NDLI: Signaling pathways underlying eosinophil cell motility revealed by using caged peptides

Content Provider	PubMed Central
Author	Walker, Jeffery W. Gilbert, Susan H. Drummond, Robert M. Yamada, Misato Sreekumar, R. Carraway, Robert E. Ikebe, Mitsuo Fay, Fredric S.
Copyright Year	1998
Abstract	Insights into structure-function relations of many proteins opens the possibility of engineering peptides to selectively interfere with a protein’s activity. To facilitate the use of peptides as probes of cellular processes, we have developed caged peptides whose influence on specific proteins can be suddenly and uniformly changed by near-UV light. Two peptides are described which, on photolysis of a caging moiety, block the action of calcium-calmodulin or myosin light chain kinase (MLCK). The efficacy of theses peptides is demonstrated in vitro and in vivo by determining their effect before and after photolysis on activities of isolated enzymes and cellular functions known to depend on calcium-calmodulin and MLCK. These caged peptides each were injected into motile, polarized eosinophils, and when exposed to light promptly blocked cell locomotion in a similar manner. The results indicate that the action of calcium-calmodulin and MLCK, and by inference myosin II, are required for the ameboid locomotion of these cells. This methodology provides a powerful means for assessing the role of these and other proteins in a wide range of spatio-temporally complex functions in intact living cells.
Starting Page	1568
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	4
Volume Number	95
Language	English
Publisher	The National Academy of Sciences
Publisher Date	1998-02-17
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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