receptors (PDGFRs) represent one of the most intensively studied families of growth factors in the last four decades. PDGF signaling plays an essential role in cell proliferation, differentiation, migration, and survival. In vivo studies have documented an important role of PDGF signaling in the normal development of several organs, such as the kidney, eye, or lung. PDGF signaling is essential for the formation of intact mesenchymal cells during embryogenesis. Recently, this knowledge has been extended to a role of PDGF signaling in diseases in general, such as cancer and atherosclerosis, and more importantly in lung diseases, including pulmonary arterial hypertension, lung cancer, and lung fibrosis. In this review, we provide an up-to-date overview of PDGF signaling, including tissue- and cell-type-specific expression patterns and effects. We highlight current therapeutic approaches modifying PDGF signaling in lung diseases and summarize clinical trials in which PDGF signaling has been inhibited. In conclusion, although PDGF inhibition has been used in multiple clinical trials, we suggest that more elaborate and specific approaches for spatio-temporal control of PDGF signaling are required for developing personalized approaches involving PDGF signaling in lung disease.

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Coexpression of the genes for platelet-derived growth factor B-chain receptor and macrophage colony-stimulating factor 1 receptor during monocytic differentiation.

Cited by 12 publications

References 34 publications

A domain of TEL conserved in a subset of ETS proteins defines a specific oligomerization interface essential to the mitogenic properties of the TEL-PDGFRbeta oncoprotein

A domain of TEL conserved in a subset of ETS proteins defines a specific oligomerization interface essential to the mitogenic properties of the TEL-PDGFRbeta oncoprotein

Regional expression of the platelet-derived growth factor and its receptors in a primate graft model of vessel wall assembly.

Platelet-Derived Growth Factor Signaling in the Lung. From Lung Development and Disease to Clinical Studies

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