Acta histochemica. Supplementband最新文献_第7页

The microtubule system and the reduplication of microtubule organizing centres in Dictyostelium discoideum. 盘状盘骨的微管系统和微管组织中心的重复。

Acta histochemica. Supplementband Pub Date : 1991-01-01

E Unger, H Hädrich, S Rubino, P Cappuccinelli, P Mühlig, E Jelke

引用次数: 0

Cortical microfilament proteins and the dynamics of the plasma membrane. 皮质微丝蛋白与质膜动力学。

Acta histochemica. Supplementband Pub Date : 1991-01-01

F Buss, C Temm-Grove, B M Jockusch

{"title":"Cortical microfilament proteins and the dynamics of the plasma membrane.","authors":"F Buss, C Temm-Grove, B M Jockusch","doi":"","DOIUrl":"","url":null,"abstract":"The microfilament system is thought to provide motor elements needed for plasma membrane dynamics. This article focuses on two protein components that may play key roles in this process: (1) Profilin, a G-actin binding protein which is considered as the source of actin subunits necessary for rapid changes in the amount of actin filaments. Our data demonstrate that profilin is synthesized even in terminally differentiated blood cells of a high dynamic potential. In addition, we show that plasma membrane-associated profilin in fibroblasts is unevenly distributed and is concentrated in areas that are highly motile. (2) The filament-forming myosin which is the classical motor protein in the microfilament system. We show that interfering with myosin filaments by microinjecting antibodies causes brush border-type microvilli on epithelial cells to loose their upright position. This result, together with our previous observations on the effects of anti-myosin injection into fibroblastic and epithelial cells (loss of stress fibers and cellular contact sites, increase in locomotory activity, delay of cytokinesis), suggests that bipolar myosin filaments are needed to maintain a specific cortical tension which is lost upon antibody binding.","PeriodicalId":7002,"journal":{"name":"Acta histochemica. Supplementband","volume":"41 ","pages":"291-301"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12974256","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}

引用次数: 0

Organization and in vitro activity of microfilament bundles associated with the basement membrane of Drosophila follicles. 果蝇卵泡基底膜微丝束的组织和体外活性。

Acta histochemica. Supplementband Pub Date : 1991-01-01

H O Gutzeit

{"title":"Organization and in vitro activity of microfilament bundles associated with the basement membrane of Drosophila follicles.","authors":"H O Gutzeit","doi":"","DOIUrl":"","url":null,"abstract":"The microfilament pattern in the somatic follicle cells of Drosophila ovarian follicles has been studied by staining F-actin with rhodaminyl-phalloidin. Parallel microfilament bundles were observed at the basal side of the follicle cells at all analyzed stages, but the organization of the microfilaments was found to undergo characteristic changes during development. At previtellogenic and early vitellogenic stages the microfilaments formed very long and thin bundles which were oriented perpendicular to the long axis of the follicle. Actin-containing cell protrusions formed only at one side of each cell indicating a planar circular cell polarity (best seen at stages 7 and 8). At later stages densely packed parallel microfilaments were observed at the basal end of the follicle cells. This pattern was maintained until stage 14 when the microfilament bundles became thinner and more widely spaced and finally disintegrated. During late vitellogenic stages the cell shape differed basally and apically: while apically the cells formed regular and very precise patterns the basal cell borders were convoluted. When stage 10 follicles were isolated in simple saline solutions the diameter of the oocyte decreased during 30 min culture. This contraction, which was presumably due to the activities of the basal microfilament bundles, could be inhibited by cytochalasins as well as azide or dinitrophenol. The reaction was most likely induced by the in vitro culture conditions, since there is no evidence that the contraction also takes place in loco.","PeriodicalId":7002,"journal":{"name":"Acta histochemica. Supplementband","volume":"41 ","pages":"201-10"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12972228","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}

引用次数: 0

Demonstration of the cytoskeleton of lens epithelial cells with gold sol techniques. 用金溶胶技术观察晶状体上皮细胞的细胞骨架。

Acta histochemica. Supplementband Pub Date : 1991-01-01

M Spindler, M Iwig

引用次数: 0

Charge dependency of the effects of estramustine derivatives on microtubule assembly in vitro. 雌二醇衍生物对体外微管组装影响的电荷依赖性。

Acta histochemica. Supplementband Pub Date : 1991-01-01

M Wallin, B Fridén, M Rutberg, J Deinum

引用次数: 0

Effect of human immunodeficiency virus type 1 protease on the intermediate filament subunit protein vimentin: cleavage, in vitro assembly and altered distribution of filaments in vivo following microinjection of protease. 人免疫缺陷病毒1型蛋白酶对中间丝亚基蛋白vimentin的影响:微注射蛋白酶后丝的切割、体外组装和体内分布的改变。

