Irving R. Hunter

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Laminin is a large (900 kDa) mosaic protein composed of many distinct domains with different structures and functions. Globular and rodlike domains are arranged in an extended four-armed, cruciform shape that is well suited for mediating between distant sites on cells and other components of the extracellular matrix. The alpha-helical coiled-coil domain of(More)
Assembly of laminin isoforms by tripleand double-stranded coiled-coil structures Jurgen Engel,* Irene Hunter,* Therese Schulthess,* Konrad Beck,t Tony W. Dixon,$ and David A. D. Parry$ *Department of Biophysical Chemistry, Biozentrum of the University of Basel, CH-4056 Basel, Switzerland; tlnstitute for Biophysics, University of Linz, A-4040 Linz, Austria(More)
We have previously provided evidence that laminin assembly occurs by the specific interaction of the alpha-helical domains of the A, B1, and B2 chains, located within the long arm of the molecule (Hunter, I., Schulthess, T., Bruch, M., Beck, K., and Engel, J. (1990) Eur. J. Biochem. 188, 205-211). Recent evidence for noncoordinate synthesis of the laminin(More)
The nature of Ig receptors carried by lipopolysaccharide (LPS)-stimulated mouse spleen B cells was analyzed by surface iodination, direct antiserum precipitation and polyacrylamide gel electrophoresis. LPS activation led to a rapid decrease of surface IgD to 20 % and 80 % of the original level on days three and five of culture, respectively. Efficiency of(More)
The multifunctional cytokine tumour necrosis factor-alpha (TNF) displays many physiological effects in a variety of tissues, especially proliferative and cytotoxic actions in immunological cells. Recently, we uncovered an important new mechanism by which TNF can sensitise airway smooth muscle (ASM) to a fixed intracellular Ca2+ concentration which in vivo(More)
The specificity of laminin chain assembly was investigated using fragments E8 and C8-9, derived from the long arm of the molecule, whose rod-like domain consists of the alpha-helical regions of the A, B1 and B2 chains. Urea-induced chain separation and unfolding were monitored by transverse urea/polyacrylamide gel electrophoresis (PAGE) and circular(More)