scholarly journals Novel monoclonal antibodies specific for human cardiac myosin light-chain 1: useful tools for analysis of normal and pathological hearts.

1993 ◽  
Vol 41 (1) ◽  
pp. 35-42 ◽  
Author(s):  
K Fujimoto ◽  
H Yasue ◽  
K Nakao ◽  
H Yamamoto ◽  
Y Hitoshi ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Monoclonal Antibodies ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Normal Adult ◽  
Human Tissues ◽  
Cardiac Myosin ◽  
Adult Type ◽  
Adult Human ◽  
Slow Type

To investigate the developmental, physiological and pathophysiological roles of human cardiac myosin light-chain 1 (LC1s), we developed two novel monoclonal antibodies (KA1 and KB1) against human cardiac LC1s and examined LC1s in normal and pathological hearts immunohistochemically. KA1 and KB1 were specific only for atrial LC1 (ALC1) and for both ALC1 and ventricular LC1 (VLC1), respectively, in human hearts. Among human tissues tested, including skeletal muscle, vascular smooth muscle, and liver, KA1 did not crossreact with proteins in any other tissues than atria, whereas KB1 crossreacted with the slow-type LC1 of skeletal muscle. Among adult mammalian hearts of several other species including pig, dog, hamster, and rat, KA1 and KB1 crossreacted only with ALC1 and with both ALC1 and VLC1, respectively. ALC1 was strongly and uniformly observed in human fetal atria and ventricles and in normal adult human atria, but sporadically in normal adult human ventricles. In the overloaded ventricle (dilated cardiomyopathy), ALC1 was highly augmented but not uniform. These results suggest that the fetal VLC1 is immunohistochemically identical to the adult type of ALC1 and that ALC1 is expressed homogeneously in human fetal ventricles and sporadically in normal adult ventricles, and is re-expressed heterogeneously and in an increased amount in the overloaded ventricle.

Clinical assessment of specific enzyme immunoassay for the human cardiac myosin light chain II (MLC II) with use of monoclonal antibodies

1990 ◽  
Vol 23 (6) ◽  
pp. 515-522 ◽  
Author(s):  
Atsushi Hirayama ◽  
Masaru Arita ◽  
Yutaka Takagaki ◽  
Akio Tsuji ◽  
Kazuhisa Kodama ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Enzyme Immunoassay ◽  
Light Chain ◽  
Clinical Assessment ◽  
Myosin Light Chain ◽  
Cardiac Myosin ◽  
Specific Enzyme

scholarly journals Novel Monoclonal Antibodies Specific for Human Cardiac Myosin Light Chain 1 ; Useful Tools for Analyses of Myosin Light Chains.

1991 ◽  
Vol 55 ◽  
pp. 406
Author(s):  
Kazuteru Fujimoto ◽  
Koichi Nakao ◽  
Hirofumi Yasue ◽  
Yasumichi Hitoshi ◽  
Kiyoshi Takatsu ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Light Chains ◽  
Myosin Light Chains ◽  
Cardiac Myosin

scholarly journals Smooth muscle myosin light chain kinase expression in cardiac and skeletal muscle

2000 ◽  
Vol 279 (5) ◽  
pp. C1656-C1664 ◽  
Author(s):  
B. Paul Herring ◽  
Shelley Dixon ◽  
Patricia J. Gallagher
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Cardiac Myocyte ◽  
Cardiac Tissue ◽  
Specific Protein ◽  
Myoblast Differentiation ◽  
Adult Skeletal Muscle

The purpose of this study was to characterize myosin light chain kinase (MLCK) expression in cardiac and skeletal muscle. The only classic MLCK detected in cardiac tissue, purified cardiac myocytes, and in a cardiac myocyte cell line (AT1) was identical to the 130-kDa smooth muscle MLCK (smMLCK). A complex pattern of MLCK expression was observed during differentiation of skeletal muscle in which the 220-kDa-long or “nonmuscle” form of MLCK is expressed in undifferentiated myoblasts. Subsequently, during myoblast differentiation, expression of the 220-kDa MLCK declines and expression of this form is replaced by the 130-kDa smMLCK and a skeletal muscle-specific isoform, skMLCK in adult skeletal muscle. These results demonstrate that the skMLCK is the only tissue-specific MLCK, being expressed in adult skeletal muscle but not in cardiac, smooth, or nonmuscle tissues. In contrast, the 130-kDa smMLCK is ubiquitous in all adult tissues, including skeletal and cardiac muscle, demonstrating that, although the 130-kDa smMLCK is expressed at highest levels in smooth muscle tissues, it is not a smooth muscle-specific protein.

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