Pub Date : 1985-01-01DOI: 10.1007/978-1-4757-4723-2_8
T Wallimann, H M Eppenberger
{"title":"Localization and function of M-line-bound creatine kinase. M-band model and creatine phosphate shuttle.","authors":"T Wallimann, H M Eppenberger","doi":"10.1007/978-1-4757-4723-2_8","DOIUrl":"https://doi.org/10.1007/978-1-4757-4723-2_8","url":null,"abstract":"","PeriodicalId":77836,"journal":{"name":"Cell and muscle motility","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/978-1-4757-4723-2_8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15004186","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1985-01-01DOI: 10.1007/978-1-4757-4723-2_10
K Wang
{"title":"Sarcomere-associated cytoskeletal lattices in striated muscle. Review and hypothesis.","authors":"K Wang","doi":"10.1007/978-1-4757-4723-2_10","DOIUrl":"https://doi.org/10.1007/978-1-4757-4723-2_10","url":null,"abstract":"","PeriodicalId":77836,"journal":{"name":"Cell and muscle motility","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15004188","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1985-01-01DOI: 10.3929/ETHZ-A-000370124
T. Wallimann, Eppenberger Hm
S: T. Wallimann, D.C. Turner, and H.M. Eppenberger. Localization of creatine kinase at the M-line of skeletal muscle myofibrils. Abstracts for 5th Annual Meeting of the Union for Swiss Societies for Experimental Biology in Basel, Switzerland (USGEB) (1973), p. 23 H.M. Eppenberger, D.C. Turner, and T. Wallimann. Evidenz für das Vorhandensein strukturell gebundener M-TypKreatinkinase (E.C. 2.7.3.2.) im Bereich der A-Bande lm quergestreiften Skelettmuskel. Hoppe-Seyler's Zeitschrift für Physiol. Chemie 354: 228 (1973) T. Wallimann, and H.M. Eppenberger. Ultrastructural localization of the M-line protein creatine kinase in chicken pectoralis muscle. Abstracts of the American Society for Cell Biology 17th Annual Meeting 15-18 Nov. 1977, San Diego, Cal. in: J.Cell Biol. 75: 326a (1977) W.F. Stafford 111, E.M. Szentkiralyi, T. Wallimann, and A.G. Szent-Gyprgyi. Interaction of light chains with scallop myosin. Abstract of the Intl. Meeting on Muscle in Alpbach, Austria (1976) A.G. Szent-Györgyi, P.D. Chantler, J. Sellers, W.F. Stafford, E.M. Szentkiralyi, and T. Wallimann. Myosin-linked calcium regulation. Abstracts of the sixth Intl. Biophysics Congress, Kyoto, Japan, 3-9 Sept. (1978), p. 86 T. Wallimann, and A.G. Szent-Györgyi. Effectsof anti-scallop myosin light-chain antibodies on myosin linked regulation. 23rd Annual Meeting of the Biophysical Society, 25-28 Febr. (1979) in: Biophys. J. 25: 72a (1979) T. Wallimann, and A.E. Szent-Györgyi. Immunological comparison of heavy and light-chains from different myosins by indirect, competitive radioimmunobinding assay, a novel IC RIBA technique. Abstract for ASBC!BS Meeting in Atlanta. in: Federation Proceedings 39: 2167, abstract 2956 (1980) Paula Flicker, Theo Wallimann, and Peter Vibert. Location of regulatory light chais in scallop myosin. Biophys. J. 33: 279a (1981) P.M.D. Harwicke, Theo Wallimann, and Andrew G. Szent-Györgyi. Proximity of the regulatory and essential light chains in scallop myosin. Biophys. J. 33: 279a (1981) H.M. Eppenberger, T.D. Doetschman, J.C. Perriard, E.E. Strehler, D. Studer, and T. Wallimann. Myomesin in cross-striated muscle cells. Cold Spring Harbor Symposium on: Molecular and Cel1ular Control of Muscle Deveelopment. 8-13 Sept. (1981) p.l0l. T. Schlösser, T. Wallimann, and H.M. Eppenberger. Physiological significance of M-line-bound creatine kinase (CK). Experientia ~: 731 (1982) E.E. Strehler, T. Wallimann, and H.M. Eppenberger. Interaction between M-line Proteins and Myosin. 22n Annual Meeting of the American Society for Cell Biology, Baltimore, 30 Nov. 4 Dec. (1982) in: J. Cell Biol. 95: 360a (1982) Walzthöny, D., M. Bähler, T. Wallimann, H. Gross, H.M. Eppenberger, and H. Moor. Improved techniques for the visualization of myosin molecules. 10th Intl. Congress on Electron Microscopy, Hamburg, 17-24 Aug. (1982) M. Bähler, E.E. Strehler, D. Walzthöny, H.M. Eppenberger, and T. Wallimann. Myosin Binding Proteins. 11th Europ. Congress on Muscle and Motility, Leicester, 14-18
