scholarly journals Rabbit skeletal muscle calcium-dependent protease requiring millimolar CA2+. Purification, subunit structure, and Ca2+-dependent autoproteolysis.

1982 ◽  
Vol 257 (12) ◽  
pp. 7203-7209 ◽  
Author(s):  
R L Mellgren ◽  
A Repetti ◽  
T C Muck ◽  
J Easly
Keyword(s):  
Skeletal Muscle ◽  
Rabbit Skeletal Muscle ◽  
Subunit Structure ◽  
Calcium Dependent ◽  
Muscle Calcium

Subunit structure of rabbit skeletal muscle phosphorylase kinase

Biochemistry ◽  
1973 ◽  
Vol 12 (4) ◽  
pp. 574-580 ◽  
Author(s):  
Taro Hayakawa ◽  
John P. Perkins ◽  
Edwin G. Krebs
Keyword(s):  
Skeletal Muscle ◽  
Rabbit Skeletal Muscle ◽  
Phosphorylase Kinase ◽  
Subunit Structure ◽  
Muscle Phosphorylase

scholarly journals N2A Titin: Signaling Hub and Mechanical Switch in Skeletal Muscle

2020 ◽  
Vol 21 (11) ◽  
pp. 3974 ◽  
Author(s):  
Kiisa Nishikawa ◽  
Stan L. Lindstedt ◽  
Anthony Hessel ◽  
Dhruv Mishra
Keyword(s):  
Skeletal Muscle ◽  
Muscle Mechanics ◽  
Active Muscle ◽  
Small Deletion ◽  
Calcium Dependent ◽  
Hypertrophic Signaling ◽  
Pevk Region ◽  
Mechanical Switch ◽  
The Impact ◽  
Muscle Calcium

Since its belated discovery, our understanding of the giant protein titin has grown exponentially from its humble beginning as a sarcomeric scaffold to recent recognition of its critical mechanical and signaling functions in active muscle. One uniquely useful model to unravel titin’s functions, muscular dystrophy with myositis (mdm), arose spontaneously in mice as a transposon-like LINE repeat insertion that results in a small deletion in the N2A region of titin. This small deletion profoundly affects hypertrophic signaling and muscle mechanics, thereby providing insights into the function of this specific region and the consequences of its dysfunction. The impact of this mutation is profound, affecting diverse aspects of the phenotype including muscle mechanics, developmental hypertrophy, and thermoregulation. In this review, we explore accumulating evidence that points to the N2A region of titin as a dynamic “switch” that is critical for both mechanical and signaling functions in skeletal muscle. Calcium-dependent binding of N2A titin to actin filaments triggers a cascade of changes in titin that affect mechanical properties such as elastic energy storage and return, as well as hypertrophic signaling. The mdm phenotype also points to the existence of as yet unidentified signaling pathways for muscle hypertrophy and thermoregulation, likely involving titin’s PEVK region as well as the N2A signalosome.

scholarly journals Effects of storage on activity and subunit structure of rabbit skeletal-muscle AMP deaminase

1980 ◽  
Vol 189 (2) ◽  
pp. 367-368 ◽  
Author(s):  
M Ranieri-Raggi ◽  
A Raggi
Keyword(s):  
Skeletal Muscle ◽  
Rabbit Skeletal Muscle ◽  
Subunit Structure ◽  
Amp Deaminase

On storage, AMP deaminase is converted into a form exhibiting hyperbolic kinetics even at low KCl concentration. This effect results from cleavage of the enzyme subunit (mol.wt. 79 000) to a product of similar size to the component of approx. mol.wt. 70 000 present in trace amounts in AMP deaminase just prepared from fresh muscle.

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