Elisabeth Skriver , Arvid B. Maunsbach , Hans Hebert , Georgios Scheiner-bobis , Wilhelm Schoner
{"title":"Two-dimensional crystalline arrays of Na,K-ATPase with new subunit interactions induced by cobalt-tetrammine-ATP","authors":"Elisabeth Skriver , Arvid B. Maunsbach , Hans Hebert , Georgios Scheiner-bobis , Wilhelm Schoner","doi":"10.1016/0889-1605(89)90013-X","DOIUrl":"10.1016/0889-1605(89)90013-X","url":null,"abstract":"<div><p>Purified membrane-bound Na,K-ATPase incubated with cobalt-tetrammine-ATP [Co(NH<sub>3</sub>)<sub>4</sub>ATP], which is a stable MgATP complex analog, shows two new types of membrane crystals, a new p21 form and a p4 form. The building blocks of the crystalline arrays correspond to (<em>αβ</em>)<sub>2</sub> dimers of the enzyme protein suggesting that α-α interaction may be important in the pumping process.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 3","pages":"Pages 189-195"},"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)90013-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13703995","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":"Insulin absorption in renal proximal tubules: A quantitative immunocytochemical study","authors":"Søren Nielsen , Erik Ilsø Christensen","doi":"10.1016/0889-1605(89)90015-3","DOIUrl":"10.1016/0889-1605(89)90015-3","url":null,"abstract":"<div><p>The purposes of the present study are mainly biological concerning proximal tubular handling of insulin: we will study the intracellular transport to subcellular compartments involved in insulin degradation, the specificity and saturability of the luminal endocytic absorption of insulin, the visualization of transtubular transport, and finally, if possible, the evaluation of the relative distribution (accumulation) of insulin in endocytic vacuoles and lysosomes. The second part is methodological: application of quantitative immunocytochemistry to endocytosis, quantitation of the effect of particle size and antigen density on labeling density on tissue sections, labeling at very low antigen densities, and effect of fish gelatin on background. Isolated renal proximal tubules were perfused with native insulin, <sup>125</sup>I-insulin, or [leucine<sup>B-25</sup>]-insulin (2% receptor-binding ability and full immunoreactivity) or exposed to native insulin from the basolateral membranes. In conclusion, the luminal uptake of insulin is of low specificity, as native and [leucine<sup>B-25</sup>]-insulin were accumulated to the same extent. Endocytic uptake is of high capacity and the mechanism is saturable. Insulin accumulated in endocytic vacuoles and lysosomes, thus following the classical degradation pathway. No other subcellular compartment is associated with insulin degradation. It was not possible to detect the basolateral uptake, indicating loss of immunoreactivity after binding to its receptor. Absolute quantitative immunocytochemistry is applicable in studying endocytosis. The labeling density increases nonproportionally with antigen density probably caused by steric hindrances. Reduction of the particle size (16 to 6 nm) increased the labeling density 17.6 times.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 3","pages":"Pages 205-220"},"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)90015-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13840263","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":"Quantitation of corneal fibril diameters from bony fish using low temperature preparative methods","authors":"Alan S. Craig , Dav1d A.D. Parry","doi":"10.1016/0889-1605(89)90022-0","DOIUrl":"10.1016/0889-1605(89)90022-0","url":null,"abstract":"<div><p>Low-temperature dehydration and embedding techniques have been used to preserve the transverse structure of corneal collagen fibrils from nine bony fish. The diameters measured all lie close to a value of 25.5 nm, in contrast to the smaller (and more diverse) diameters measured from “conventionally” prepared controls. The results are consistent with our earlier studies on the corneas from mammals, amphibians, birds, reptiles, and cartilaginous and bony fish which showed that the collagen fibrils from the bony fish were significantly smaller than those from animals of the other vertebrate classes. Thus, on the basis of the enhanced ability of the low-temperature preparative techniques to preserve collagen fibril structure the “<em>in vivo</em>” corneal collagen fibril diameters have been revised from 17 to 25.5 nm for bony fish (this work) and from 25 to 36 nm for all other classes of vertebrates (our previous work).