Acta histochemica. Supplementband Pub Date : 1991-01-01

R L Shoeman, E Mothes, B Höner, C Kesselmeier, P Traub

{"title":"Effect of human immunodeficiency virus type 1 protease on the intermediate filament subunit protein vimentin: cleavage, in vitro assembly and altered distribution of filaments in vivo following microinjection of protease.","authors":"R L Shoeman, E Mothes, B Höner, C Kesselmeier, P Traub","doi":"","DOIUrl":"","url":null,"abstract":"The intermediate filament (IF) subunit protein vimentin is efficiently cleaved in vitro by purified human immunodeficiency virus type 1 (HIV-1) protease. Immunological data confirm that identical sites are cleaved when vimentin is polymerized into filaments or occurs as protofilaments. Preformed filaments require 10 times more protease to achieve the same extent of cleavage seen with protofilaments, suggesting that the cleavage sites are partially masked in IFs. The primary cleavage gives rise to molecule lacking most of the tail domain and which not only remains in preformed filaments, but also is capable of polymerizing into essentially normal 10 nm filaments. However, these filaments of the vimentin primary cleavage product show a propensity to form large lateral aggregates. The three secondary cleavage products of vimentin additionally lack portions of the head domain, are almost quantitatively released from preformed filaments and are not capable of forming filaments de novo. These results confirm and extend previous data obtained with desmin and provide a limit for that portion of the tail domain of type III IF subunit proteins that play a role in IF formation and stability. Microinjection of HIV-1 protease into cultured human skin fibroblasts resulted in a large increase in the percentage of cells with an altered and abnormal distribution of vimentin IFs. Most commonly, the IFs were observed to have collapsed into a clump with a juxtanuclear localization. The efficient cleavage of vimentin observed in vitro and the ability of microinjected HIV-1 protease to alter IF distribution in vivo suggest that IF proteins may serve as substrates within HIV-1 infected cells and may play a role in viral infection.","PeriodicalId":7002,"journal":{"name":"Acta histochemica. Supplementband","volume":"41 ","pages":"129-41"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12972322","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}

引用次数: 0

Measurements of the G-/F-actin equilibrium in ADP-stimulated human platelets. adp刺激的人血小板中G-/ f -肌动蛋白平衡的测量。

Acta histochemica. Supplementband Pub Date : 1991-01-01

P Spangenberg, S Heptinstall, J Crawford, U Till

引用次数: 0

Tubulin orientation in microtubules probed with domain-specific antibodies. 用结构域特异性抗体探测微管中的微管蛋白取向。

Acta histochemica. Supplementband Pub Date : 1991-01-01

P Dráber, E Dráberová, I Linhartová, V Viklický

{"title":"Tubulin orientation in microtubules probed with domain-specific antibodies.","authors":"P Dráber, E Dráberová, I Linhartová, V Viklický","doi":"","DOIUrl":"","url":null,"abstract":"A panel of monoclonal antibodies specific to alpha- or beta-tubulin subunits was used to study the location of tubulin molecules in microtubules. Limited proteolysis of tubulin with trypsin and chymotrypsin followed by immunoblotting demonstrated that the antibodies discriminated between structural domains of tubulin subunits. Antibodies against N-terminal domains were tested for their ability to interfere with the formation of microtubules in vitro. Although the antibodies exhibited similar association constants when tested on immobilized tubulin, they differed in their inhibitory effect on microtubule assembly. The sedimentation assay using microtubules prepared from purified tubulin showed an almost undetectable binding of the antibodies with the strongest inhibitory power to the microtubules. Immunofluorescence staining of unfixed detergent-extracted cells revealed that antibodies to determinants on C-terminal domains labelled microtubules, but these were not decorated with antibodies against N-terminal domains. The same results were obtained after a microinjection of antibodies into living cells. The data indicate that while parts of C-terminal domains of both subunits are exposed on the exterior of microtubules, considerable regions of the N-terminal domains are not. The surface regions of N-terminal domains appear to be involved in the formation of microtubules.","PeriodicalId":7002,"journal":{"name":"Acta histochemica. Supplementband","volume":"41 ","pages":"9-18"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12889655","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}

引用次数: 0

Structural and chemical changes in the cytoskeleton of the goldfish Mauthner cells after vestibular stimulation. 前庭刺激后金鱼毛纳细胞骨架的结构和化学变化。

Acta histochemica. Supplementband Pub Date : 1991-01-01

D A Moshkov, L N Saveljeva, G V Yanjushina, V A Funtikov

{"title":"Structural and chemical changes in the cytoskeleton of the goldfish Mauthner cells after vestibular stimulation.","authors":"D A Moshkov, L N Saveljeva, G V Yanjushina, V A Funtikov","doi":"","DOIUrl":"","url":null,"abstract":"The ultrastructure and protein content of goldfish Mauthner cells (M-cells) at different functional states induced by natural vestibular stimulations were studied. 2-h stimulation, usually causing a fatiguing of the fishes, was found to be accompanied by ultrastructural changes within M-cells and a decreased content of cytoskeletal proteins. After training by short stimulations resulting in a long-term adaptation of the fishes, the ultrastructure and protein content of M-cells could not be distinguished qualitatively and quantitatively from those of non-adapted fishes. When the adapted fishes were stimulated for 2 h the content of a 70-kDa protein was found to be increased. In addition, the content of a 42-kDa protein, obviously actin, was elevated in this case. Correspondingly, electron microscopic analysis demonstrated a significantly increased resistance of the cytoskeleton to fatiguing stimulation. The data obtained indicate that the neural cytoskeleton is a central target of fatiguing stimulation. We suppose that the 70-kDa protein is responsible for the adaptive properties of the cytoskeleton. This protein is assumed to be identical with one of the so-called heat-shock proteins of non-neural cells which have the same electrophoretic mobility and are also able to protect the cytoskeleton under stress conditions.","PeriodicalId":7002,"journal":{"name":"Acta histochemica. Supplementband","volume":"41 ","pages":"241-7"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12972231","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}

引用次数: 0

Alzheimer's disease: a monoclonal antibody raised against paired helical filaments. 阿尔茨海默病:一种单克隆抗体产生对抗成对螺旋细丝。

Acta histochemica. Supplementband Pub Date : 1991-01-01

M Brückner, U Bendix, M Hube, T Arendt, V Bigl

引用次数: 0