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Biotech / Medical : Biotransplant(BTRN) -- Ignore unavailable to you. Want to Upgrade?

To: Pseudo Biologist who wrote (269)	5/25/1999 8:57:00 PM
From: scaram(o)uche	Respond to of 1475

scramble, scramble, scramble..... window, window, window....... read, read, read....... "never mind". - g - Yes, well, my argument was good, whoever is (if) developing the sucker. - vbg -

To: Pseudo Biologist who wrote (269)	5/25/1999 9:05:00 PM
From: scaram(o)uche	Respond to of 1475

>> do people get paid to come up with these names?? << Yup! And, I usually never learn the trade names, and just go on using their precursors. In this instance, however, it's no excuse for my confusion..... I've always thought, mistakenly, that they were developing an anti-LFA-3. :-(

To: Pseudo Biologist who wrote (269)	5/25/1999 9:25:00 PM
From: scaram(o)uche	Read Replies (1) \| Respond to of 1475

this is the only relevant reference that I can find, but, of course, we are hoping that 507 is reactive with a special epitope.... J Immunol 1992 Apr 1;148(7):2023-9 CD2/LFA-3 ligation induces phospholipase-C gamma 1 tyrosine phosphorylation and regulates CD3 signaling. Kanner SB, Damle NK, Blake J, Aruffo A, Ledbetter JA Bristol-Myers Squibb Pharmaceutical Research Institute, Seattle, WA 98121. Activation of T cells through the TCR/CD3 receptor complex with either specific Ag or antibody results in tyrosine phosphorylation of intracellular protein substrates and phosphatidylinositol-phospholipase C (PLC) signaling, leading to the generation of PI breakdown products and the mobilization of intracellular calcium. Stimulation of the T cell surface receptor CD2 similarly propagates early signals through phosphatidylinositol-PLC activation. Previous reports have shown that CD3 activation leads to tyrosine phosphorylation of the PLC isozyme PLC gamma 1. In this report, we investigated the potential similarity between CD3-induced signaling through PLC gamma 1 and that induced by CD2. We show that stimulation of CD2 receptors on T cells caused tyrosine phosphorylation of PLC gamma 1. Cross-linking of CD2 with CD3 receptors augmented the phosphorylation of PLC gamma 1 on tyrosine, whereas ligation of the CD45 tyrosine phosphatase with CD2 receptors prevented PLC gamma 1 tyrosine phosphorylation. T cells stimulated by ligation of CD2 with its counter-receptor in the form of a soluble LFA-3/Ig fusion protein cross-linked on the cell surface, resulted in a low, but detectable level of PLC gamma 1 phosphorylation with prolonged kinetics, whereas that induced by cross-linking with anti-CD2 was stronger but transient. Co-ligation of LFA-3/Ig with suboptimal concentrations of anti-CD3 resulted in profound augmentation of PLC gamma 1 tyrosine phosphorylation, mobilization of intracellular calcium and T cell proliferation. To explore the relationship between CD3- and CD2-stimulated signaling, T cells were desensitized through 1 h incubation with anti-CD3. CD3 receptor modulation potently down-regulated CD2-induced PLC gamma 1 tyrosine phosphorylation and calcium mobilization. In contrast, PMA or ionomycin treatment did not alter CD2-stimulated tyrosine phosphorylation of PLC gamma 1, suggesting that tyrosine kinase inhibition by CD3 receptor modulation was not caused by signaling events downstream of PLC gamma 1. Taken together, these results support the hypothesis that CD2 provides a potent co-stimulatory signal for CD3-induced T cell activation that is associated with tyrosine kinase(s) and PLC gamma 1.