Myosin, parvalbumin and myofibril expression in barbel (Barbus barbus L.) lateral white muscle during development

Abstract

Histo- and immunohistochemical techniques have recently been used to study the fibre type and myosin expression in fish muscle during development. In the present work, embryonic, larval and adult myosin isozymes (heavy and light chains) and parvalbumin isotypes were analyzed, from fertization to the adult stage, by polyacrylamide gel electrophoresis of barbel (Barbus barbus L.) trunk muscle extracts. The examined myosins display the sequential transitions from embryonic to larval and adult forms characteristic of higher vertebrates. They are characterized by specific heavy chains but their light chains differ only by the LC1/LC3 stoichiometry with LC3 exceeding LC1 after 10 days. Sarcoplasmic parvalbumins show considerable and unforeseen developmental transitions in their isotype distribution: the PA II isotype first appears after hatching and becomes the predominant form until the length reaches about 6 cm. One month after hatching, the amount of PA II then decreases and the synthesis of PA III and IV further increases to reach the typical adult pattern at a size of 18 cm. These observations show that the distribution of parvalbumin isotypes reflects the stage of development. It suggests a specific role for each isotype in relation to muscle activity. Microscopy illustrates the progressive development of somites, muscles cells, and myofibrils, which accelerates at hatching when movements increase.

Mechanisms of Fish Sound Production

“…They are particularly abundant in the white fast-contracting muscles of amphibians and fishes, where they function as a calcium shuttle between the cytoplasm and the SR. Parvalbumin isoforms and myofibrillar proteins differ between fish larvae and adults (Focant et al 1992Crockford and Johnston 1993;Huriaux et al 2003), providing different contractile properties. They are considered responsible for calcium accumulation in the cytoplasm during muscle activity and may promote faster muscle relaxation (Gerday 1982;Klug et al 1988;Appelt et al 1991).…”

Differentiation and growth of muscle in the fish Sparus aurata (L): I. Myosin expression and organization of fibre types in lateral muscle from hatching to adult

“…In fish, the expression of adult isoforms of myosin in slow-red, pink and fast-white muscle is preceded by 'embryonic' and 'larval' isoforms during development (van Raamsdonk et al, 1978;Scapolo et al, 1988;Martinez et al, 1991;Focant et al, 1992;Crockford & Johnston, 1993;Veggetti et al, 1993;Johnston, 1994;Johnston & Horne, 1994). In higher vertebrates primary myotubes all express a slow myosin at an early stage, but in fish the myosin expression of the first fibres to be formed is uncertain.…”

“…In higher vertebrates primary myotubes all express a slow myosin at an early stage, but in fish the myosin expression of the first fibres to be formed is uncertain. Analysis of developmental changes in myosin expression in fish muscle is also complicated by large interspecific variations in the histochemical and immunohistochemical properties of myosin isoforms and in the timing of their developmental transitions (van Raamsdonk et al, 1982;Ramanello et aI., 1987;Scapolo et al, 1988;Focant et al, 1992;Veggetti et al, 1993). Analysis of developmental changes in myosin expression in fish muscle is also complicated by large interspecific variations in the histochemical and immunohistochemical properties of myosin isoforms and in the timing of their developmental transitions (van Raamsdonk et al, 1982;Ramanello et aI., 1987;Scapolo et al, 1988;Focant et al, 1992;Veggetti et al, 1993).…”

Regeneration of skeletal muscle in two teleost fish: Sparus aurata and Brachydanio rerio

“…However, in other fish differences cannot be demonstrated or are evident during some conditions but not in others in the same species (Nathanailides et al 1995;Ennion et al 1995). Some 'developmental' myosin isoforms are expressed during embryonic and larval life in fish (van Raamsdonk et al 1982b;Scapolo et al 1988;Martinez et al 1991;Focant et al 1992;Veggetti et al 1993;Brooks and Johnston 1993;Crockford and Johnston 1993), but they are poorly characterised compared to their higher-vertebrate equivalents. As far as we know, the myosin isoform expression in regenerating fibres in fish muscle has never been described, and the extent to which myosin isoform expression can be used as a marker for myoblast lineage in fish is also unknown.…”