scholarly journals -304-BIOCHEMICAL EVALUATION OF INTRACORONARY THROMBOLYSIS BY PLASMA CREATINE PHOSPHOKINASE AND SERUM CARDIAC MYOSIN LIGHT CHAIN

1986 ◽  
Vol 50 (6) ◽  
pp. 549
Author(s):  
Mitsuaki Isobe ◽  
Ryozo Nagai ◽  
Yoshio Yazaki ◽  
Hideaki Nakaoka ◽  
Fumimaro Takaku ◽  
...  
Keyword(s):  
Light Chain ◽  
Myosin Light Chain ◽  
Creatine Phosphokinase ◽  
Cardiac Myosin ◽  
Intracoronary Thrombolysis ◽  
Biochemical Evaluation

scholarly journals Clinical significance of serum cardiac myosin light chain 1 in patients on maintenance hemodialysis.

1993 ◽  
Vol 26 (7) ◽  
pp. 1315-1317
Author(s):  
Arata Uemura ◽  
Hideto Ooishi ◽  
Toshiyuki Akahori ◽  
Jyunnosuke Yamamoto ◽  
Masao Shibata ◽  
...  
Keyword(s):  
Clinical Significance ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Maintenance Hemodialysis ◽  
Cardiac Myosin

Promoter upstream elements of the chicken cardiac myosin light-chain 2-A gene interact with trans-acting regulatory factors for muscle-specific transcription

1989 ◽  
Vol 9 (6) ◽  
pp. 2513-2525
Author(s):  
T Braun ◽  
E Tannich ◽  
G Buschhausen-Denker ◽  
H H Arnold
Keyword(s):  
Light Chain ◽  
Myosin Light Chain ◽  
Mutational Analysis ◽  
Nuclear Proteins ◽  
Chain Gene ◽  
Cardiac Myosin ◽  
Mobility Shift ◽  
Light Chain Gene ◽  
Sequence Elements

A segment of the 5'-flanking region of the chicken cardiac myosin light-chain gene extending from nucleotide -64 to the RNA start site is sufficient to allow muscle-specific transcription. In this paper, we characterize, by mutational analysis, sequence elements which are essential for the promoter activity. Furthermore, we present evidence for a negative-acting element which is possibly involved in conferring the muscle specificity. Nuclear proteins specifically bind to the DNA elements, as demonstrated by gel mobility shift assays and DNase I protection footprinting. The significance of the DNA-protein interactions for the function of the promoter in vivo is demonstrated by competition experiments in which protein-binding oligonucleotides were microinjected into nuclei of myotubes, where they successfully competed for the protein factors which are required to trans activate the MLC2-A promoter. The ability to bind nuclear proteins involves two closely spaced AT-rich sequence elements, one of which constitutes the TATA box. The binding properties correlate well with the capacity to activate transcription in vivo, since mutations in this region of the promoter concomitantly lead to loss of binding and transcriptional activity.

scholarly journals Human cardiac myosin light chain 4 (MYL4) mosaic expression patterns vary by sex

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Tony Y. Wang ◽  
Dan E. Arking ◽  
Joseph J. Maleszewski ◽  
Karen Fox-Talbot ◽  
Tim O. Nieuwenhuis ◽  
...  
Keyword(s):  
Light Chain ◽  
Myosin Light Chain ◽  
Expression Patterns ◽  
Cardiac Myosin ◽  
Mosaic Expression

scholarly journals Expression of cardiac myosin light chain 1 isoforms in human conduction system

1992 ◽  
Vol 58 ◽  
pp. 279
Author(s):  
Kazuteru Fujimoto ◽  
Koichi Nakao ◽  
Michihisa Jougasaki ◽  
Hirofumi Yasue ◽  
Yasumichi Hitoshi ◽  
...  
Keyword(s):  
Light Chain ◽  
Myosin Light Chain ◽  
Conduction System ◽  
Cardiac Myosin

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.

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