Soluble Calcium Binding Proteins in Vertebrate and Invertebrate Muscles

Gerday, Ch.

doi:10.1007/978-3-642-73042-9_2

Cited by 41 publications

(32 citation statements)

References 66 publications

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“…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). The parvalbumin content is more elevated in high-speed sonic than in white muscle of the oyster toadfish Opsanus tau (Hamoir et al 1980;Appelt et al 1991;Tikunov and Rome 2009).…”

Section: Parvalbuminsmentioning

confidence: 99%

Mechanisms of Fish Sound Production

Fine

Parmentier

2015

Animal Signals and Communication

111

123

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Fishes have evolved multiple mechanisms for sound production, many of which utilize sonic muscles that vibrate the swimbladder or the rubbing of bony elements. Sonic muscles are among the fastest muscles in vertebrates and typically drive the swimbladder to produce one sound cycle per contraction. These muscles may be extrinsic, typically extending from the head to the swimbladder, or intrinsic, likely a more-derived condition, in which muscles attach exclusively to the bladder wall. Recently discovered in Ophidiiform fishes, slow muscles stretch the swimbladder and associated tendons, allowing sound production by rebound (cock and release). In glaucosomatids, fast muscles produce a weak sound followed by a louder one, again produced by rebound, which may reflect an intermediate in the evolution of slow to superfast sonic muscles. Historically, the swimbladder has been modeled as an underwater resonant bubble. We provide evidence for an alternative hypothesis, namely that bladder sounds are driven as a forced rather than a resonant response, thus accounting for broad tuning, rapid damping, and directionality of fish sounds. Cases of sounds that damp slowly, an indication of resonance, are associated with tendons or bones that continue to vibrate and hence drive multiple cycles of swimbladder sound. Stridulation sounds, best studied in catfishes and damselfishes, are produced, respectively, as a series of quick jerks causing rubbing of a ribbed process against a rough surface or rapid jaw closing mediated by a specialized tendon. A cladogram of sonic fishes suggests that fish sound production has arisen independently multiple times.

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Section: Parvalbuminsmentioning

confidence: 99%

Mechanisms of Fish Sound Production

Fine

Parmentier

2015

Animal Signals and Communication

111

123

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“…The slow fiber types of this fish were termed 'yellow' because of the lack of hemoglobin or myoglobin in the animal, and may represent a special case for the role of parvalbumin in slow-twitch muscle. Other work (Gerday, 1982) suggests that fish red muscle does contain parvalbumin of a fiber-type specific form, although Gillis (1985) indicates that red muscle contains only 'trace' amounts of parvalbumin. The differing accounts in the literature as to the role of parvalbumin in slow fish muscle require clarification.…”

Section: +mentioning

confidence: 99%

Parvalbumin correlates with relaxation rate in the swimming muscle of sheepshead and kingfish

Wilwert

Madhoun

Coughlin

2006

Journal of Experimental Biology

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expression of parvalbumin isoforms will differ between the anterior and posterior red muscle, but little longitudinal variation will be observed in parvalbumin expression in white and pink muscle. We successfully employed protein electrophoresis (SDS-PAGE) with western blots to identify two parvalbumin isoforms in each muscle fiber type. SDS-PAGE and densitometry were used to determine the relative expression levels of the two parvalbumin isoforms and total parvalbumin expression. Red muscle displays a significant shift, from anterior to posterior, in the relative expression of the two isoforms, both in their relative contribution and in total parvalbumin content, but white and pink muscle did not. The red muscle of southern kingfish, Menticirrhus americanus (Pisces, F. Scianidae) showed a pattern similar to the red muscle of sheepshead.

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“…They have been extensively studied in various teleost species by means of electrophoretic techniques (Focant et al 1976(Focant et al , 1981Focant 1977, 1985;Johnston et al 1977;Hamoir et al 1980;Huriaux et al 1983Huriaux et al , 1990Rowlerson et al 1985;Scapolo and Rowlerson 1987;Ochiai et al 1988;Gerday 1988;Karasinski and Kilarski 1989;Martinez et al 1989Martinez et al , 1990a. Nevertheless, very poor attention has been given to the differentiation of these proteins during fish ontogeny (Van Raamsdonk et al 1978, 1982Scapolo et al 1988;Martinez et al 1991).…”

Section: Introductionmentioning

confidence: 99%

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

Focant

Huriaux

Vandewalle

et al. 1992

Fish Physiol Biochem

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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.

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Soluble Calcium Binding Proteins in Vertebrate and Invertebrate Muscles

Cited by 41 publications

References 66 publications

Mechanisms of Fish Sound Production

Mechanisms of Fish Sound Production

Parvalbumin correlates with relaxation rate in the swimming muscle of sheepshead and kingfish

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

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