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  • 1
    Electronic Resource
    Electronic Resource
    Protamine inhibits platelet derived growth factor receptor activity but not epidermal growth factor activity (1984)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 26 (1984), S. 205-220 
    Details
    ISSN: 0730-2312
    Keywords: PDGF ; EGF ; receptor ; oncogenes ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Protamine sulfate blocked 125I-PDGF binding to its specific physiological receptor on Swiss mouse 3T3 cells. Reduced 125I-PDGF binding in the presence of protamine sulfate correlated directly with a protamine sulfate dose-dependent decrease in the PDGF-dependent incorporation of [3H]-thymidine into 3T3 cells and a decreased PDGF-stimulated tyrosine-specific protein kinase activity in isolated membrane preparations of 3T3 cells. Protamine sulfate blocked 125I-PDGF binding to simian sarcoma virus transformed cells (SSV-NIH 3T3 and SSV-NPl cells) and to nontransformed cells in a manner qualitatively identical to unlabelled PDGF. In contrast, protamine sulfate enhanced the specific binding of 125I-EGF by increasing the apparent number of EGF receptors on the cell surface. The increase in 125I-EGF receptor binding was not prevented by cycloheximide nor by actinomycin D. Protamine sulfate did not affect 125I-EGF binding to membranes from 3T3 cells or the EGF-stimulated 3T3 cell membrane tyrbsinc specific protein kinase activity, suggesting that protamine sulfate may have exposed a population of cryptic EGF receptors otherwise not accessible. Protamine sulfate was fractionated into four active fractions by Sephadex G-50 gel filtration columns; the half maximum inhibition concentration of 125I-PDGF binding to 3T3 cells of protamines I and II (MW ∼ 11,000 daltons and 7,000 daltons, respectively) is ∼ 0.4 μM. Protamine II (MW ∼ 4,800 daltons) was equally active (half maximum inhibition concentration ∼ 0.4 μM); protamine IV (MW ∼ 3,300 daltons) was substantially less active (half maximum inhibition concentration ∼ 2.8 μM).These investigations have extended previous observations that protamine sulfate is a potent inhibitor of PDGF binding and establish that protamine sulfate blocks PDGF binding at the physiological receptor, preventing PDGF initiated biological activities. Protamine sulfate can be used as a reagent to separate the influence of PDGF and EGF on cells with high specificity and has been used to demonstrate that the receptors on simian sarcoma virus transformed 3T3 cells qualitatively respond identically to protamine sulfate as to unlabelled PDGF and are likely identical to those on nontransformed 3T3 cells.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240260402
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  • 2
    Electronic Resource
    Electronic Resource
    Platelet-derived growth factor is structurally related to the putative transforming protein p28 sis of simian sarcoma virus (1983)
    [s.l.] : Nature Publishing Group
    Nature 304 (1983), S. 35-39 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A partial amino acid sequence of human platelet-derived growth factor, the major mitogen in serum for cells of mesenchymal origin, has been determined. A region of 104 contiguous amino acids shows virtual identity with the predicted sequence of p28sis, the putative transforming ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/304035a0
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  • 3
    Electronic Resource
    Electronic Resource
    cDNA clones reveal differences between human glial and endothelial cell platelet-derived growth factor A-chains (1987)
    [s.l.] : Nature Publishing Group
    Nature 328 (1987), S. 619-621 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Three different cDNA clones were isolated from a Agtll HUVE cell-derived cDNA library8 using two oligonucleotide probes (A-l and A-2, Fig. 1), subcloned into the EcoRl site of pGEM-2, and sequenced10. The DNA sequence of the largest cDNA clone (BT-1) begins at nucleotide 351 and continues to about ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/328619a0
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  • 4
    Electronic Resource
    Electronic Resource
    Role of platelet-derived growth factor in wound healing (1991)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 45 (1991), S. 319-326 
    Details
    ISSN: 0730-2312
