Gene expression analyses of essential catch factors in the smooth and striated adductor muscles of larval, juvenile and adult great scallop (Pecten maximus).
The scallop adductor muscle consists of striated fibres responsible for the fast closure of the shells, and smooth fibres able to maintain tension in a prolonged state of contraction called catch. Formation of the force-bearing catch linkages has been demonstrated to be initiated by dephosphorylation of the key catch-regulating factor twitchin by a calcineurin-like phosphatase, while the involvement of other thick filament proteins is uncertain. Here we report on the development of catchability of the adductor smooth muscle in the great scallop (Pecten maximus) by analysing the spatio-temporal gene expression patterns of the myosin regulatory light chain (MLCr), twitchin, myorod and calcineurin using whole mount in situ hybridization and real-time quantitative PCR. The MLCr signal was identified in the retractor and adductor muscles of the pediveliger larvae, and the juvenile and adult scallop displayed abundant mRNA levels of MLCr in the smooth and striated adductor muscles. Twitchin was mainly expressed in the smooth adductor muscle during metamorphosis, whereas the adult striated adductor muscle contained seven-folds higher twitchin mRNA levels compared to the smooth portion. Calcineurin expression predominated in the gonads and in the smooth adductor, and five-folds higher mRNA levels were measured in the smooth than in the striated fibres at the adult stage. In contrast to the other genes examined, the expression of myorod was confined to the smooth adductor muscle suggesting that myorod plays a permissive role in the molluscan catch muscles, which are first required at the vulnerable settlement stage as a component of the predator defence system.
Andersen
Øivind
Ø
Nofima Marin, As, Norway. oivind.andersen@nofima.no
Torgersen
Jacob S
JS
Pagander
Helene H
HH
Magnesen
Thorolf
T
Johnston
Ian A
IA
D000222:Adaptation, Physiological / Q000502:physiology; D000375:Aging / Q000502:physiology; D000818:Animals; D001522:Behavior, Animal / Q000502:physiology; D029742:Caenorhabditis elegans Proteins / Q000235:genetics; D019703:Calcineurin / Q000235:genetics; D002148:Calmodulin-Binding Proteins / Q000235:genetics; D019143:Evolution, Molecular; D005786:Gene Expression Regulation / Q000502:physiology; D007814:Larva / Q000235:genetics / Q000254:growth & development / Q000378:metabolism; D008675:Metamorphosis, Biological / Q000502:physiology; D009119:Muscle Contraction / Q000502:physiology; D009124:Muscle Proteins / Q000235:genetics*; D009130:Muscle, Smooth / Q000166:cytology / Q000378:metabolism*; D054792:Muscle, Striated / Q000166:cytology / Q000378:metabolism*; D018994:Myosin Light Chains / Q000235:genetics; D038081:Organogenesis / Q000502:physiology; D049897:Pectinidae / Q000235:genetics* / Q000254:growth & development / Q000378:metabolism*; D012333:RNA, Messenger / Q000032:analysis / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013045:Species Specificity; D015854:Up-Regulation / Q000235:genetics
D029742:Caenorhabditis elegans Proteins; D002148:Calmodulin-Binding Proteins; D009124:Muscle Proteins; D018994:Myosin Light Chains; D012333:RNA, Messenger; C489233:unc-22 protein, C elegans; D019703:Calcineurin