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ABCG5/G8 Crystallization in a Lipidic Bicelle Environment for X-Ray Crystallography
Published on: August 25, 2023
Alpha B-crystallin in skeletal muscle: purification and localization
Y Atomi1, S Yamada, R Strohman
1Department of Sports Sciences, College of Arts & Sciences, University of Tokyo.
Journal of Biochemistry
|November 1, 1991
Summary
Hindlimb suspension causes atrophy in rat soleus muscles, reducing a soluble 22-kDa protein. This protein was identified as alpha B-crystallin, a myofibril-stabilizing protein in slow skeletal muscle.
Area of Science:
- Muscle Atrophy Research
- Skeletal Muscle Physiology
- Protein Biochemistry
Background:
- Hindlimb suspension is a model for muscle atrophy.
- A specific soluble 22-kDa protein decreases early in soleus muscle atrophy.
Purpose of the Study:
- Identify the 22-kDa protein.
- Investigate its role in skeletal muscle, particularly during atrophy.
Main Methods:
- Protein purification using chromatography.
- Partial amino acid sequencing and HPLC analysis.
- Immunoblotting with polyclonal antibodies.
- Immunocytochemical localization in myofibrils.
Main Results:
- The 22-kDa muscle protein shares sequence identity with rat lens alpha B-crystallin.
- Antibodies to alpha B-crystallin recognized the muscle protein.
- Alpha B-crystallin is expressed in slow skeletal muscle and localized to Z-bands.
- Its levels decrease in atrophied soleus muscle.
Conclusions:
- The 22-kDa protein decreased during hindlimb suspension is alpha B-crystallin.
- Alpha B-crystallin is a myofibril-stabilizing protein in slow skeletal muscle.
