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. 2001 Dec;7(6):868-71.
doi: 10.3748/wjg.v7.i6.868.

Preliminary research on myosin light chain kinase in rabbit liver

B Ren  1 , H Q Zhu, Z F Luo, Q Zhou, Y Wang, Y Z Wang
Affiliations

Preliminary research on myosin light chain kinase in rabbit liver

B Ren et al. World J Gastroenterol. 2001 Dec.

Abstract

Aim: To study preliminarily the properties of myosin light chain kinase (MLCK) in rabbit liver.

Methods: The expression of MLCK was detected by reverse transcription-polymerase chain reaction(RT-PCR); the MLCK was obtained from rabbit liver, and its activity was analyzed by gamma-(32)P incorporation technique to detect the phosphorylation of myosin light chain.

Results: MLCK was expressed in rabbit liver, and the activity of the enzyme was similar to rabbit smooth muscle MLCK, and calmodulin-dependent. When the concentration was 0.65 mg x L(-1), the activity was at the highest level.

Conclusion: MLCK expressed in rabbit liver may catalyze the phosphorylation of myosin light chain, which may play important roles in the regulation of hepatic cell functions.

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Figures

Figure 1
Figure 1
Reverse transcription polymerase chain reaction of cellular total RNA from hepatocytes in New Zealand rabbit. 1.100 bp DNA ladder; 2-3, PCR products: amplified MLCK DNA fragments.
Figure 2
Figure 2
A: Comparison of enzymatic activity between smMLCK and rabbit liver MLCK (P > 0.05); B: Effect of CaM on MLCK in rabbit liver activity (P < 0.01).
See this image and copyright information in PMC

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