{"title":"The role of ZBP1 in eccentric exercise-induced skeletal muscle necroptosis.","authors":"Kexin Shi, Xiaoxue Wang, Zhifei Ke, Junping Li","doi":"10.1007/s10974-023-09660-6","DOIUrl":"10.1007/s10974-023-09660-6","url":null,"abstract":"<p><p>This study aimed to explore the occurrence of necroptosis in skeletal muscle after eccentric exercise and investigate the role and possible mechanisms of ZBP1 and its related pathway proteins in the process, providing a theoretical basis for the study of exercise-induced skeletal muscle injury and recovery. Forty-eight male adult Sprague-Dawley rats were randomly divided into a control group (C, n = 8) and an exercise group (E, n = 40). The exercise group was further divided into 0 h (E0), 12 h (E12), 24 h (E24), 48 h (E48), and 72 h (E72) after exercise, with 8 rats in each subgroup. At each time point, gastrocnemius muscle was collected under general anesthesia. The expression levels of ZBP1 and its related pathway proteins were assessed using Western blot analysis. The colocalization of pathway proteins was examined using immunofluorescence staining. After 48 h of eccentric exercise, the expression of necroptosis marker protein MLKL reached its peak (P < 0.01), and the protein levels of ZBP1, RIPK3, and HMGB1 also peaked (P < 0.01). At 48 h post high-load eccentric exercise, there was a significant increase in colocalization of ZBP1/RIPK3 pathway proteins, reaching a peak (P < 0.01). (1) Eccentric exercise induced necroptosis in skeletal muscle, with MLKL, p-MLKL<sup>S358</sup>, and HMGB1 significantly elevated, especially at 48 h after exercise. (2) After eccentric exercise, the ZBP1/RIPK3-related pathway proteins ZBP1, RIPK3, and p-RIPK3<sup>S232</sup> were significantly elevated, particularly at 48 h after exercise. (3) Following high-load eccentric exercise, there was a significant increase in the colocalization of ZBP1/RIPK3 pathway proteins, with a particularly pronounced elevation observed at 48 h post-exercise.</p>","PeriodicalId":16422,"journal":{"name":"Journal of Muscle Research and Cell Motility","volume":" ","pages":"311-323"},"PeriodicalIF":2.7,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"54229557","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Jennifer R Fleming, Iljas Müller, Thomas Zacharchenko, Kay Diederichs, Olga Mayans
{"title":"Molecular insights into titin's A-band.","authors":"Jennifer R Fleming, Iljas Müller, Thomas Zacharchenko, Kay Diederichs, Olga Mayans","doi":"10.1007/s10974-023-09649-1","DOIUrl":"10.1007/s10974-023-09649-1","url":null,"abstract":"<p><p>The thick filament-associated A-band region of titin is a highly repetitive component of the titin chain with important scaffolding properties that support thick filament assembly. It also has a demonstrated link to human disease. Despite its functional significance, it remains a largely uncharacterized part of the titin protein. Here, we have performed an analysis of sequence and structure conservation of A-band titin, with emphasis on poly-FnIII tandem components. Specifically, we have applied multi-dimensional sequence pairwise similarity analysis to FnIII domains and complemented this with the crystallographic elucidation of the 3D-structure of the FnIII-triplet A84-A86 from the fourth long super-repeat in the C-zone (C4). Structural models serve here as templates to map sequence conservation onto super-repeat C4, which we show is a prototypical representative of titin's C-zone. This templating identifies positionally conserved residue clusters in C super-repeats with the potential of mediating interactions to thick-filament components. Conservation localizes to two super-repeat positions: Ig domains in position 1 and FnIII domains in position 7. The analysis also allows conclusions to be drawn on the conserved architecture of titin's A-band, as well as revisiting and expanding the evolutionary model of titin's A-band.</p>","PeriodicalId":16422,"journal":{"name":"Journal of Muscle Research and Cell Motility","volume":" ","pages":"255-270"},"PeriodicalIF":2.7,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10665226/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9557291","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Daren Elkrief, Oleg Matusovsky, Yu-Shu Cheng, Dilson E Rassier
