Publication List English

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

Downregulation of GSTK1 Is a Common Mechanism Underlying Hypertrophic Cardiomyopathy

Comparative Transcriptome Analysis Identifies CCDC80 as a Novel Gene Associated with Pulmonary Arterial Hypertension

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.