Dear John,
unfortunately, I was not able to find your personal email address. The
protein we are talking about is IL-16. It seems not to be important whether
IL-16 was expressed in procaryotic or mammalian cells, as a collegue of mine
has shown by comparing the activation of MAPKs by both proteins. He
expressed IL-16 in E. coli and in the baculovirus system (J Immunol 1998,
160:5874). However, the amounts that have to be taken to see a signal are
tremendously high (up to 15 µg/ml) and are out of any naturally occuring
concentrations.
IL-16 has been shown to be bioactive only in its homotetrameric form (J
Immunol 1982, 128:2563 ff and 2569 ff). So we (and others) think, that this
is the reason why we have to take these loads of IL-16 to see an effect on
our cells. The question now is, how to produce IL-16 in that way that it
folds in a proper way and builds up tetramers? Any suggestions are more than
wellcome.
In the moment I am not convinced that what ever we and others see in our
cells is specific or just caused by unspecific side effects...
Best wishes, Dirk
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Dr. Dirk Seegert
Christian-Albrechts-Universität Kiel
1. Medizinische Klinik, Mucosaimmunologie
Schittenhelmstr. 12
D-24105 Kiel
GERMANY
Tel. +49 (431) 597-1373
Fax +49 (431) 597-1842
http://www.mucosa.de
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