    Keywords: tissue repair ; macrophage ; fibroblast ; extracellular matrix ; growth factors ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Platelet-derived growth factor (PDGF) is a potent activator for cells of mesenchymal origin. PDGF stimulates chemotaxis, proliferation, and new gene expression in monocytes-macrophages and fibroblasts in vitro, cell types considered essential for tissue repair. Therefore, we analyzed the influence of exogenously administered recombinant B chain homodimers of PDGF (PDGF-BB) on two experimental tissue repair paradigms, incisional and excisional wounds. In both types of wounds, as little as 20-200 picomoles applied a single time to wounds significantly augmented the time dependent influx of inflammatory cells and fibroblasts and accelerated provisional extracellular matrix deposition and subsequent collagen formation. In incisional wounds, PDGF-BB augmented wound breaking strength 50-70% over the first 3 weeks; in excisional wounds, PDGF-BB accelerated time to closure by 30%. PDGF-BB exaggerated, but did not alter, the normal course of soft tissue repair, resulting in a significant acceleration of healing. Long term observations established no apparent differences between PDGF-BB treated and non-treated wounds. Thus, the vulnerary effects of PDGF-BB were transient and fully reversible in both wound healing models. Furthermore, analysis of PDGF-treated and non-treated wounds has provided important insights into mechanisms of normal and deficient tissue repair processes. PDGF appears to transduce its signal through wound macrophages and may trigger the induction of positive autocrine feedback loops and synthesis of endogenous wound PDGF and other growth factors, thereby enhancing the cascade of tissue repair processes required for a fully-healed wound. Thus, PDGF and other wound produced polypeptide growth factors may be the critical regulators of extracellular matrix deposition within healing wounds.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240450403
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  • 5
    Electronic Resource
    Electronic Resource
    Platelet-derived growth factor/sis in normal and neoplastic cell growth (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 133 (1987), S. 95-99 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Platelet-derived growth factor (PDGF) is the major growth factor in serum and a potent mitogen for cells mesenchymal origin. It is a highly basic heterodimeric protein with a molecular mass of -30 kDa and binds to a cell surface receptor with high affinity. The amino acid sequence of PDGF revealed sequence homology to the v-sis gene product of simian sarcoma virus (SSV), a transforming retrovirus. Characterization of cells transformed by SSV has revealed PDGF-related proteins in subcellular organelles and in conditioned media consistent with the autocrine stimulation of cell growth through cell surface receptors and perhaps through an internal autocrine mechanism as the growth factor and its receptor are processed. PDGF is also a potent chemotactic agent for inflammatory and other mesenchymal cells and has been implicated in normal tissue repair processes such as wound healing, as well as in aberrant proliferative processes like atherogenesis.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041330418
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  • 6
    Electronic Resource
    Electronic Resource
    Inhibition of the binding of low-density lipoprotein to its cell surface receptor in human fibroblasts by positively charged proteins (1978)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 8 (1978), S. 223-234 
    Details
    ISSN: 0091-7419
    Keywords: low-density lipoprotein ; cell surface receptor ; fibroblasts ; platelet factor 4 ; histones ; protamine ; poly-L-lysine ; glycoproteins ; cholesterol ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: A group of proteins and polyamino acids with positively charged domains were shown to inhibit the binding of 125I-LDL to its receptor on the surface of human fibroblasts. The list of inhibitory proteins included platelet factor 4 (which has a cluster of lysine residues at its carboxyl terminus), two lysinerich histones, poly-L-lysines of chain length greater than 4, and protamine. These proteins were effective in the concentration range of 5-50 μg/ml. Two other positively charged proteins, lysozyme and avidin, did not inhibit 125I-LDL binding. Kinetic studies suggested that protamine was not acting simply as a competitive inhibitor with regard to the LDL receptor. In light of previous data showing that polyanions such as heparin and polyphosphates also inhibit 125I-LDL binding to its cell surface receptor, the current findings suggest that charge interactions are important in this binding reaction. In a related series of studies, a number of glycoproteins and their asialo derivatives as well as a number of sugar phosphates failed to inhibit 125I-LDL binding to its receptor in fibroblasts.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400080302
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