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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Urological research 21 (1993), S. 9-15 
    ISSN: 1434-0879
    Keywords: Dorsal prostate ; Enzyme activity ; Immunohistochemistry ; Mammary gland ; Secretory transglutaminase ; Tissue-type transglutaminase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Transglutaminases with different functions and tissue distribution patterns can be distinguished by specific antibodies and by inhibition of enzyme activity in the presence of guanosine triphosphate (GTP). The most common form is the so-called tissue-type transglutaminase that is apparently involved in membrane, stabilization processes, e.g. during apoptosis, and can be inhibited by incubation with GTP at low calcium concentrations. A secretory transglutaminase that cannot be inhibited by GTP is synthesized in an androgen-dependent manner in the dorsal prostate of the rat, the site suggested to represent the origin of the Dunning tumor used as an experimental model in prostate cancer research. Here we studied the expression of transglutaminases in different Dunning tumor lines — mainly in the highly differentiated H subline - and characterized the enzyme both biochemically and immunocytochemically. A very high enzyme activity was found only in the less well differentiated HI-F tumor line. Immunohistochemical reactions and Western blot analysis showed that there is no secretory transglutaminase present in any of the Dunning tumor lines studied. Transglutaminase activity of the Dunning tumor results from the so-called tissue-type enzyme that is nonorgan specific. The absence of a secretory form of transglutaminase does not suport the contention of a prostatic origin o the Dunning tumor.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1434-0879
    Keywords: Transglutaminases ; Prostate cancer ; Metastasis ; Cellular wound repair
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Using biochemical assays, we compared enzyme activities with the immunoreactivity of antibodies against rat seminal transglutaminase (TGase), human erythrocyte TGase and guinea pig liver TGase in human normal prostate, primary prostatic carcinomas and prostatic carcinoma cell lines. Glandular cells of the epithelium were only exceptionally positive with the antibody against (rat) secretory TGase. Using the antibodies against tissue-type TGase, most immunoreactive cells were found in the basal cell layer of prostatic epithelium as well as in stroma (fibroblasts, endothelial cells), whereas immunoreactive glandular cells were sparse. In the case of benign prostatic hyperplasia, few, irregularly distributed secretory cells along with a small number of stromal cells were also immunoreactive with the tissue-type TGase antibody. In dedifferentiated carcinomas, immunoreactive cells were nearly completely absent. Of the prostate cancer cell lines, the LNCaP line showed neither TGase enzyme activity nor immunoreactivity, whereas the PC-3 cell line displayed significant enzyme activity and immunoreactivity. No hormone-dependent changes in either enzyme activity or immunoreactivity were recorded after in vitro treatment of the respective cell lines with estrogens, androgens and antiandrogens. As there is no correlation between androgen deprivation and TGase expression in nonmalignant and malignant human prostatic epithelial cells, TGase activity more likely indicates cellular lesions and consecutive repair mechanisms.
    Type of Medium: Electronic Resource
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