Cholinesterase Activity and Inherited Muscular Dystrophy of the Chicken

Wilson, Barry W.; Montgomery, Madison; Asmundson, R. V.

doi:10.3181/00379727-129-33283

Cited by 30 publications

(6 citation statements)

References 9 publications

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“…In early development (3-day chick embryo), the isoenzyme of lower molecular weight, ach-I, was predominant. Electrophoresis of skeletal muscle homogenates from IS-day embryos produced three zones of activity while in adult muscle, the isoenzymes of higher molecular weight, ach-2 and ach-3, are present but in much lower concentrations (Maynard, 1966;Wilson et al, 1969). Similar changes were observed in the isoenzyrnes of the developing chick brain (Maynard, 1966).…”

Section: I 2)mentioning

confidence: 55%

“…I .7) Acetylcholinesterase (ach) has been shown to exist as three electrophoretically distinct isoenzymes in vertebrate brain and muscle tissue Maynard, 1966;Wilson, Montgomery & Asmundson, 1969). The forms apparently do not differ significantly in nett surface charge but have differing molecular weights of approximately 220,000 (ach-I), 300,000 (ach-a) and 420,000 (ach-3) (Wilson, Montgomery & Asmundson, 1969). This suggests that the isoenzymes are explicable in terms of aggregation phenomena (Grafuis & Millar, 1965).…”

Section: I 2)mentioning

confidence: 99%

“…Ontogenetic studies on acetylcholinesterase have shown that large changes in activity (Nachmansohn, 1939), localization (Mumenthaler & Engel, 1961 ;Filogamo & Gebella, 1967;Wilson et al, 1969) and isoenzyme pattern (Maynard, 1966;Wilson et al, 1969) occur during tissue development. In muscles of the chicken, acetylcholinesterase activity decreases rapidly within 2 weeks after hatching of normal birds but retains its high level in those homozygous for inherited muscular dystrophy Wilson, Mettler & Asmundson, 1970).…”

Section: I 2)mentioning

confidence: 99%

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Isoenzymes and Ontogeny

Masters

Holmes

1972

Biological Reviews

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Summary 1. In this review, representative data on the nature of enzyme multiplicity and the developmental progressions of multiple enzyme forms have been collected, and the significance of this material has been discussed in relation to gene involvement during tissue differentiation. 2. In addition, emphasis has been directed towards the relevance of this onto‐genetic information to a wide variety of biological phenomena, such as the possibilities of metabolic advantage conferred by the distinctive properties and physiological locations of these multiple enzyme forms, the insight into the subunit structure and compositional interrelationships of proteins, the aetiology of disease states, the relationship to hormone action, the extra nuclear specification of enzymes, and the transformations between particulate and soluble enzymes. 3. Three isoenzyme systems in particular have been chosen for the special development of these themes and treated in some detail; lactate dehydrogenase (LDH), aldolase and the esterases. Briefer accounts of the ontogeny of other less‐studied series of multiple enzyme forms have also been included. 4. In relation to LDH, the major findings and conclusions of the pioneering investigators have been outlined, together with the reassessments which have been necessitated by recent studies of LDH ontogeny. It is evident, for example, that the early embryonic form of this enzyme is not necessarily parental as previously thought, and the realization appears to possess wide‐ranging implications in regard to the control of synthesis of the enzymes. An indirect role of oxygen in LDH biosynthesis is indicated together with the independent regulation of the separate genes. 5. Recent developments in the enzymology of preimplantation ova have been discussed. It is noteworthy that the extraordinary levels of LDH activity which have been reported to be associated with these early developmental stages, may arise by extracellular adsorption rather than by an intrinsic synthesis of enzyme. Hence contemporary interest in this area has shifted towards a comprehension of the biochemical significance of the extremely unusual, selective concentrations of extracellular lactate dehydrogenase in the oviduct, the relation of this enzyme to the specialized growth requirements of the ova, and the influences of reproductive hormones on these oviducal isoenzymes. 6. The role of aldolase ontogeny as well as the composition, gene control, and native state of these lysases is also reviewed. This enzyme provides a particular example of the manner in which tissue modification of the catalytic and structural properties of enzymes may influence interpretations of the native state of purified proteins, and in this case, also, the observable microheterogeneity satisfies previous disquietude in regard to the existence of different subunits in the muscle enzyme. 7. The basic developmental importance of aldolase‐C is stressed by the occurrence of this form of the enzyme in the early embryos of many different species. Furthermore, a ...