S: T.沃利曼,D.C.特纳和H.M.埃彭伯格。肌酸激酶在骨骼肌肌原纤维m线的定位。瑞士巴塞尔实验生物学协会联盟第五届年会摘要(USGEB)(1973),第23页H.M. Eppenberger, D.C. Turner和T. Wallimann。文献资料:文献资料:文献资料:文献资料:文献资料:文献资料:文献资料:文献资料:文献资料:文献资料:霍普-塞勒时代<s:1>物理学报。化学354:228 (1973)T. Wallimann和H.M. Eppenberger。鸡胸肌肌酸激酶m系蛋白的超微结构定位。1977年11月15-18日,加州圣地亚哥,美国细胞生物学学会第17届年会摘要,细胞生物学杂志,75:326a (1977) W.F. Stafford 111, E.M. Szentkiralyi, T. Wallimann和A.G. Szent-Gyprgyi。轻链与扇贝肌球蛋白的相互作用。全文摘要。在奥地利Alpbach的肌肉会议(1976)A.G. Szent-Györgyi, P.D. Chantler, J. Sellers, W.F. Stafford, E.M. Szentkiralyi和T. Wallimann。肌球蛋白连接钙调节。第六届国际会议摘要。生物物理学大会,日本京都,1978年9月3-9日,p. 86 T. Wallimann和A.G. Szent-Györgyi。抗扇贝肌球蛋白轻链抗体对肌球蛋白相关调控的影响。第23届生物物理学会年会,2月25-28日。(1979)见:《生物物理学》。[j] . 25: 72a(1979)王晓明,王晓明。Szent-Györgyi。通过间接、竞争性放射免疫结合试验对不同肌球蛋白重链和轻链的免疫学比较,这是一种新的IC RIBA技术。ASBC的摘要!BS在亚特兰大开会。Paula Flicker, Theo Wallimann, and Peter Vibert。扇贝肌凝蛋白调控轻链的定位。生物物理学。[j] . 33: 279a(1981)王志强。Szent-Györgyi。扇贝肌球蛋白调节链和必需轻链的接近性。生物物理学。[j] . 33: 279a (1981): H.M. Eppenberger, T.D. Doetschman, J.C. Perriard, E.E. Strehler, D. Studer, T. Wallimann。交叉横纹肌细胞中的肌凝蛋白。冷泉港研讨会:肌肉发育的分子和细胞控制。1981年9月8-13日,第11页。T. Schlösser, T. Wallimann和H.M. Eppenberger。m线结合肌酸激酶(CK)的生理意义。《经验》杂志:731(1982)。m系蛋白与肌球蛋白的相互作用。美国细胞生物学学会年会上,巴尔的摩,11月30日至12月(1982):J.细胞生物学,95:360a (1982) Walzthöny, D., M. Bähler, T. Wallimann, H. Gross, H.M. Eppenberger和H. Moor。肌球蛋白分子可视化技术的改进。10 Intl。电子显微镜大会,汉堡,8月17-24日(1982年)M. Bähler, E.E. Strehler, D. Walzthöny, H.M. Eppenberger和T. Wallimann。肌球蛋白结合蛋白,第11欧共体。肌肉和运动性大会,莱斯特,1982年9月14-18日,in: J.肌肉和细胞运动性1:484 (1983)Theo ~vallimann, Toni Schlösser, Hans M. Eppenberger。m线结合肌酸激酶的atp再生潜能。生理学意义。第11期。肌肉和运动性大会,莱斯特,1982年9月14-18日,in: J.肌肉和细胞运动性3:503-504 (1983)A.G. Szent-Györgyi, T. Wallimann和P.M.D. Hardwicke。扇贝肌凝蛋白的轻链运动及其调控。Biopyhs。j .我!: 227a(1983)西奥·沃利曼,托尼Schlösser,和汉斯·m·埃彭伯格。m线结合肌酸激酶(CK)。定位和功能。EMBO肌肉发生研讨会,boldernjzrich,瑞士,1983年3月7-12日,Pau1a F. Flicker, Theo Wa11imann, Peter Vibert。sc110p肌球蛋白调节轻链的定位。1983年3月21日至26日,奥地利Alpbach的EMBO工作坊,Doris Wa1zthöny, Martin Bäh1er, Hans M. Eppenberger和Theo Wa11imann。在EM支持膜上固定后,通过直接遮蔽冷冻干燥的肌球蛋白分子来观察。1983年3月21日至26日,奥地利Alpbach的EMBO工作坊,Theo Wa11imann, Toni Schlösser和Hans M. Epenberger。m -1结合肌酸激酶的atp再生潜能。Physio1ogcia1意义。1983年3月21日至26日在奥地利Alpbach举行的EMBO研讨会,Wa1zthöny博士,Bäh1er博士,H.M. Eppenberger, A. Engel和T. Wal1imann。冷冻干燥和阴影的原肌凝蛋白、肌凝蛋白、含c蛋白的重肌凝蛋白(HMM)和STEM中“未染色”肌凝蛋白的可视化。电子显微镜联合会议,比利时安特卫普,1983年9月11-16日。摘要No. 52, p. 74 (1983) D. Wa1zthöny, M. Bähler, H.M. Eppenberger, A. Engel和T. Wallimann。阴影显示肌凝蛋白棒的螺距值和周期性表面电荷分布。STEM中未染色肌球蛋白的可视化。12日欧洲。肌肉和运动性大会,塞格德,匈牙利,1983年9月10日,见:J. Musc1e Res.和Ce11 . Moti1ity M. Bäh1er, H.M. Eppenberger和T. Wal1imann。 表明m系蛋白在粗纤维的组装和结构中起作用。12日欧洲。肌肉和动力大会,塞格德,匈牙利,1983年9月10日,见:J.肌肉和动力Theo Wa11imann, T. Schlösser和H.M. Eppenberger。m线结合肌酸激酶(CK)参与CPshuttle。12日欧洲。肌肉和运动大会,塞格德,匈牙利,1983年9月10日,见:J.肌肉和运动
{"title":"Localization and function of M-line-bound creatine kinase. M-band model and creatine phosphate shuttle.","authors":"T. Wallimann, Eppenberger Hm","doi":"10.3929/ETHZ-A-000370124","DOIUrl":"https://doi.org/10.3929/ETHZ-A-000370124","url":null,"abstract":"S: T. Wallimann, D.C. Turner, and H.M. Eppenberger. Localization of creatine kinase at the M-line of skeletal muscle myofibrils. Abstracts for 5th Annual Meeting of the Union for Swiss Societies for Experimental Biology in Basel, Switzerland (USGEB) (1973), p. 23 H.M. Eppenberger, D.C. Turner, and T. Wallimann. Evidenz für das Vorhandensein strukturell gebundener M-TypKreatinkinase (E.C. 