{"title":"From amino-acid to disease: the effects of oxidation on actin-myosin interactions in muscle.","authors":"Daren Elkrief, Oleg Matusovsky, Yu-Shu Cheng, Dilson E Rassier","doi":"10.1007/s10974-023-09658-0","DOIUrl":"10.1007/s10974-023-09658-0","url":null,"abstract":"<p><p>Actin-myosin interactions form the basis of the force-producing contraction cycle within the sarcomere, serving as the primary mechanism for muscle contraction. Post-translational modifications, such as oxidation, have a considerable impact on the mechanics of these interactions. Considering their widespread occurrence, the explicit contributions of these modifications to muscle function remain an active field of research. In this review, we aim to provide a comprehensive overview of the basic mechanics of the actin-myosin complex and elucidate the extent to which oxidation influences the contractile cycle and various mechanical characteristics of this complex at the single-molecule, myofibrillar and whole-muscle levels. We place particular focus on amino acids shown to be vulnerable to oxidation in actin, myosin, and some of their binding partners. Additionally, we highlight the differences between in vitro environments, where oxidation is controlled and limited to actin and myosin and myofibrillar or whole muscle environments, to foster a better understanding of oxidative modification in muscle. Thus, this review seeks to encompass a broad range of studies, aiming to lay out the multi layered effects of oxidation in in vitro and in vivo environments, with brief mention of clinical muscular disorders associated with oxidative stress.</p>","PeriodicalId":16422,"journal":{"name":"Journal of Muscle Research and Cell Motility","volume":" ","pages":"225-254"},"PeriodicalIF":2.7,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41131281","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Oksana P Gerzen, Ruslan V Lisin, Alexander A Balakin, Elena A Mukhlynina, Daniil A Kuznetsov, Larisa V Nikitina, Yuri L Protsenko
{"title":"Characteristics of the right atrial and right ventricular contractility in a model of monocrotaline-induced pulmonary arterial hypertension.","authors":"Oksana P Gerzen, Ruslan V Lisin, Alexander A Balakin, Elena A Mukhlynina, Daniil A Kuznetsov, Larisa V Nikitina, Yuri L Protsenko","doi":"10.1007/s10974-023-09651-7","DOIUrl":"10.1007/s10974-023-09651-7","url":null,"abstract":"<p><p>Pulmonary arterial hypertension (PAH) leads to changes in the pump function of the heart and causes right-sided myocardial hypertrophy and heart failure. This study was the first to compare the contractile characteristics of the multicellular myocardial preparations of the right atrium (RA) and right ventricle (RV) of male rats from the control group (CON) and the group with monocrotaline (MCT)-induced hypertrophy at the molecular and multicellular levels. In both RA and RV in MCT-treated rats, the fraction of motile filaments and the maximum sliding velocity of actin and reconstituted thin filaments over myosin decreased, and the ratio of α-/β-myosin heavy chains (MHC) shifted towards β-MHC. In the RA strips and RV trabeculae, the maximum shortening velocity, the extent of muscle shortening, the amplitude of isometric stress, the amount of work decreased. PAH leads to a greater drop in right atrial contractility than that of the ventricle.</p>","PeriodicalId":16422,"journal":{"name":"Journal of Muscle Research and Cell Motility","volume":" ","pages":"299-309"},"PeriodicalIF":2.7,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9593831","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Fatemeh Abbasi Yeganeh, Corinne Summerill, Zhongjun Hu, Hamidreza Rahmani, Dianne W Taylor, Kenneth A Taylor