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Section: I 2)mentioning

confidence: 55%

Section: I 2)mentioning

confidence: 99%

Section: I 2)mentioning

confidence: 99%

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Isoenzymes and Ontogeny

Masters

Holmes

1972

Biological Reviews

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“…Sarcoplasmic AChE is maximal around the sites of motor endplates and declines in a regular fashion to either side. It is, however, present throughout the length of fibers in dystrophic biceps muscles [43][44][45].…”

Section: Are Dystrophic αR Fibers Akin To Embryonic or Denervated?mentioning

confidence: 99%

Caveolin-3: A Causative Process of Chicken Muscular Dystrophy

Kikuchi

2020

Biomolecules

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The etiology of chicken muscular dystrophy is the synthesis of aberrant WW domain containing E3 ubiquitin-protein ligase 1 (WWP1) protein made by a missense mutation of WWP1 gene. The β-dystroglycan that confers stability to sarcolemma was identified as a substrate of WWP protein, which induces the next molecular collapse. The aberrant WWP1 increases the ubiquitin ligase-mediated ubiquitination following severe degradation of sarcolemmal and cytoplasmic β-dystroglycan, and an erased β-dystroglycan in dystrophic αW fibers will lead to molecular imperfection of the dystrophin-glycoprotein complex (DGC). The DGC is a core protein of costamere that is an essential part of force transduction and protects the muscle fibers from contraction-induced damage. Caveolin-3 (Cav-3) and dystrophin bind competitively to the same site of β-dystroglycan, and excessive Cav-3 on sarcolemma will block the interaction of dystrophin with β-dystroglycan, which is another reason for the disruption of the DGC. It is known that fast-twitch glycolytic fibers are more sensitive and vulnerable to contraction-induced small tears than slow-twitch oxidative fibers under a variety of diseased conditions. Accordingly, the fast glycolytic αW fibers must be easy with rapid damage of sarcolemma corruption seen in chicken muscular dystrophy, but the slow oxidative fibers are able to escape from these damages.

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“…overproduced in the affected fast-twitch muscles (Wilson et al, 1968), and this enzyme becomes significantly elevated in the plasma of these chickens. Wilson et al (1973a) first reported this latter phenomenon for dystrophic chickens at 5 , 12, and 14 weeks of age, noting that the plasma contained four-to fivefold the normal concentration of AChE.…”

mentioning

confidence: 95%

Changes in the Levels and Forms of Cholinesterases in the Blood Plasma of Normal and Dystrophic Chickens

Lyles

Barnard

Silman

1980

Journal of Neurochemistry

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Acetylcholinesterase (AChE) and pseudocholinesterase (°ChE) were analysed in the blood plasma of developing chickens, both normal and those with inherited muscular dystrophy. The amounts and the molecular forms of each were examined. °ChE concentration rises in the plasma of normal and dystrophic chicks at the end of embryonic development and is maintained after hatching at a constant, relatively high level, accounting for 90‐95% of total cholinesterase activity in normal plasma. This level is maintained in normal and dystrophic chickens. In embryonic plasma of both normal and dystrophic chicks, on the other hand, the levels of AChE are higher than those of °ChE. Immediately after hatching the AChE level decreases rapidly in normal plasma, reaching a very low level by 2‐3 weeks ex ovo. The AChE level in plasma from dystrophic birds, although less than normal from day 19 in ovo to 2 weeks ex ovo, subsequently increases to peak around 4 months at levels 15‐20‐fold of those in normal birds. There is virtually no enzyme of either type in the erythrocytes of normal or dystrophic chickens. The changes of AChE in plasma were correlated with the alterations of AChE in dystrophic fast‐twitch muscles, suggesting that the latter pool is a precursor of the plasma AChE. Both the AChE and the °ChE in plasma exist in multiple molecular forms, which are similar to certain of those found previously in the muscles of these birds. The major form (60‐80%) of both enzymes in the plasma is the M form (sedimentation coefficient ≥11 S) in all cases, but it is accompanied by certain other forms. In no case is there any of the heaviest form (H2, 19‐20 S) of AChE or of °ChE found in normal and dystrophic muscle, which is attached at the synapses in normal muscle. The pattern of forms of plasma °ChE is constant at all ages, and in normal and dystrophic chickens. The pattern of forms of AChE in the plasma, in contrast, varies with age and with dystrophy in a characteristic manner. The sedimentation coefficients and the amounts of the enzymes in fast‐twitch muscle of dystrophic animals are compared with those of the plasma forms, and an interpretation is given of the characteristic patterns of AChE and of χE in their blood.

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Cholinesterase Activity and Inherited Muscular Dystrophy of the Chicken

Cited by 30 publications

References 9 publications

Isoenzymes and Ontogeny

Isoenzymes and Ontogeny

Caveolin-3: A Causative Process of Chicken Muscular Dystrophy

Changes in the Levels and Forms of Cholinesterases in the Blood Plasma of Normal and Dystrophic Chickens

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