Digestion of proteins associated with the Z-disc by calpain

Bullard, Belinda; Sainsbury, G M; Miller, Nigel

doi:10.1007/bf01843580

Cited by 43 publications

(16 citation statements)

References 45 publications

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“…Z-discs are degraded in the early stages of muscle fibre autolysis by calpain, a calcium dependent protease that is distributed throughout the sarcomere of striated muscle fibres but is more concentrated in the Z-disc (Goll et al, 1990). Calpain disrupts the Z-disc in striated muscles of vertebrates and insect ffight muscle without affecting the overall structure of the rest of the sarcomere (Reddy et al, 1975;Dayton et al, 1976;Reedy et al, 1981;Bullard et al, 1990). ca-Actinin is released from the vertebrate Z-disc without being cleaved, therefore it is likely that calpain digests a protein that anchors a-actinin in the Z-disc (Goll et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

Kettin, a large modular protein in the Z-disc of insect muscles.

et al. 1993

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Z‐discs of insect flight muscle contain a large protein of 500–700 kDa. Monoclonal antibodies label an epitope in the molecule at the Z‐disc in Drosophila and Lethocerus (waterbug). A partial cDNA of 1.6 kb from the Drosophila gene has been cloned and sequenced. The corresponding amino acid sequence has a modular structure composed of four conserved repeats of 95 amino acids homologous to immunoglobulin C2 domains (called class II domains in muscle proteins), separated by less conserved linker sequences of 35 amino acids. An expressed class II domain with flanking linker sequences binds to actin and alpha‐actinin but not to myosin. Single molecules of the protein would be large enough to span the Z‐disc. We suggest that the protein acts as scaffolding in the Z‐disc and we call the protein kettin. The Ca2+ activated protease, calpain, disrupts the Z‐disc of striated muscle, releasing alpha‐actinin intact. Calpain digests kettin to a series of peptides of between 30 and 170 kDa which are released from the myofibril. Digestion of kettin may cause disintegration of the Z‐disc and alpha‐actinin release which lead to disassembly of the myofibril.

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Section: Introductionmentioning

confidence: 99%

Kettin, a large modular protein in the Z-disc of insect muscles.

et al. 1993

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“…The intramuscular PL level is reported to decrease on the postmortem aging of beef, pork, and chicken; this change affects the qualities of meat (e.g., myofibrillar fragmentation and drip loss). [4][5][6][7][8][9][10][11] However, there is still little information on the effect of muscle position and breed on the PL compositions. The aim of this study was to evaluate the effect of postmortem aging on the intramuscular fatty acid and PL compositions in primal cuts (round and loin) of cattle and Yezo sika deer.…”

Section: Discussionmentioning

confidence: 99%

Decrease in Intramuscular Levels of Phosphatidylethanolamine Bearing Arachidonic Acid During Postmortem Aging Depends on Meat Cuts and Breed

Yamashita

Shimada

Sakurai

et al. 2019

Euro J Lipid Sci & Tech

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The intramuscular phospholipid (PL) level is reported to decrease upon postmortem aging of beef, pork, and chicken, and the change affects meat qualities (e.g., myofibrillar fragmentation and drip loss); however, there is still little information on the effect of muscle position and breed on PL compositions. A preliminary study is performed to investigate the effect of intramuscular PL composition on postmortem aging of beef and venison. Loin and round parts of beef and venison are kept at 4 °C for 28 postmortem days to elucidate the maximum effect of meat aging. The arachidonic acid (20:4n‐6) content in PL decreases in round meat during postmortem aging, while the PL 20:4n‐6 content is not affected in loin meat. The PL molecular species analysis reveals that such content reduction is consistent with decreases in phosphatidylethanolamine (PtdEtn) levels, especially that bearing 20:4n‐6. In addition, the content reduction by aging is affected by the meat cuts and the breed. These results suggest that PL variation depends on meat cuts and breed, and the release of 20:4n‐6 from PL has a considerable influence on meat qualities owing to the high reactivity of the polyunsaturated chain. The present results will enable eventual improvement of the taste, smell, and texture of meat during postmortem aging. Practical Applications: This preliminary study investigates the changes in intramuscular PL composition in beef and venison after postmortem aging. Consequently, PL variation depends on meat cuts and may be induced potentially owing to activity of cytosolic phospholipase A2. Meat properties (e.g., drip, flavor, and taste) are considered as affected by the PL hydrolysis and the 20:4n‐6 release. Therefore, monitoring of variation of PL species might be useful to estimate the condition of meat quality by postmortem aging. Our preliminary study investigates the changes in intramuscular phospholipid (PL) composition in beef and venison after postmortem aging. Postmortem aging decreases the phospholipid levels in meats. The 20:4n‐6 is released from the meat phospholipid during postmortem aging. The two above‐mentioned are considered due to hydrolyzation of the diacylglycerophospholipids in meats. The hydrolysis of phospholipid may depend on meat cuts and breed.

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“…Calpain 1 and 2 do not degrade actin, suggesting that another factor involved in F-actin maintenance may also be required during thin filament turnover [84]. Calpain 1 and/or calpain 2 will release α-actinin while calpain 1 and/or calpain 3 cleave filamin C from the Z-disc [78,80,85,86]. All three calpains will free titin at the Z-disc, with most studies focused on calpain 3 and its localization to titin throughout muscle development [84,[87][88][89].…”

Section: Calpain Mediated Breakdown Of Z-disc and Thin Filamentsmentioning

confidence: 99%

Assembly and Maintenance of Sarcomere Thin Filaments and Associated Diseases

Prill

Dawson

2020

IJMS

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Sarcomere assembly and maintenance are essential physiological processes required for cardiac and skeletal muscle function and organism mobility. Over decades of research, components of the sarcomere and factors involved in the formation and maintenance of this contractile unit have been identified. Although we have a general understanding of sarcomere assembly and maintenance, much less is known about the development of the thin filaments and associated factors within the sarcomere. In the last decade, advancements in medical intervention and genome sequencing have uncovered patients with novel mutations in sarcomere thin filaments. Pairing this sequencing with reverse genetics and the ability to generate patient avatars in model organisms has begun to deepen our understanding of sarcomere thin filament development. In this review, we provide a summary of recent findings regarding sarcomere assembly, maintenance, and disease with respect to thin filaments, building on the previous knowledge in the field. We highlight debated and unknown areas within these processes to clearly define open research questions.

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Digestion of proteins associated with the Z-disc by calpain

Cited by 43 publications

References 45 publications

Kettin, a large modular protein in the Z-disc of insect muscles.

Kettin, a large modular protein in the Z-disc of insect muscles.

Decrease in Intramuscular Levels of Phosphatidylethanolamine Bearing Arachidonic Acid During Postmortem Aging Depends on Meat Cuts and Breed

Assembly and Maintenance of Sarcomere Thin Filaments and Associated Diseases

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