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  • 1
    ISSN: 1432-2307
    Keywords: Arginase ; Gastric cancer ; Immunohistochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract High levels of arginase have been detected in gastric adenocarcinoma. To examine the hypothesis that this is due to macrophage infiltration into the tumour, we localized the cellular distribution of arginase by immunohistochemical staining. We examined gastric adenocarcinomas and their corresponding normal tissues (n=45), leiomyomas (n=2), leiomyosarcomas (n=3), human gastric adenocarcinoma cell lines (n=3), and benign gastric ulcers (n=4) by the avidin-biotin-peroxidase complex technique. Macrophages with strong arginase immunoreactivity were observed infiltrating both gastric normal and cancer tissues. No arginase immunoreactivity was observed in normal mucosal gland, muscular and serosal tissues or benign gastric ulcers. The immunoreactivity of arginase was positive but heterogeneous in most specimens of gastric adenocarcinoma (62.2%) and was absent from gastric intestinal metaplasia, leiomyomas and leiomyosarcomas. Among the 28 neoplasms with arginase immunoreactivity, scattered immunoreactivity was also noted in adjacent dysplastic glands in 12 (42.8%) specimens. Arginase immunoreactivity was observed in all three gastric cancer cell lines. Arginase is present in the cytoplasm but not in the nucleus. These data suggest that the high arginase levels in adenocarcinoma cancer tissues originate largely from cancer cells.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1617-4623
    Keywords: Key words Protein kinase ; Wounding ; Abscisic acid ; Methyl jasmonate ; Signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A cDNA encoding a protein kinase, which may be involved in the wound signal transduction pathway, was isolated from Nicotiana tabacum. The cDNA, named WAPK, is 1227 bp in length and contains an ORF of 1017 bp. The ORF encodes a polypeptide of 339 amino acids, with a calculated molecular mass of 38234 Da. Analysis of the deduced amino acid sequence shows that the N-terminal region of WAPK contains a catalytic region composed of eleven subdomains which are typically found in Ser/Thr protein kinases. This region shows 78–84% sequence identity with similar regions of abscisic acid (ABA)-induced and external-stimuli-responsive protein kinases. However, the C-terminal region of WAPK shows little homology with similar regions of Ser/Thr protein kinases, except for a 16-amino acid stretch near the end of the catalytic domain. Kinase assays using a WAPK fusion protein expressed in E. coli revealed that WAPK autophosphorylates on serine residue(s). The WAPK gene is predominantly expressed in flowers, moderately in roots, and poorly in leaves. Transcripts were not detected in stems. The WAPK gene was induced by wounding (within 1.5 h), by abscisic acid (within 0.5 h), and by methyl jasmonate (within 2 h). The induction pattern of WAPK mRNA upon wounding was not affected by treatment with diethyldithiocarbamic acid, a reagent which inhibits jasmonic acid biosynthesis. These results suggest that the WAPK gene is regulated by ABA in the wound signal transduction pathway.
    Type of Medium: Electronic Resource
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