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  • 1
    Electronic Resource
    Electronic Resource
    Effects of kainic acid lesioning on poly(ADP-ribose) polymerase (PARP) activity in the rat striatum in vivo (2000)
    Springer
    Amino acids 19 (2000), S. 229-237 
    Details
    ISSN: 1438-2199
    Keywords: Keywords: Amino acids ; Kainic acid ; Neurodegeneration ; Excitotoxicity ; Poly(ADP-ribose) polymerase ; PARP ; In vivo
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary. Poly(ADP-ribose) polymerase (PARP) is activated in glutamate-induced toxicity of neurons in culture (Cosi et al., 1994). Since injection of the excitatory amino acid, kainic acid (KA) into the rat striatum induces a delayed neuronal death, the effects of this in vivo excitotoxin lesioning procedure on striatal PARP activity was investigated. PARP activity was measured in striatal extracts both in the absence ("endogenous" activity) and presence ("total" activity) of exogenously-added fragmented DNA. KA (5 nmols/1 μl) produced significant and time-dependent changes in striatal PARP activity, compared to saline-injected control animals: no changes at 6 h after intrastriatal KA, a 68% and 48% decrease in endogenous and total PARP activity respectively at 12 h, a doubling in endogenous PARP activity at 24 h, and a 382% and 60% increase in endogenous and total activities at 1 week after KA. PARP cleavage was not detected at any time point. These results suggest a participation of PARP in KA-induced toxicity in the brain in vivo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007260070054
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  • 2
    Electronic Resource
    Electronic Resource
    Organ-specific expression of the intestinal epithelium-related antigen A33, a cell surface target for antibody-based imaging and treatment in gastrointestinal cancer (2000)
    Springer
    Cancer chemotherapy and pharmacology 46 (2000), S. S27 
    Details
    ISSN: 1432-0843
    Keywords: Key words Monoclonal antibody ; A33 ; Gastric cancer ; Immunohistochemistry ; Tumor targeting
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Murine monoclonal antibody A33 (mA33) was developed by the Memorial Sloan-Kettering Cancer Center and by the New York Branch of the Ludwig Institute for Cancer Research. It is an immunoglobulin (Ig)G2a antibody that detects a protease- and neuraminidase-resistant, periodate-sensitive epitope. Serological analysis of the antigen showed that it is expressed in a few colorectal cancer cell lines and a pancreatic cancer cell line, but is basically not reactive with other types of cell line. Normal fibroblasts and normal kidney cell lines reacted negatively to mA33. Immunohistochemical study of normal tissues identified the large and small intestinal mucosa as the principal site of A33 expression. Tests in tumor samples demonstrated that only tumors of the gastrointestinal tract are consistently A33 positive. A33 is found in 95% of primary and metastatic colorectal cancers, with uniform expression throughout the tumors in most cases. A33 is also detected in 63% of gastric cancers, with uniform expression in 45% of cases. Eighty-three percent of intestinal-type gastric cancers were positive for A33, and about 50% of the diffuse-type and mucinous cancers were mA33 positive. A33 was expressed in 50% of the pancreatic cancers but with marked heterogeneity. Other epithelial cancers, sarcomas, neuroectodermal tumors, and lymphoid neoplasms were generally A33 negative. A33 is the first example of a constitutively expressed, organ-specific epithelial membrane antigen permitting highly specific tumor targeting in patients with gastrointestinal cancer. Encouraged by the success of the biodistribution and imaging characteristic studies performed at Memorial Sloan-Kettering Cancer Center by the New York Branch of the Ludwig Institute in colorectal cancers, a new clinical study of humanized monoclonal antibody huA33 against A33 antigen-positive gastric cancers has been initiated in Japan.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00014045
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  • 3
    Electronic Resource
    Electronic Resource
    A short peptide derived from the antisense homology box of Fas ligand induces apoptosis in anti-Fas antibody-insensitive human ovarian cancer cells (2000)
    Springer
    Apoptosis 5 (2000), S. 37-41 
    Details
    ISSN: 1573-675X
    Keywords: Anti-Fas antibody ; antisense homology box-derived peptide ; apoptosis ; Fas ligand ; ovarian cancer.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract We found that a short synthetic peptide corresponding to the “antisense homology box” of Fas ligand induced apoptotic cell death of Fas-expressing human ovarian cancer cell lines. The peptide was deduced from residues 256–265 of human Fas ligand, based on the hypothesis that it should contain a specific binding site to the corresponding Fas. Interestingly, the ovarian cancer cell line NOS4, which was sensitive to anti-Fas antibody induced apoptosis, was not affected by the peptide, whereas another cell line, SKOV-3, which was insensitive to anti-Fas antibody, was killed by the peptide. Thus, this short peptide was shown to have a unique activity to induce apoptosis in human ovarian cancer cells in a manner different from anti-Fas antibody.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009633525205
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    Paper (German National Licenses)
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