</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 3","pages":"Pages 276-278"},"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)90022-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53918036","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":"Intramitochondrial helical filaments in medullary tubules of the rat kidney","authors":"Hiroyuki Sasaki, Teruo Suzuki","doi":"10.1016/0889-1605(89)90017-7","DOIUrl":"10.1016/0889-1605(89)90017-7","url":null,"abstract":"<div><p>Characteristic helical filaments were frequently found within dilated intracristal spaces of the mitochondria in epithelial cells of renal medullary tubules of normal rats of both sexes. These filaments had a helical structure with right-handed rotation. The approximate dimensions were 4 nm in thickness, 13 nm in helical diameter, and 16 nm in pitch. The filaments were common in all strains of rats examined in the present study but not in animals of other species including mice, guinea pigs, golden hamsters, Mongolian gerbils, house musk shrews, and rabbits. In Sprague-Dawley strain rats, the filaments were found not only in animals of all ages but also in 6-week-old germ-free animals and fetuses at the 18th day of gestation. Even in the same rats, the helical filaments were completely absent in the cortical tubules.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 3","pages":"Pages 229-239"},"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)90017-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13703996","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}
Gabriella Pasqua , Francesca Dalla Vecchia , Nicoletta Rascio , Giorgio Casadorot
{"title":"Influence of exogenous sucrose on the greening of oat","authors":"Gabriella Pasqua , Francesca Dalla Vecchia , Nicoletta Rascio , Giorgio Casadorot","doi":"10.1016/0889-1605(89)90019-0","DOIUrl":"10.1016/0889-1605(89)90019-0","url":null,"abstract":"<div><p>The greening of roots and leaves has been studied in whole oat seedlings grown on White's medium either with or without 2% sucrose. The added nutrient promotes chlorophyll synthesis and chloroplast differentiation in the roots. Yet it manifests a negative effect in the foliar tissues where it accelerates the decline in chlorophyll as well as the chloroplast ultrastructural alterations usually associated with senescence. The negative effect of the nutrient in the leaves is probably a consequence of the addition of exogenous sucrose to the endogenous sugars produced by photosynthesis. The foliar tissues would therefore be in the presence of high sucrose concentrations, which are known to be harmful for the photosynthetic apparatus. SDS-PAGE analysis of thylakoid polypeptides from root and leaf chloroplasts has revealed organ-specific differences in the electrophoretic patterns.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 3","pages":"Pages 249-254"},"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)90019-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53917989","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}
Mary G. Hamilton , Theodore T. Herskovits , Paul S. Furcinitti , Joseph S. Wall
{"title":"Scanning transmission electron microscopic study of molluscan hemocyanins in various aggregation states: comparison with light scattering molecular weights","authors":"Mary G. Hamilton , Theodore T. Herskovits , Paul S. Furcinitti , Joseph S. Wall","doi":"10.1016/0889-1605(89)90016-5","DOIUrl":"10.1016/0889-1605(89)90016-5","url":null,"abstract":"<div><p>The masses of individual particles of the hemocyanins of six members of two molluscan classes, Polyplacophora and Gastropods, have been determined by scanning transmission electron microscopy (STEM) of unstained specimens dried from the frozen state. The decameric hemocyanins of two chitons, <em>Mopalia muscosa</em> and <em>Stenoplax conapicua</em>, had masses of 4.20 ± 0.18 and 4.47 ± 0.56 MDa, respectively; the didecameric hemocyanins of two gastropods, <em>Fasciolaria tulipa</em> and <em>Pleuroploca gigantea</em>, had masses of 8.67 ± 0.44 and 8.96 ± 0.39 MDa, respectively; and the tridecameric hemocyanin of <em>Lunatia heros</em> had a mass of 13.50 ± 0.44 MDa. The STEM values were in close agreement with those obtained by light scattering measurements of the same samples in solution. For <em>Busycon centrarium</em>, a gastropod with a multidecameric hemocyanin, nine size classes from didecamers to decadecamers with masses that corresponded to multiples of a basic decamer (4.4 MDa) were detected. The appearance of unstained specimens of the cylindrical particles differs from negatively stained specimens. Viewed end-on the cylinders show no internal structure, but in well-preserved specimens cavities are apparent in the side views of the cylinders that resemble those seen in negatively stained specimens. Although they lack the characteristic “tiered” appearance, the number of decameric units can be counted and their arrangement within the particle seen.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 3","pages":"Pages 221-228"},"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)90016-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13777216","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}
Muhsin Özel , Stefan Hℷlund , Hans R. Gelderblom , Bror Morein
