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Homodimeric Murine Interleukin-3 Agonists Indicate that Ligand Dimerization is Important for High-Affinity Receptor Complex Formation

 

作者: MütherHorst,   KühlckeKlaus,   GessnerAndré,   AbdallahSaid,   LotherHeinz,  

 

期刊: Growth Factors  (Taylor Available online 1994)
卷期: Volume 10, issue 1  

页码: 17-27

 

ISSN:0897-7194

 

年代: 1994

 

DOI:10.3109/08977199409019600

 

出版商: Taylor&Francis

 

关键词: interleukin-3;dimerization;cystine-bonding;agonists;receptor-recognition

 

数据来源: Taylor

 

摘要:

AbstractHomodimeric murine interleukin 3 (mIL-3) agonists were generated by intermolecular cystine-bonding. Steady-state binding assays and association kinetics performed at 4°C using these agonists revealed specific binding to both the high-and low-affinity receptor. DSS-mediated crosslinking studies performed at 4°C with agonist concentrations compatible with high-affinity receptor complex formation allowed to detect protein complexes of theαchain, theβchain(s) and the high-affinity receptor complex migrating with apparent molecular weights of 90 kDa, 140 kDa, and above 180 kDa, respectively. In contrast, monomeric mIL-3 was crosslinked to theαchain receptor only unless high concentrations were used. Binding studies performed at 4°C revealed a positive cooperative interaction of monomeric mIL-3 with the low-affinity receptor. Proliferation studies and association kinetics performed at 37°C showed that under physiological conditions these agonists were at least 2-to 3-fold more potent than monomeric mIL-3. We therefore propose that dimerization of mIL-3 may be involved in high-affinity receptor complex formation.

 

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