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  • intimal hyperplasia  (1)
  • phaseolin  (1)
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  • 1
    Electronic Resource
    Electronic Resource
    Effect of short-term treatment with a monoclonal antibody to P-selectin on balloon catheter-induced: Intimal hyperplasia, re-endothelialization, and attenuation of endothelial-dependent relaxation (1997)
    Springer
    Molecular and cellular biochemistry 176 (1997), S. 13-20 
    Details
    ISSN: 1573-4919
    Keywords: endothelium ; polymorphonuclear leukocyte ; nitric oxide ; intimal hyperplasia ; P-selectin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The effects of an anti-P-selectin monoclonal antibody (MAb, PB1.3; Cytel Corporation) on neoendothelialization; neoendothelial function, as evidenced by acetylcholine-induced relaxation (nitric oxide formation); and intimal hyperplasia following embolectomy catheter-induced injury to the rabbit thoracic aorta were investigated. Catheter injury was induced in two groups of New Zealand White rabbits. One group received no treatment, while the second group received short-term treatment with the MAb (i.p., immediately before and 12 h after induction of catheter injury). A third group underwent a sham operation and served as uninjured controls. Following sacrifice at 2 weeks after injury, aortic rings were assessed for degree of intimal hyperplasia, neoendothelial morphology (scanning electron microscopy), and acetylcholine-induced relaxation. Aortic tissue from catheter-injured animals that received treatment exhibited improved neoendothelial morphology, as compared with tissue from untreated but catheterized animals; however, no statistically significant attenuation of the hyperplastic response or improvement in the attenuated neoendothelial-dependent acetylcholine-induced relaxant response that is characteristic of neoendothelium that forms after catheter denudation was observed. These data suggest that short-term attenuation of P-selectin-mediated polymorphonuclear leukocyte (PMN)/endothelium, PMN/platelet interactions, and/or thrombin formation beneficially affects neoendothelialization of the vascular wall following balloon catheter-induced injury.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006858424790
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  • 2
    Electronic Resource
    Electronic Resource
    Expression of de novo high-lysine α-helical coiled-coil proteins may significantly increase the accumulated levels of lysine in mature seeds of transgenic tobacco plants (1997)
    Springer
    Plant molecular biology 34 (1997), S. 15-29 
    Details
    ISSN: 1573-5028
    Keywords: α-helical coiled-coil ; conglycinin ; lysine ; methionine ; phaseolin ; seed storage proteins ; nutritional quality
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have designed protein molecules based on an α-helical coiled-coil structure. These proteins can be tailored to complement nutritionally unbalanced seed meals. In particular, these proteins may contain up to 43% mol/mol of the essential amino acid lysine. Genes encoding such proteins were constructed using synthetic oligonucleotides and the protein stability was tested for in vivo by expression in an Escherichia coli model system. A protein containing 31% lysine and 20% methionine (CP 3-5) was expressed in transgenic tobacco seeds utilizing the seed specific bean phaseolin and soybean β-conglycinin promoters. Both promoters provided a level of expression in the mature transgenic tobacco seeds which resulted in a significant increase in the total lysine content of the seeds. Several of these transgenic lines were analyzed for three generations to determine the stability of gene expression. Plants transformed with the soybean β-conglycinin promoter/CP 3-5 gene consistently expressed the high-lysine phenotype through three generations. However, expression of the high-lysine phenotype in plants transformed with the bean phaseolin/CP 3-5 was variable. This is the first report of a significant increase in seed lysine content due to the seed-specific expression of a de novo protein sequence.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005809900758
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