{"title":"Quaternary structure of the immunostimulating complex (Iscom)","authors":"Muhsin Özel , Stefan Hℷlund , Hans R. Gelderblom , Bror Morein","doi":"10.1016/0889-1605(89)90018-9","DOIUrl":"10.1016/0889-1605(89)90018-9","url":null,"abstract":"<div><p>Proteins of either HIV-1, hepatitis B, or rabies virus were incorporated with the adjuvant substance Quil A and cholesterol into the immunostimulating complex: iscom. Formation and symmetry of this regular complex were analyzed by electron microscopy. Micellar structures with a diameter of about 12 nm, occasionally with a 7-nm stain-filled center, were formed in a 0.03% water suspension of Quil A. Cavities or holes appeared in the smooth structures of cholesterol upon the addition ofing Quil A, and after mixing Quil A and cholesterol 1:1 fragile and flattened structures of matrix were produced withth a diameter of about 40 nm. By freeze-drying the matrix was preserved as a cage-like, isometric particle. Stable iscom particles composed of Quil A, cholesterol, and selected viral proteins had an approximate diameter of 32 nm. The particles had an uniform, cage-like structure, exhibiting icosahedral symmetry, irrespective of the viral proteins incorporated. Tilting experiments and rotational image analysis indicated that the iscoms were composed of 20 morphological subunits assembled in a pentagonal dodecahedron with a hole on each of the 12 pentagonal faces. The symmetrical shape of the iscom might explain both its remarkable stability and its capacity to efficiently present antigens to the immune system.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 3","pages":"Pages 240-248"},"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)90018-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13777217","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}
Kyung-Soo Kim , Rodrigo A. Valverde , J. Allan Dodds
{"title":"Cytopathology of satellite tobacco mosaic virus and its helper virus in tobacco","authors":"Kyung-Soo Kim , Rodrigo A. Valverde , J. Allan Dodds","doi":"10.1016/0889-1605(89)90014-1","DOIUrl":"10.1016/0889-1605(89)90014-1","url":null,"abstract":"<div><p>Ultrastructural responses of tobacco cells infected with a newly discovered satellite virus (STMV) that has an isometric morphology and is associated with rigid rodshaped tobacco mosaic virus (TMV) were studied <em>in situ</em>. In cells infected with TMV alone,TMV particles occurred as crystalline arrays in the cytoplasm and were usually associated with TMV-characteristic X bodies. In cells infected with both TMV and STMV, particles of STMV occurred only in cells that contained TMV particles, which suggests a correlation between the satellite and helper virus presence. However, the replication and/or accumulation sites of STMV appear to be independent from its helper virus. Unlike TMV particles, STMV particles were associated with several cytopathic structures such as granular inclusions, membranous vesicles of 50–80 nm, and myelin-like bodies which were all bounded by a single common membrane, No X bodies occurred in cells containing STMV particles, and the mitochondria possessed abnormal tubular structures containing flocculent material.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 3","pages":"Pages 196-204"},"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)90014-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53917960","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}
John W. Austin , Andreas Engel , R.G.E. Murray , Ueli Aeb
{"title":"Structural analysis of the S-Layer of Lampropedia hyalina","authors":"John W. Austin , Andreas Engel , R.G.E. Murray , Ueli Aeb","doi":"10.1016/0889-1605(89)90020-7","DOIUrl":"10.1016/0889-1605(89)90020-7","url":null,"abstract":"<div><p>The two-dimensional (2D) structure of the regularly structured surface layer (S-layer) of the gram-negative eubacterium <em>Lampropedia hyalina</em> has been determined at the molecular level to a nominal resolution of 2.1 nm by transmission electron microscopy and digital image processing. The inner, or “perforate,” layer consists of dimeric block-shaped units located at two-fold symmetry axes. These morphological dimers associate around three-fold symmetry axes to form a continuous layer with p6 symmetry and a lattice constant of 14.6 ± 0.4 nm. Scanning transmission electron microscopy (STEM) yields a mass-per-area (MPA) value for the perforate layer of 3.5 kDa/nm<sup>2</sup>. The outer, or “punctate,” layer is composed of long, roughly cylindrical units centered on six-fold symmetry axes, which are connected by six fine linking arms joining at the three-fold symmetry axes to create a hexagonal layer with a lattice constant of 25.6 ± 0.5 nm. The MPA of the “composite”-i.e., perforate plus punctate—layer is 10.2 kDa/nm<sup>2</sup>.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 3","pages":"Pages 255-264"},"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)90020-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53918015","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":"Cumulative subject index for volume 102","authors":"","doi":"10.1016/0889-1605(89)90025-6","DOIUrl":"https://doi.org/10.1016/0889-1605(89)90025-6","url":null,"abstract":"","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"102 3","pages":"Pages 309-312"},"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)90025-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72240452","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}