Role of calcium-dependent proteinase in molt-induced claw muscle atrophy
The claw closer muscle of the Bermuda land crab Gecarcinus lateralis undergoes a sequential atrophy and restoration during each intermolt cycle. Muscle protein decreases 40% during proecdysis and is restored following ecdysis. Amino acid incorporation into protein of postecdysial muscle is five times greater than that in anecdysial muscle. Since the rates of protein synthesis in anecdysial and proecdysial muscle are the same it appears that proecdysial muscle atrophy is caused primarily by an increase in protein degradation. A calcium-dependent proteinase (CDP) active at neutral pH has been implicated in the nonlysosomal hydrolysis of myofibrillar proteins. We have examined the role of a CDP in atrophy of the claw closer muscle. The many similarities between crustacean and vertebrate CDPs have established this crustacean system as a simple and convenient model for the role of Ca/sup 2 +/-dependent proteolysis in myofibrillar protein turnover and its manifestation in the structure of the sarcomere. 16 references, 8 figures. (ACR)
- Research Organization:
- Oak Ridge National Lab., TN (USA)
- DOE Contract Number:
- AC05-84OR21400
- OSTI ID:
- 6408439
- Report Number(s):
- CONF-8405243-1; ON: DE85001275
- Country of Publication:
- United States
- Language:
- English
Similar Records
Ca/sup 2 +/-dependent proteolytic activity in crab claw muscle: effects of inhibitors and specificity for myofibrillar proteins
Molt cycle-associated changes in calcium-dependent proteinase activity that degrades actin and myosin in crustacean muscle
Related Subjects
59 BASIC BIOLOGICAL SCIENCES
ALKALINE EARTH METALS
ANIMALS
AQUATIC ORGANISMS
ARTHROPODS
ATROPHY
CALCIUM
CRABS
CRUSTACEANS
DECAPODS
ELEMENTS
ENZYME ACTIVITY
ENZYMES
HYDROLASES
INVERTEBRATES
METALS
MORPHOLOGICAL CHANGES
MUSCLES
PATHOLOGICAL CHANGES
PEPTIDE HYDROLASES
PHYSIOLOGY
ULTRASTRUCTURAL CHANGES