Androgen receptor (AR) plays a key role in cell growth both in the normal prostate and in prostate cancer. Androgen ablation and prolonged antiandrogen therapy can give rise to AR-dependent prostate tumors, which nonetheless can grow in the androgen-deprived milieu. Here we describe the ribozyme approach to selectively degrading the AR mRNA and thereby inhibiting AR function.
View Article and Find Full Text PDFArch Immunol Ther Exp (Warsz)
May 1998
The effect of human lactoferrin on the human lymphoblastic T cell line (Jurkat) was tested with regard to proliferation and differentiation. Lactoferrin enhanced cell proliferation in a serum-reduced (1% fetal calf serum) culture. The stimulatory effect of lactoferrin on proliferation depended on the degree of iron saturation but the amplitude of the effect was low, similar to that obtained in the presence of serum transferrin.
View Article and Find Full Text PDFBinding of either iron-saturated or iron-free lactoferrin to the Jurkat human lymphoblastic T-cell line was saturable with a dissociation constant Kd of 40 nM. The total number of binding sites was estimated to be approximately 300,000. Non-specific binding did not exceed 30% of the total binding.
View Article and Find Full Text PDFMonoclonal antibodies have been raised against the soluble lactotransferrin binding protein purified from the cell culture supernatant of Jurkat cell line, a human T-lymphoblastic cell. All monoclonal antibodies were able to specifically bind to the membrane of Jurkat cells. One of the monoclonal antibodies, DP5B3G10, recognized both the soluble lactotransferrin-binding protein and the membrane lymphocyte lactotransferrin receptor after SDS-PAGE in presence of 2-mercaptoethanol and electrotransfer on nitrocellulose.
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