2.7.3.2.) im Bereich der A-Bande lm quergestreiften Skelettmuskel. Hoppe-Seyler's Zeitschrift für Physiol. Chemie 354: 228 (1973) T. Wallimann, and H.M. Eppenberger. Ultrastructural localization of the M-line protein creatine kinase in chicken pectoralis muscle. Abstracts of the American Society for Cell Biology 17th Annual Meeting 15-18 Nov. 1977, San Diego, Cal. in: J.Cell Biol. 75: 326a (1977) W.F. Stafford 111, E.M. Szentkiralyi, T. Wallimann, and A.G. Szent-Gyprgyi. Interaction of light chains with scallop myosin. Abstract of the Intl. Meeting on Muscle in Alpbach, Austria (1976) A.G. Szent-Györgyi, P.D. Chantler, J. Sellers, W.F. Stafford, E.M. Szentkiralyi, and T. Wallimann. Myosin-linked calcium regulation. Abstracts of the sixth Intl. Biophysics Congress, Kyoto, Japan, 3-9 Sept. (1978), p. 86 T. Wallimann, and A.G. Szent-Györgyi. Effectsof anti-scallop myosin light-chain antibodies on myosin linked regulation. 23rd Annual Meeting of the Biophysical Society, 25-28 Febr. (1979) in: Biophys. J. 25: 72a (1979) T. Wallimann, and A.E. Szent-Györgyi. Immunological comparison of heavy and light-chains from different myosins by indirect, competitive radioimmunobinding assay, a novel IC RIBA technique. Abstract for ASBC!BS Meeting in Atlanta. in: Federation Proceedings 39: 2167, abstract 2956 (1980) Paula Flicker, Theo Wallimann, and Peter Vibert. Location of regulatory light chais in scallop myosin. Biophys. J. 33: 279a (1981) P.M.D. Harwicke, Theo Wallimann, and Andrew G. Szent-Györgyi. Proximity of the regulatory and essential light chains in scallop myosin. Biophys. J. 33: 279a (1981) H.M. Eppenberger, T.D. Doetschman, J.C. Perriard, E.E. Strehler, D. Studer, and T. Wallimann. Myomesin in cross-striated muscle cells. Cold Spring Harbor Symposium on: Molecular and Cel1ular Control of Muscle Deveelopment. 8-13 Sept. (1981) p.l0l. T. Schlösser, T. Wallimann, and H.M. Eppenberger. Physiological significance of M-line-bound creatine kinase (CK). Experientia ~: 731 (1982) E.E. Strehler, T. Wallimann, and H.M. Eppenberger. Interaction between M-line Proteins and Myosin. 22n Annual Meeting of the American Society for Cell Biology, Baltimore, 30 Nov. 4 Dec. (1982) in: J. Cell Biol. 95: 360a (1982) Walzthöny, D., M. Bähler, T. Wallimann, H. Gross, H.M. Eppenberger, and H. Moor. Improved techniques for the visualization of myosin molecules. 10th Intl. Congress on Electron Microscopy, Hamburg, 17-24 Aug. (1982) M. Bähler, E.E. Strehler, D. Walzthöny, H.M. Eppenberger, and T. Wallimann. Myosin Binding Proteins. 11th Europ. Congress on Muscle and Motility, Leicester, 14-18 ","PeriodicalId":77836,"journal":{"name":"Cell and muscle motility","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"70170207","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1985-01-01DOI: 10.1007/978-1-4757-4723-2_5
N Marceau, S H Swierenga
The possible relationship between cytoskeletal events and growth regulation in response to stimulation by calcium and by growth factors such as EGF can be summarized as follows: An elaborate interaction exists between calcium and serum growth factors, such as EGF, in the initiation of DNA synthesis in quiescent cells. This implies that many processes between the external signals delivered at the cell surface and the sequential intracellular events that lead to chromosomal replication, and ultimately to cell division, must be coordinated in a reproducible manner. It is now apparent that because of its possible role as a dynamic integrator of the cytoplasm, the cytoskeleton could represent the coordinator of the events that lead to replication. Calcium (with its intracellular acceptor, calmodulin) and cAMP (which can act by opposing mechanisms) are extensively involved in the control of the