Interleukin-1 biotechnology

IL-1 continues to be a focus of clinical investigation. This stems from its observed  

Most of these effects are most likely mediated not only directly by IL-1, but also by various additional cytokines (including IL-2) induced by IL-1 administration. 

The observed effects prompted initiation of clinical trials assessing IL-l s efficacy in treating  

IL-1 thus displays toxic effects comparable to administration of TNF (see later), or high levels of IL-2. However, several clinical studies are still underway, and this cytokine may yet prove therapeutically useful, either on its own or, more likely, when administered at lower doses with additional therapeutic agents. 

Because of its role in mediating acute/chronic inflammation, (downward) modulation of IL-1 levels may prove effective in ameliorating the clinical severity of these conditions. Again, several approaches may prove useful in this regard, including administration of  

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Goodson, R. J., and Katre, N.V. Site-directed PEGylation of recombinant interleukin-2 at its glycosylation site. Biotechnology 8(4) 343-346. 1990. 

Biotechnology-derived products may be classified into monoclonal antibodies, gene therapy, vaccines, enzymes, and interleukins. The current major therapeutic areas for these substances are cancer or cancer-related conditions, AIDS or HIV-related disease, diabetes, human growth hormone, myocardial infarction, and inflammatory disease. 

N.L. Jeon, H. Baskaran, S.K.W. Dertinger, G.M. Whitesides, L. Van de Water and M. Toner, Neutrophil chemotaxis in hnear and complex gradients of interleukin-8 formed in a microfabricated device. Nature Biotechnology, 20(8), 826-830 (2002). 

Proteins that contain disulfide bonds often fold slowly in vitro because the oxidation and coixect pairing of the cysteine residues becomes the rate-limiting step and the bonds formed ai e not always the coiiect ones. Many proteins, especially those that are secreted by eu-kaiyotes, aie stabilized by disulfide bonds. Examples of such proteins include those used for medical or biotechnological puiposes, such as interleukins, IFNs, antibodies and then fragments, insulin, TGF, and many toxins and proteases. Expression of recombinant proteins as inclusion bodies in bacteria can be a very efficient way to produce cloned proteins, as long as the inclusion body protein can be successfully refolded. 

Tami J. Interleukins and interferons. In Crommelin, DJA, Sindelar RD eds. Pharmaceutical Biotechnology An Introduction for Pharmacists and Pharmaceutical Scientists. Amsterdam Harwood Academic Publishers, 1997 215-227. 

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