{"title":"The cryo-EM 3D image reconstruction of isolated Lethocerus indicus Z-discs.","authors":"Fatemeh Abbasi Yeganeh, Corinne Summerill, Zhongjun Hu, Hamidreza Rahmani, Dianne W Taylor, Kenneth A Taylor","doi":"10.1007/s10974-023-09657-1","DOIUrl":"10.1007/s10974-023-09657-1","url":null,"abstract":"<p><p>The Z-disk of striated muscle defines the ends of the sarcomere, which repeats many times within the muscle fiber. Here we report application of cryoelectron tomography and subtomogram averaging to Z-disks isolated from the flight muscles of the large waterbug Lethocerus indicus. We use high salt solutions to remove the myosin containing filaments and use gelsolin to remove the actin filaments of the A- and I-bands leaving only the thin filaments within the Z-disk which were then frozen for cryoelectron microscopy. The Lethocerus Z-disk structure is similar in many ways to the previously studied Z-disk of the honeybee Apis mellifera. At the corners of the unit cell are positioned trimers of paired antiparallel F-actins defining a large solvent channel, whereas at the trigonal positions are positioned F-actin trimers converging slowly towards their (+) ends defining a small solvent channel through the Z-disk. These near parallel F-actins terminate at different Z-heights within the Z-disk. The two types of solvent channel in Lethocerus are similar in size compared to those of Apis which are very different in size. Two types of α-actinin crosslinks were observed between oppositely oriented actin filaments. In one of these, the α-actinin long axis is almost parallel to the F-actins it crosslinks. In the other, the α-actinins are at a small but distinctive angle with respect to the crosslinked actin filaments. The utility of isolated Z-disks for structure determination is discussed.</p>","PeriodicalId":16422,"journal":{"name":"Journal of Muscle Research and Cell Motility","volume":" ","pages":"271-286"},"PeriodicalIF":1.8,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10843718/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10143470","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Obituary: Professor John Michael Squire.","authors":"Edward P Morris, Carlo Knupp, Pradeep K Luther","doi":"10.1007/s10974-023-09656-2","DOIUrl":"10.1007/s10974-023-09656-2","url":null,"abstract":"","PeriodicalId":16422,"journal":{"name":"Journal of Muscle Research and Cell Motility","volume":" ","pages":"125-132"},"PeriodicalIF":2.7,"publicationDate":"2023-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10500871","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pradeep K Luther, Edward P Morris, David A D Parry, Kenneth A Taylor
{"title":"John Squire: a leader and seminal contributor to experimental and theoretical muscle research for over 50 years.","authors":"Pradeep K Luther, Edward P Morris, David A D Parry, Kenneth A Taylor","doi":"10.1007/s10974-023-09659-z","DOIUrl":"10.1007/s10974-023-09659-z","url":null,"abstract":"","PeriodicalId":16422,"journal":{"name":"Journal of Muscle Research and Cell Motility","volume":"44 3","pages":"123-124"},"PeriodicalIF":2.7,"publicationDate":"2023-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41176485","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The vertebrate muscle superlattice: discovery, consequences, and link to geometric frustration.","authors":"Rick P Millane, Pradeep K Luther","doi":"10.1007/s10974-023-09642-8","DOIUrl":"10.1007/s10974-023-09642-8","url":null,"abstract":"<p><p>Early x-ray diffraction studies of muscle revealed spacings larger than the basic thick filament lattice spacing and led to a number of speculations on the mutual rotations of the filaments in the myosin lattice. The nature of the arrangements of the filaments was resolved by John Squire and Pradeep Luther using careful electron microscopy and image analysis. The intriguing disorder in the rotations, that they termed the myosin superlattice, remained a curiosity, until work with Rick Millane and colleagues showed a connection to \"geometric frustration,\" a well-known phenomenon in statistical and condensed matter physics. In this review, we describe how this connection gives a satisfying physical basis for the myosin superlattice, and how recent work has shown relationships to muscle mechanical behaviour.</p>","PeriodicalId":16422,"journal":{"name":"Journal of Muscle Research and Cell Motility","volume":" ","pages":"153-163"},"PeriodicalIF":2.7,"publicationDate":"2023-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10541841/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9455204","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Xinrui Huang, Iratxe Torre, Michele Chiappi, Zhan Yin, Anupama Vydyanath, Shuangyi Cao, Oliver Raschdorf, Morgan Beeby, Bonnie Quigley, Pieter P de Tombe, Jun Liu, Edward P Morris, Pradeep K Luther
