{"title":"Author index for volume 102","authors":"","doi":"10.1016/0889-1605(89)90024-4","DOIUrl":"https://doi.org/10.1016/0889-1605(89)90024-4","url":null,"abstract":"","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 3","pages":"Page 308"},"PeriodicalIF":0.0,"publicationDate":"1989-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(89)90024-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72240454","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":"Cellular polarity in cultured animal pole cells of Xenopus embryos","authors":"Mari Asada-Kubota","doi":"10.1016/0889-1605(89)90021-9","DOIUrl":"10.1016/0889-1605(89)90021-9","url":null,"abstract":"<div><p>The expression of intracellular and surface polarity in cultured animal pole cells of <em>Xenopus</em> embryos (stages 6, 8, and 10) was examined morphologically and immunocytochemically. When control embryos reached stage 23, daughter cells derived from a single or a few animal pole cells formed aggregates. Outer cells of the aggregates displayed intracellular and surface polarity and expressed an epidermis-specific antigen (XEPI-1) on the apical surface circumference, while these characteristics had not yet been established in the animal pole cells at the time of isolation. However, inner cells of the aggregates did not display the cellular polarity along an outer-inner axis of the aggregates and displayed the antigen randomly within the aggregates. These results indicate that the expression of cellular polarity in epidermal differentiation of <em>Xenopus</em> embryos <em>in vitro</em> depends on the position within the aggregates formed by daughter cells derived from isolated animal pole cells.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 3","pages":"Pages 265-275"},"PeriodicalIF":0.0,"publicationDate":"1989-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(89)90021-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13777218","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":"Abstract from the forty-first annual meeting of the Scandinavian Society for Electron Microscopy June 4–7, 1989, Uppsala, Sweden","authors":"","doi":"10.1016/0889-1605(89)90023-2","DOIUrl":"https://doi.org/10.1016/0889-1605(89)90023-2","url":null,"abstract":"","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 3","pages":"Pages 279-307"},"PeriodicalIF":0.0,"publicationDate":"1989-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(89)90023-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72240453","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":"Different aspects of tubulin polymerization in spermatids of cyprinodontidae (fish, teleost)","authors":"Omar Thiom Thiaw, Xavier Mattei","doi":"10.1016/0889-1605(89)90049-9","DOIUrl":"10.1016/0889-1605(89)90049-9","url":null,"abstract":"<div><p>Our study concerns 10 genera and 26 species of cyprinodontid fish. In the cytoplasm of spermatids tubulin polymerizes in various forms according to species. We have demonstrated the presence of classic microtubules with a diameter of 24 nm and also of tubules of smaller diameter (15 run) and greater diameter (30 to 50 nm). Microtubules are very numerous in the cytoplasm of certain species. They may be arranged without any order or form bundles which may contain several hundred parallel elements. They never form a manchette. In two species (<em>Aplocheilichthys normani</em> and <em>Epiplatys fasciolatus</em>) only spermatids that degenerate show this peculiarity. The microtubules present two kinds of decorations. The first type are small elements composed of MAP which enable two or more microtubules to link up. The second type are curved tubulin elements that give the microtubule that bear them the appearance of an incomplete doublet. Doublets and triplets may also be formed. Cyprinodontidae spermatocytes and spermatids probably synthesize a very large quantity of tubulin which polymerizes in certain species.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 2","pages":"Pages 122-131"},"PeriodicalIF":0.0,"publicationDate":"1989-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(89)90049-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53919314","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":"Le spermatozoïde de Ophidion sp. (poisson, téléostéen) : particularités ultrastructurales du flagelle","authors":"X. Mattei, D. Thiam, O. T. Thiaw","doi":"10.1016/0889-1605(89)90053-0","DOIUrl":"https://doi.org/10.1016/0889-1605(89)90053-0","url":null,"abstract":"","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 1","pages":"162-169"},"PeriodicalIF":0.0,"publicationDate":"1989-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(89)90053-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53919415","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":"Le spermatozoide de Ophidion sp. (Poisson, téléostéen): Particularités ultrastructurales du flagelle","authors":"Xavier Mattei , Djiby Thiam , Omar Thiom Thiaw","doi":"10.1016/0889-1605(89)90053-0","DOIUrl":"https://doi.org/10.1016/0889-1605(89)90053-0","url":null,"abstract":"<div><p>The spermatozoon of <em>Ophidion</em> sp. possesses an elongated nucleus 8 μm long, a short midpiece (0,6 μm), and a long flagellum (100 μm). The flagellar membrane extends in the form of two diametrically opposed sidefins. Evolving spermatids and spermatozoa are found in the lumen of the seminiferous tubes. The sections of flagella show filamentary and tubular elements disposed parallel to the axoneme microtubules. We have divided the flagella into three types. In type 1 the tip of the sidefins contains 20 to 30 filaments 5 run in diameter and between these and the axoneme 20 to 30 tubular elements 15 to 20 nm in diameter. Type 2 possesses a dense cytoplasm and a few tubular elements 10 nm in diameter disposed at the tip of the sidefins. Type 3 contains a cytoplasm which is not dense and in which we found polysaccharides and 1 to 8 tubular elements forming a palisade which lines the plasma membrane at the tip of the sidefins. We interpret these three types as three successive stages in the organization of the flagellum during spermiogenesis. Type 3 corresponds to the spermatic flagellum. These 10-nm-diameter tubules do not have the same chemical composition as the microtubules. Elements of the cytoskeleton serve as a support for the sidefins.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 2","pages":"Pages 162-169"},"PeriodicalIF":0.0,"publicationDate":"1989-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(89)90053-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72241847","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}
