cDNA clones reveal differences between human glial and endothelial cell platelet-derived growth factor A-chains

Tong, Benton D.; Auer, David E.; Jaye, Michael; Kaplow, June; Ricca, George A.; McConathy, Evelyn; Drohan, William N.; Deuel, Thomas F.

doi:10.1038/328619a0

Cited by 95 publications

(35 citation statements)

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“…In vivo, PDGF isoforms are produced by normal surrounding tissues or cells present in tumors, such as macrophages and vascular endothelial cells (2,51,52). Moreover, normal mammalian nervous tissue has been shown to express PDGF-AA and -BB ( 14,15).…”

Section: Discussionmentioning

confidence: 99%

Human neuroblastoma cells express alpha and beta platelet-derived growth factor receptors coupling with neurotrophic and chemotactic signaling.

Matsui¹,

Sano²,

Tsukamoto³

et al. 1993

J. Clin. Invest.

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Both platelet-derived growth factor (PDGF) A-and B-chains are expressed in mammalian neurons, but their precise roles still remain to be clarified. In the present studies, we examined the expression of two PDGF receptor genes in human tumor cell lines derived from neural crest. The expression of a and / or , PDGF receptors was detected in a wide variety of neural crest-derived human tumor cell lines such as neuroblastoma, primitive neuroectodermal tumor, and Ewing's sarcoma by RNA blot analysis, and confirmed by immunoblot analysis. We have also demonstrated that PDGF receptors on the human neuroblastoma cell lines were biologically functional. Accordingly, chemotactic and mitogenic activities were induced by either PDGF-AA or PDGF-BB in serum-free medium. PDGF isoforms as well as nerve growth factor induced morphological changes showing neuronal cell maturation. Moreover, PDGF coordinately increased the levels of the transcript ofthe midsize neurofilament gene. The neuroblastoma cell lines also expressed the transcripts of PDGF A-and B-chains. These findings suggest that PDGF isoforms are involved not only in the promotion of the neuroblastoma cell growth, but also in neuronal cell migration, growth, and differentiation in human brain development. (J. Clin. Invest. 1993. 92:1153-1160

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Section: Discussionmentioning

confidence: 99%

Human neuroblastoma cells express alpha and beta platelet-derived growth factor receptors coupling with neurotrophic and chemotactic signaling.

Matsui¹,

Sano²,

Tsukamoto³

et al. 1993

J. Clin. Invest.

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“…For example, bovine aortic or human umbilical vein endothelial cells stripped from blood vessels contain only 10% and 1.3%, respectively, as much Bchain transcript as the same cells in monolayer culture (28). When endothelium switches from a monolayer to tubelike structures in culture it alters its expression of A-and B-chain mRNA (29)(30)(31). Transient expression of PDGF is induced in response to cell activation by coagulation factors and by cytokines, as well as by variations in cell substrate (1,12,27).…”

Section: Discussionmentioning

confidence: 99%

Platelet-derived growth factor activity and mRNA expression in healing vascular grafts in baboons. Association in vivo of platelet-derived growth factor mRNA and protein with cellular proliferation.

Golden¹,

Au²,

Kirkman³

et al. 1991

J. Clin. Invest.

117

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In a baboon graft model of arterial intimal thickening, smooth muscle cells (SMC) have been observed to proliferate underneath an intact monolayer of endothelium and in the absence of platelet adherence. Because platelets are not present and therefore cannot be a major source of growth stimulus, we have proposed that the vascular wall cells in the graft intima express mitogens and regulate SMC proliferation. To test this hypothesis, we assayed the grafts for mitogenic activity and expression of growth factor genes. Segments of healing graft and of normal artery, when perfused ex vivo, released mitogenic activity into the perfusate. The graft released more mitogen than the normal arterial segment, and some of the activity was inhibitable with an antibody to human platelet-derived growth factor (PDGF). In addition, Northern analysis of total RNA demonstrated higher expression of PDGF-A chain mRNA in the graft intima compared to normal artery. PDGF-B chain mRNA was barely detectable in both tissues. PDGF mRNA levels within the graft interstices were not measured. In situ hybridization of 7.5-or 12-wk grafts indicated that some luminal endothelial cells and adjacent intimal SMC contained PDGF-A chain mRNA. By thymidine autoradiography, intimal SMC were observed to be proliferating in the inner third of the intima. These data demonstrate a difference in the pattern of PDGF transcript expression and luminal perfusate activity in graft as compared with control arteries. The association of intimal smooth muscle cell proliferation with intimal PDGF mRNA expression and release of PDGF-like protein supports the hypothesis that factors from cells that have grown into the graft or populated its surface rather than platelets may regulate intimal smooth muscle cell proliferation in this model. (J. Clin. Invest. 1991. 87:406-414.)

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“…A propeptide-like sequence, with no homology to known sequences, extends from residue 164 to ϳ234 in the human protein. The C-terminal portion of PDGF-C, termed GFD, has 25% homology to VEGF (4) and 23% homology to PDGF A-chain (32,33). Separating the propeptide and GFD is a predicted protease cleavage site (RKSR, residues 231-234).…”

Section: Identification and Characterization Of Human Pdgf-cmentioning

confidence: 99%

Platelet-derived Growth Factor C (PDGF-C), a Novel Growth Factor That Binds to PDGF α and β Receptor

Gilbertson¹,

Duff²,

West³

et al. 2001

Journal of Biological Chemistry

245

224

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We have characterized platelet-derived growth factor (PDGF) C, a novel growth factor belonging to the PDGF family. PDGF-C is a multidomain protein with the Nterminal region homologous to the extracellular CUB domain of neuropilin-1, and the C-terminal region consists of a growth factor domain (GFD) with homology to vascular endothelial growth factor (25%) and PDGF Achain (23%). A serum-sensitive cleavage site between the two domains allows release of the GFD from the CUB domain. Competition binding and immunoprecipitation studies on cells bearing both PDGF ␣ and ␤ receptors reveal a high affinity binding of recombinant GFD (PDGF-CC) to PDGF receptor-␣ homodimers and PDGF receptor-␣/␤ heterodimers. PDGF-CC exhibits greater mitogenic potency than PDGF-AA and comparable or greater mitogenic activity than PDGF-AB and PDGF-BB on several mesenchymal cell types. Analysis of PDGF-CC in vivo in a diabetic mouse model of delayed wound healing showed that PDGF-CC significantly enhanced repair of a full-thickness skin excision. Together, these studies describe a third member of the PDGF family (PDGF-C) as a potent mitogen for cells of mesenchymal origin in in vitro and in vivo systems with a binding pattern similar to PDGF-AB.

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cDNA clones reveal differences between human glial and endothelial cell platelet-derived growth factor A-chains

Cited by 95 publications

References 0 publications

Human neuroblastoma cells express alpha and beta platelet-derived growth factor receptors coupling with neurotrophic and chemotactic signaling.

Human neuroblastoma cells express alpha and beta platelet-derived growth factor receptors coupling with neurotrophic and chemotactic signaling.

Platelet-derived growth factor activity and mRNA expression in healing vascular grafts in baboons. Association in vivo of platelet-derived growth factor mRNA and protein with cellular proliferation.

Platelet-derived Growth Factor C (PDGF-C), a Novel Growth Factor That Binds to PDGF α and β Receptor

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