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http://dx.doi.org/10.1007/BF02150806 | DOI Listing |
Neoplasma
February 2007
Institute of Hematology and Blood Transfusion, Prague 12820, Czech Republic.
Bovine seminal ribonuclease (BS RNase), a dimeric homolog of bovine pancreatic ribonuclease (RNase A), is known to display special biological activities namely cytotoxicity for human tumor cells. Because some plant ribonucleases have a similar mass weight and structure as the animal ribonuclease, effects of a commercial product of Mung bean (Phaseolus aureus) nuclease (PhA) were studied on proliferation of ML-2 human tumor cells, as well as it's aspermatogenic, embryotoxic, immunogenic, and immunosuppressive activity, and therapeutic efficiency in athymic mice bearing human melanoma tumor. Concerning the antiproliferative activity, PhA nuclease was almost non-effective in vitro on ML-2 cells and also immunosuppressive activity on human lymphocyte in mixed culture was very low compared to that of BS RNase.
View Article and Find Full Text PDFAnticancer Drugs
August 2006
Laboratory of Genetics, Department of Anthropology, Faculty of Science of the Charles University, Prague, Czech Republic.
The antiproliferative and antitumor effect of wheat leaf ribonuclease was tested in vitro on the human ML-2 cell line and in vivo on athymic nude mice bearing human melanoma tumors. The antiproliferative activity of this plant ribonuclease was negligible in comparison with bovine seminal ribonuclease. In the experiments in vivo, a significant decrease of the tumor size, however, was observed in the mice treated with wheat leaf ribonuclease (27 kDa) compared with the control RNase A and polyethylene glycol.
View Article and Find Full Text PDFAnticancer Drugs
February 2002
Institut für Medizinische Virologie, Klinikum der Johann Wolfgang Goethe-Universität, 60596 Frankfurt am Main, Germany.
Bovine seminal ribonuclease (BS-RNase) is an antitumoral active enzyme exhibiting specific antitumoral action against a number of different cancer cell lines. However, its systemic use is limited by its pharmacokinetic properties and antigenicity. Therefore, it was conjugated to polyethylene glycol (PEG) chains to overcome these problems.
View Article and Find Full Text PDFBiol Reprod
February 1998
Department of Histology and Medical Embryology, La Sapienza University, Rome, Italy.
The distribution of alpha6beta1 integrins at the level of cell-to-cell contacts within the rat seminiferous epithelium was investigated. Double fluorescence experiments using phalloidin staining of actin filaments and anti-integrin subunit antibodies showed that the receptor belongs to the Sertoli cell lateral domains engaged in the characteristic junctional structures known as ectoplasmic specializations (ES), at the level both of inter-Sertoli junctions and of the contacts between Sertoli cells and elongating spermatids. In the seminiferous epithelium of aspermatogenic testes, obtained through X-irradiation in utero (Sertoli-cell-only testes), at the level of inter-Sertoli junctions both ES and alpha6beta1 integrins are present.
View Article and Find Full Text PDFAm J Reprod Immunol
October 1996
Department of Biology, Medical University, Sofia, Bulgaria.
Problem: Sera from infertile patients with elevated reactivity against normozoospermic seminal plasma (NSP) have been selected to investigate human antibody binding to seminal fluid antigens present in abnormal ejaculates.
Method: Sera from 32 idiopathically infertile patients and 44 control sera from fertile individuals were examined by ELISA against: 1) pooled seminal plasma from asthenozoospermic ejaculates (AsthSP), 2) pooled seminal plasma from patients with aspermatogenic azoospermia (AzooSP), and 3) chromatographic fractions from NSP, AsthSP and AzooSP.
Results: Of 32 patients positive for anti-NSP antibodies, only four exhibited increased reactivity to whole AsthSP and/or AzooSP, while 14 recognized antigens of different Mr and various distributions in the corresponding chromatographic fractions.
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