integrity of the cytoskeleton. Distinct protein kinases are activated by calcium/calmodulin, EGF, and cAMP as aspects of the prereplicative response, and many of the substrates for phosphorylation are cytoskeletal proteins. The emerging picture seems to include a direct involvement of these protein kinases in the cascade of regulatory events that leads to the initiation of DNA synthesis. Thus, the cytoskeleton has a direct role in the transmission of proliferative signals from external receptor sites to the nucleus. A means by which neoplastic cells can bypass the normal regulatory pathways is proposed in the light of recent data showing that the product of oncogenes are protein kinases or proteins that intimately interact with cellular protein kinases.
{"title":"Cytoskeletal events during calcium- or EGF-induced initiation of DNA synthesis in cultured cells. Role of protein phosphorylation and clues in the transformation process.","authors":"N Marceau, S H Swierenga","doi":"10.1007/978-1-4757-4723-2_5","DOIUrl":"https://doi.org/10.1007/978-1-4757-4723-2_5","url":null,"abstract":"<p><p>The possible relationship between cytoskeletal events and growth regulation in response to stimulation by calcium and by growth factors such as EGF can be summarized as follows: An elaborate interaction exists between calcium and serum growth factors, such as EGF, in the initiation of DNA synthesis in quiescent cells. This implies that many processes between the external signals delivered at the cell surface and the sequential intracellular events that lead to chromosomal replication, and ultimately to cell division, must be coordinated in a reproducible manner. It is now apparent that because of its possible role as a dynamic integrator of the cytoplasm, the cytoskeleton could represent the coordinator of the events that lead to replication. Calcium (with its intracellular acceptor, calmodulin) and cAMP (which can act by opposing mechanisms) are extensively involved in the control of the integrity of the cytoskeleton. Distinct protein kinases are activated by calcium/calmodulin, EGF, and cAMP as aspects of the prereplicative response, and many of the substrates for phosphorylation are cytoskeletal proteins. The emerging picture seems to include a direct involvement of these protein kinases in the cascade of regulatory events that leads to the initiation of DNA synthesis. Thus, the cytoskeleton has a direct role in the transmission of proliferative signals from external receptor sites to the nucleus. A means by which neoplastic cells can bypass the normal regulatory pathways is proposed in the light of recent data showing that the product of oncogenes are protein kinases or proteins that intimately interact with cellular protein kinases.</p>","PeriodicalId":77836,"journal":{"name":"Cell and muscle motility","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14120774","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Tropomyosin. Structural and functional diversity.","authors":"M R Payne, S E Rudnick","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77836,"journal":{"name":"Cell and muscle motility","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15004184","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1985-01-01DOI: 10.1007/978-1-4757-4723-2_2
A Ben-Ze'ev
{"title":"Cell shape, the complex cellular networks, and gene expression. Cytoskeletal protein genes as a model system.","authors":"A Ben-Ze'ev","doi":"10.1007/978-1-4757-4723-2_2","DOIUrl":"https://doi.org/10.1007/978-1-4757-4723-2_2","url":null,"abstract":"","PeriodicalId":77836,"journal":{"name":"Cell and muscle motility","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13723630","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}