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Books > Science & Mathematics > Biology, life sciences > Biochemistry > Proteins
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Calcium Binding Proteins in Normal and Transformed Cells (Paperback, Softcover reprint of the original 1st ed. 1990)
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Calcium Binding Proteins in Normal and Transformed Cells (Paperback, Softcover reprint of the original 1st ed. 1990)
Series: Advances in Experimental Medicine and Biology, 269
Expected to ship within 10 - 15 working days
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The First European Symposium on Calcium-Binding Proteins in Normal
and Transformed Cells was held at the Faculty of Medicine of the
"Universit6 Libre de Bruxelles" in Brussels, Belgium, April 20-22,
1989. Delegates from seventeen countries attended. This Symposium
was initiated through an EEC Stimulation Program. The formal
program included forty verbal presentations by invited speakers and
sixty miniposter presentations, and was formulated by the
Organizing and Scientific Committee: E. Carmeliet (Leuven), J. P.
Collin (Poitiers), S. Forsen (Lund), C. W. Heizmann (Ziirich), D.
E. M. Lawson (Cambridge), P. Miroir (Brussels), J. L. Pasteels
(Brussels) and R. Pochet (Brussels). This volume contains the
papers prepared by the invited speakers. The contributions are
grouped according to their general subject matter: Genes of
Calcium-Binding Protein Family, Structure/Function Relationships,
The Cytoskeleton and Calcium-Binding Proteins, Calcium-Binding
Proteins in TransforlIled Cells, Calcium/Lipid-Binding Proteins,
Calcium-Binding Proteins Substrates and Immunohistochemistry of
Calbindin and Calretinin. The highlights of the symposium are
numerous. Among the items to be noted are the growing number of
abundant proteins which interact with calcium and sometimes with
other second messenger sys- tems; specifically pH associated with
the tyrosine kinase calpactin, calcYclin, p9Ka induced by growth
fac- tors, MRP-8 and MRP-14 (also called cystic fibrosis antigen,
L1 or calgranulins) forming half the soluble protein of
granulocytes. New structure/function relationships on calbindin D9K
and calmodulin have emerged from nuclear magnetic resonance and
site-directed mutagenesis studies.
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