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  • Life and Medical Sciences  (6)
  • growth factor receptors  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Production of a monoclonal antibody directed against the nerve growth factor receptor from sympathetic membranes (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 27 (1985), S. 121-132 
    Details
    ISSN: 0730-2312
    Keywords: growth factor receptors ; monoclonal antibodies ; nerve growth factor ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Spleen cells from BALB/c mice immunized with a plasma membrane-enriched fraction from rabbit sympathetic ganglia were fused with the mouse myeloma NS1. A hybrid clone was obtained that produced monoclonal antibody directed against the receptor for nerve growth factor (NGF). The antibody, identified as IgG, was able to immunoprecipitate solubilized NGF receptor in the presence or absence of bound NGF. The antibody bound specifically to sympathetic membranes with high affinity but did not affect the binding of 125I-NGF to its receptor in sympathetic or sensory neurons or PC12 cells.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240270206
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  • 2
    Electronic Resource
    Electronic Resource
    Purification and partial characterization of bovine pituitary fibroblast growth factor (1983)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 21 (1983), S. 195-208 
    Details
    ISSN: 0730-2312
    Keywords: pituitary fibroblast growth factor ; silver staining ; amino acid analysis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: A purification procedure and partial characterization of bovine pituitary fibroblast growth factor (FGF) are described. The steps of the published methods [3,4] which yield inhomogeneous material, were retained, with modifications. The final isolation, with an additional purification of ∼20-fold, was achieved by electro-phoresis in polyacrylamide gels at acid pH. The mitogenic peptide has a molecular weight of 14,500-15,00 as determined on SDS gels, chromatographs as a monomer in nondenaturing conditions, and is active at the picomolar level in effecting the incorporation of 3H-thymidine in Balb/c 3T3 cells. A preliminary amino acid composition is presented.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240210302
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  • 3
    Electronic Resource
    Electronic Resource
    Nerve growth factor biosynthesis: Isolation and characterization of a guinea pig prostate kallikrein (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 29 (1985), S. 309-319 
    Details
    ISSN: 0730-2312
    Keywords: guinea pig ; kallikrein ; nerve growth-factor ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Guinea pig prostate contains one major soluble esteropeptidase activity. The protein has been purified and characterized and found to be a glycoprotein comprised of a single polypeptide chain. The molecular weight of the deglycosylated protein is approximately 26,000. The esteropeptidase has a similar Km for lysine and arginine synthetic substrates, although the Vmax for arginine is much greater than that for lysine. Amino-terminal sequence analysis has also revealed a marked degree of homology to mouse γ-nerve growth factor (NGF) and the kallikrein family of serine proteases. In contrast to γ-NGF, however, the guinea pig enzyme does not appear to form stable complexes with β-NGF.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240290405
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  • 4
    Electronic Resource
    Electronic Resource
    Role of glandular kallikreins as growth factor processing enzymes: Structural and evolutionary considerations (1987)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 33 (1987), S. 65-75 
    Details
    ISSN: 0730-2312
    Keywords: precursor ; hormone ; limited proteolysis ; submandibular gland ; prostate ; nerve growth factor ; epidermal growth factor ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Hormones and growth factors are generally released from larger precursors by limited proteolysis. The causative agents remain poorly defined with respect to location and properties. One subset of proteases, the glandular kallikreins, have been implicated in a few cases, in part because of their specific association with mature forms of some hormones. However, limited distribution and low copy number in some species cast doubt on this hypothesis, and they may well play other physiological functions that remain to be elucidated.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240330107
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  • 5
    Electronic Resource
    Electronic Resource
    Modulation of growth factor induced fiber outgrowth in rat pheochromocytoma (PC12) cells by a fibronectin receptor antibody (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 138 (1989), S. 121-128 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Rat pheochromocytoma PC12 cells respond to the binding of nerve growth factor (NGF) and basic fibroblast growth factor (bFGF) by extending neurites in a manner resembling sympathetic neurons. This response requires cell attachment to an appropriate substratum (Fujii et al., J. Neurosci., 2:1157, 1982); attachment factors which function in this capacity include the adhesive proteins fibronectin and laminin. Incubating PC12 cells with a ployclonal antiserum directed against a putative 140-kDa fibroblast cell surface fibronectin receptor (anti-gp140) perturbed spreading but not attachment of the cells to fibronectin and laminin substrates. However, in the presence of anti-gp 140 or its Fab fragments, NGF-stimulated neurite outgrowth was dramatically reduced. The antibody also caused a retraction of previously extended neurites. SDS-PAGE analysis of immunoprecipitates of PC12 cells surface labeled with 125I identified a prominent 120-140-kDa band, suggesting that the site of anti-gp 140 action in PC12 cells is also through a fibronectin receptor.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041380117
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  • 6
    Electronic Resource
    Electronic Resource
    PC12-E2 cells: A stable variant with altered responses to growth factor stimulation (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 164 (1995), S. 522-532 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A variant cell line, designated E2, characterized by more rapid responses to nerve growth factor (NGF) and basic fibroblast growth factor (bFGF) and markedly more robust responses to interleukin-6 and 8-Br-cAMP, has been subcloned from the rat PC12 cell line. The enhanced responsiveness to NGF in E2 cells is not due to receptor overexpression as judged by TrkA protein levels and tyrosine kinase activity, but may be associated with the increased and prolonged tyrosine phosphorylation of ERK1 (extracellular signal regulated kinase 1) and ERK2. The rapid morphological differentiation induced by different growth factors in E2 cells is constitutively express some differentiation-associated molecules that allow direct entry into the neuronal program. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041640310
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