Aurelio Bairati, Federica Cheli, Antonella Oggioni, Laura Vitellaro-Zuccarello
{"title":"The head cartilage of cephalopods II. Ultrastructure of isolated native collagen fibrils and of polymeric aggregates obtained in Vitro: Comparison with the cartilage of mammals","authors":"Aurelio Bairati, Federica Cheli, Antonella Oggioni, Laura Vitellaro-Zuccarello","doi":"10.1016/0889-1605(89)90050-5","DOIUrl":"10.1016/0889-1605(89)90050-5","url":null,"abstract":"<div><p>Native collagen fibrils were isolated from cephalopod head cartilage and mammal hyaline cartilage. The analysis with TEM after positive and negative staining demonstrated that the fibrils have a periodic structure similar to that of fibrillar type I collagen of mammals. The banding pattern of polymeric forms (SLS, FLS) obtained <em>in vitro</em> from squid cartilage collagen was remarkably different from the analogous forms of mammal collagen types I and II.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 2","pages":"Pages 132-138"},"PeriodicalIF":0.0,"publicationDate":"1989-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(89)90050-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13777750","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":"Organization of the nuclear pore complex in Saccharomyces cerevisiae","authors":"Jerry Lynn Allen, Michael G. Douglas","doi":"10.1016/0889-1605(89)90047-5","DOIUrl":"10.1016/0889-1605(89)90047-5","url":null,"abstract":"<div><p>Fractions enriched for nuclear pore complexes (NPCs) have been isolated from <em>Saccharomyces cerevisiae</em>. The sequential extraction of nuclei with detergent, nucleases, and salt reveals an organization of the yeast NPC similar to other eukaryotes. Yeast NPCs contain a 30-nm “ring” structure not previously described in other organisms. This structure appears to organize 10-nm filaments into an assembly which exhibits an eight-fold rotational symmetry. Some proteins in the NPC fraction are capable of forming intermediate-sized filaments. These studies suggest that some component of the nuclear pore complex organizes an interaction between nuclear and cytoplasmic networks of intermediate filaments.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 2","pages":"Pages 95-108"},"PeriodicalIF":0.0,"publicationDate":"1989-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(89)90047-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13839557","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}
Akio Tsuboi , Harald Engelhardt , Ute Santarius , Norihiro Tsukagoshi , Shigezo Udaka , Wolfgang Baumeister
{"title":"Three-dimensional structure of the surface protein layer (MW layer) of Bacillus brevis 47","authors":"Akio Tsuboi , Harald Engelhardt , Ute Santarius , Norihiro Tsukagoshi , Shigezo Udaka , Wolfgang Baumeister","doi":"10.1016/0889-1605(89)90055-4","DOIUrl":"10.1016/0889-1605(89)90055-4","url":null,"abstract":"<div><p>The three-dimensional (3D) structure of one surface protein layer from <em>Bacillus brevis</em> 47, the middle wall (MW) layer, has been reconstructed from tilted-view electron micrographs after correlation averaging to a resolution of 2 nm. The MW layer has p6 symmetry with a center-to-center spacing of 18.3 nm and a minimum thickness of 5.5 nm. The reconstruction reveals a distinct domain structure: the heavier domain of six monomers jointly forms a massive core centered at the sixfold symmetry axis, and lighter domains interconnect adjacent unit cells. In addition, the larger domains collectively form a pore by making contact with each other towards the inner surface, while the smaller domains establish a second connectivity towards the outer surface of the S layer. The MW layer of <em>B. brevis</em> resembles the S layer of <em>Acetogenium kivui</em> in various aspects: they have very similar lattice parameters and highly reminiscent 3D structures; the pores penetrate through the whole core and appear to determine the porosity of the S layers.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 2","pages":"Pages 178-187"},"PeriodicalIF":0.0,"publicationDate":"1989-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(89)90055-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13778377","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":"Structural and material design of mature mineralized radula teeth of Patella vulgata (gastropoda)","authors":"Paul van der Wal","doi":"10.1016/0889-1605(89)90052-9","DOIUrl":"10.1016/0889-1605(89)90052-9","url":null,"abstract":"<div><p>The molluscan radula is a cutting apparatus employed in feeding. It is a toothed ribbon located in the mouth cavity. This study focuses on the characterization, organization, and hardness of the various components in full grown, mineralized, radula teeth of the common limpet <em>Patella vulgata</em>. Three major components are identified: Fibrous organic material, acicular crystals of goethite (α-FeOOH), and silica (SiO<sub>2</sub>). Each forms a coherent network intertwined with the other two. The goethite crystals lie parallel to the fibers in the organic framework. The orientations of fibers and crystals are described in detail. The hardness of the leading part, i.e., the part that leads in the cutting direction, is about twice the hardness in the trailing part. It is argued that this difference results from the greater compactness of the mineral matter in the leading part. The function of the tooth as a cutting device is discussed on the basis of the data presented in this study.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 2","pages":"Pages 147-161"},"PeriodicalIF":0.0,"publicationDate":"1989-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(89)90052-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53919350","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}