{"title":"Cryo-electron tomography of intact cardiac muscle reveals myosin binding protein-C linking myosin and actin filaments.","authors":"Xinrui Huang, Iratxe Torre, Michele Chiappi, Zhan Yin, Anupama Vydyanath, Shuangyi Cao, Oliver Raschdorf, Morgan Beeby, Bonnie Quigley, Pieter P de Tombe, Jun Liu, Edward P Morris, Pradeep K Luther","doi":"10.1007/s10974-023-09647-3","DOIUrl":"10.1007/s10974-023-09647-3","url":null,"abstract":"<p><p>Myosin binding protein C (MyBP-C) is an accessory protein of the thick filament in vertebrate cardiac muscle arranged over 9 stripes of intervals of 430 Å in each half of the A-band in the region called the C-zone. Mutations in cardiac MyBP-C are a leading cause of hypertrophic cardiomyopathy the mechanism of which is unknown. It is a rod-shaped protein composed of 10 or 11 immunoglobulin- or fibronectin-like domains labelled C0 to C10 which binds to the thick filament via its C-terminal region. MyBP-C regulates contraction in a phosphorylation dependent fashion that may be through binding of its N-terminal domains with myosin or actin. Understanding the 3D organisation of MyBP-C in the sarcomere environment may provide new light on its function. We report here the fine structure of MyBP-C in relaxed rat cardiac muscle by cryo-electron tomography and subtomogram averaging of refrozen Tokuyasu cryosections. We find that on average MyBP-C connects via its distal end to actin across a disc perpendicular to the thick filament. The path of MyBP-C suggests that the central domains may interact with myosin heads. Surprisingly MyBP-C at Stripe 4 is different; it has weaker density than the other stripes which could result from a mainly axial or wavy path. Given that the same feature at Stripe 4 can also be found in several mammalian cardiac muscles and in some skeletal muscles, our finding may have broader implication and significance. In the D-zone, we show the first demonstration of myosin crowns arranged on a uniform 143 Å repeat.</p>","PeriodicalId":16422,"journal":{"name":"Journal of Muscle Research and Cell Motility","volume":" ","pages":"165-178"},"PeriodicalIF":2.7,"publicationDate":"2023-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10542292/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9350272","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Kenton P Arkill, C Charles Michel, Elizabeth V M Rider, Elise A Wood, Mathew O Small, Jennifer L E Brown, Abigail L Kinnaird
{"title":"John squire and endothelial glycocalyx structure: an unfinished story.","authors":"Kenton P Arkill, C Charles Michel, Elizabeth V M Rider, Elise A Wood, Mathew O Small, Jennifer L E Brown, Abigail L Kinnaird","doi":"10.1007/s10974-022-09629-x","DOIUrl":"10.1007/s10974-022-09629-x","url":null,"abstract":"<p><p>John Squire did not only produce leading works in the muscle field, he also significantly contributed to the vascular permeability field by ultrastructural analysis of the endothelial glycocalyx. Presented here is a review of his involvement in the field by his main collaborator C.C. Michel and his last postdoctoral researcher KP Arkill. We end on a reinterpretation of his work that arguably links to our current understanding of endothelial glycocalyx structure and composition predicting 6 glycosaminoglycans fibres per syndecan core protein, only achieved in the endothelium by dimerization.</p>","PeriodicalId":16422,"journal":{"name":"Journal of Muscle Research and Cell Motility","volume":" ","pages":"217-223"},"PeriodicalIF":2.7,"publicationDate":"2023-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10542707/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10858818","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}