Myosin Light Chain Kinase / Actin Interaction in Phorbol Dibutyrate-Stimulated Smooth Muscle Cells
Abstract.: Previous work has suggested that in addition to its kinase activity, myosin light chain kinase (MLCK) exhibits non-kinase properties within its N-terminus that could influence cytoskeletal organization of smooth muscle cells (A. Nakamura et al. Biochem Biophys Res Commun. 2008;369:135-143...
Saved in:
| Main Authors: | , , , , , , , , , , , , , , |
|---|---|
| Format: | Book |
| Published: |
Elsevier,
2011-01-01T00:00:00Z.
|
| Subjects: | |
| Online Access: | Connect to this object online. |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
MARC
| LEADER | 00000 am a22000003u 4500 | ||
|---|---|---|---|
| 001 | doaj_3e9da05155d74a178f41b97c8c271147 | ||
| 042 | |a dc | ||
| 100 | 1 | 0 | |a Sean E. Thatcher |e author |
| 700 | 1 | 0 | |a Mike E. Fultz |e author |
| 700 | 1 | 0 | |a Hideyuki Tanaka |e author |
| 700 | 1 | 0 | |a Haruo Hagiwara |e author |
| 700 | 1 | 0 | |a Hou-Li Zhang |e author |
| 700 | 1 | 0 | |a Ying Zhang |e author |
| 700 | 1 | 0 | |a Kohichi Hayakawa |e author |
| 700 | 1 | 0 | |a Shinji Yoshiyama |e author |
| 700 | 1 | 0 | |a Akio Nakamura |e author |
| 700 | 1 | 0 | |a Hong Hui Wang |e author |
| 700 | 1 | 0 | |a Takeshi Katayama |e author |
| 700 | 1 | 0 | |a Masaru Watanabe |e author |
| 700 | 1 | 0 | |a Yuan Lin |e author |
| 700 | 1 | 0 | |a Gary L. Wright |e author |
| 700 | 1 | 0 | |a Kazuhiro Kohama |e author |
| 245 | 0 | 0 | |a Myosin Light Chain Kinase / Actin Interaction in Phorbol Dibutyrate-Stimulated Smooth Muscle Cells |
| 260 | |b Elsevier, |c 2011-01-01T00:00:00Z. | ||
| 500 | |a 1347-8613 | ||
| 500 | |a 10.1254/jphs.10296FP | ||
| 520 | |a Abstract.: Previous work has suggested that in addition to its kinase activity, myosin light chain kinase (MLCK) exhibits non-kinase properties within its N-terminus that could influence cytoskeletal organization of smooth muscle cells (A. Nakamura et al. Biochem Biophys Res Commun. 2008;369:135-143). Myosin ATPase activity measurements indicate that the 26 - 41 peptide of MLCK significantly decreases ATPase activity as the concentration of this peptide increases. Sliding velocity of actin-filaments on myosin and stress responses in skinned smooth muscle tissue are also inhibited. Peptide-mediated uptake and the microinjection technique in cells indicate that the peptide was necessary for actin-filament stabilization. Fluorescence resonance energy transfer analysis indicated that in the presence of MLCK, α-actin but not β-actin remodeled during phorbol 12,13-dibutyrate (PDBu)-induced contractions. PDBu also induced podosomes in the cell. When MLCK expression was down-regulated by introduction of RNAi for MLCK by lentivirus vector into the cells, we failed to observe the podosome induction upon PDBu stimulation. Rescue experiments indicate that the non-kinase activity of MLCK plays an important role in maintaining actin stress fibers and in the PDBu-induced reorganization of actin-filaments in smooth muscle cells. Keywords:: actin-remodeling, podosome, phorbol 12,13-dibutyrate (PDBu), FRET analysis, myosin light chain kinase (MLCK)-deficient cell | ||
| 546 | |a EN | ||
| 690 | |a Therapeutics. Pharmacology | ||
| 690 | |a RM1-950 | ||
| 655 | 7 | |a article |2 local | |
| 786 | 0 | |n Journal of Pharmacological Sciences, Vol 116, Iss 1, Pp 116-127 (2011) | |
| 787 | 0 | |n http://www.sciencedirect.com/science/article/pii/S1347861319307285 | |
| 787 | 0 | |n https://doaj.org/toc/1347-8613 | |
| 856 | 4 | 1 | |u https://doaj.org/article/3e9da05155d74a178f41b97c8c271147 |z Connect to this object online. |