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EGF receptor kinase suppresses ciliogenesis through activation of USP8 deubiquitinase

Chemokines protect vascular smooth muscle cells from cell death induced by cyclic mechanical stretch.

New photic stimulating system with white light-emitting diodes to elicit electroretinograms from zebrafish larvae.

Potential protective function of the sterol regulatory element binding factor 1-fatty acid desaturase 12 axis in early-stage age-related macular degeneration

Activation of Sterol Regulatory Element Binding Factors by Fenofibrate and Gemfibrozil Stimulates Myelination in Zebrafish

tThe Ca2+-activated protease (Calpain) modulates Ca2+/calmodulin dependent activity of smooth muscle myosin light chain kinase.


Ito M, Tanaka T, Nunoki K, Hidaka H, Suzuki K.
Biochem Biophys Res Commun. 1987 Jun 30;145(3):1321-8.


The Ca2+ -activated neutral protease can proteolyze both Ca2+ -dependent cyclic nucleotide phosphodiesterase and smooth muscle myosin light chain kinase. Ca2+ -dependent cyclic nucleotide phosphodiesterase from rat brain was converted to the Ca2+ -independent active form by Ca2+ -activated protease. The proteolytic effects on myosin light chain kinase of Ca2+-activated protease differed in the presence and absence of the Ca2+-calmodulin (CaM) complex. In the presence of bound CaM, myosin light chain kinase (130k dalton) was degradated to a major fragment of 62 kDa, which had Ca2+/CaM-dependent enzyme and CaM-binding activity. When digestion occurred in the absence of bound CaM, myosin light chain kinase cleaved to a fragment of 60 kDa. This peptide had no enzymatic activity in the presence or absence of the Ca2+-CaM complex. Available evidence suggests that the Ca2+-activated proteases may recognize the conformational change of smooth muscle myosin light chain kinase induced by Ca2+-CaM complex.