{"title":"Lithium-induced structural changes in the cortical distal nephron localized by computer-assisted three-dimensional reconstruction","authors":"Jens Dørup , Peter D. Ottosen , Sten Christensen","doi":"10.1016/0889-1605(88)90038-9","DOIUrl":"10.1016/0889-1605(88)90038-9","url":null,"abstract":"<div><p>Lithium treatment is known to cause tubule dilation in distal nephron segments both in rat and in man. However, due to the heterogeneous cell composition of the distal nephron and the cellular changes following lithium treatment, it has been difficult to identify the structurally changed segments. In this study we have therefore applied computer-assisted reconstruction of cortical distal nephron segments. Tubule dilation was demonstrated in connecting and initial collecting tubules and in the first part of cortical collecting ducts (CCD) whereas it was absent from distal straight and distal convoluted tubules. Principal cells (P cells) in the CCD showed swelling of the cytoplasm, accumulation of actin-like microfilaments, and abnormal arrangements of basolateral membranes. Connecting tubule cells (CNT cells) showed similar but less pronounced changes. Intercalated cells (I cells) showed an accumulation of vesicles in the apical cytoplasm and a reduced luminal surface area. Lesions in P and CNT cells may, at least in part, explain the diabetes insipidus and sodium loss found during lithium treatment. Proton secretion in I cells is probably mediated by an ATPase present in the luminal membrane. The reduction in area of this membrane may explain why lithium-treated animals have a lowered ability to excrete an acid load.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"100 3","pages":"Pages 212-223"},"PeriodicalIF":0.0,"publicationDate":"1988-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90038-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14372008","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":"Further evidence for the correlation between the primary structure and the stain exclusion banding pattern of the segment-long-spacing crystallites of collagen","authors":"Kunihiko Kobayashi , Yoko Hashimoto , Taro Hayakawa , Takeshi Hoshino","doi":"10.1016/0889-1605(88)90042-0","DOIUrl":"10.1016/0889-1605(88)90042-0","url":null,"abstract":"<div><p>Recently, we have noted the direct correlation between the primary structure of type I collagen and the electron microscopical banding pattern of the negatively stained segment-long-spacing (SLS) crystallites (<span>K. Kobayashi, T. Ito, and T. Hoshino (1986)</span>, <em>J. Electr. Microsc.</em> <strong>35</strong>, 272–275). In this paper, we examined the correlation in the other types of collagen. Unstained light bands (stain excluding bands) of the negatively stained SLSs of type II and type III collagens were located at the clusters of large hydrophobic amino acid residues along the respective molecules. Photographic averaging of the pattern improved the visual comparison of the correlation. We also noted a few occasions of discrepancy from the above-mentioned correlation. Preliminary computer simulation experiments revealed that, among amino acid parameters so far reported, only the hydrophobicity values of <span>G. D. Rose and S. Roy (1980)</span>, <em>Proc. Natl. Acad. Sci. USA</em> <strong>77</strong>, 4643–4647) explained the ability of amino acids for the negative staining (stain exclusion) of the collagen SLSs.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"100 3","pages":"Pages 255-262"},"PeriodicalIF":0.0,"publicationDate":"1988-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90042-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13616307","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}
Magda de Eguileor, Franco Cotelli, Roberto Valvassori, Maurizio Brivio, Laura di Lernia
{"title":"Functional significance of intermediate filament meshwork in annelid helical muscles","authors":"Magda de Eguileor, Franco Cotelli, Roberto Valvassori, Maurizio Brivio, Laura di Lernia","doi":"10.1016/0889-1605(88)90025-0","DOIUrl":"10.1016/0889-1605(88)90025-0","url":null,"abstract":"<div><p>A desmin-like protein of mol wt 54 kDa was identified in the body wall muscles of some Polychaeta, Oligochaeta, and Hirudinea utilizing SDS-PAGE followed by blot and screening with a vertebrate anti-desmin antibody. The pattern in immunofluorescence is compared to electron micrographs where several bundles of filamentous structures are clearly identifiable. These bundles are unevenly arranged in round or flattened circomyarian fibers and sometimes clearly connect <em>Z</em> elements with hemidesmosomes. The mechanism of intermediate filaments as a functional integration in muscle fibers is analyzed and a possible role as a block to superelongation typical of helical muscles is discussed.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"100 2","pages":"Pages 183-193"},"PeriodicalIF":0.0,"publicationDate":"1988-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90025-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14353742","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}
Chung-Fu Chang , Debby A. Rankert , Tzyy-Wen Jeng , David G. Morgan, Michael F. Schmid , Wah Chiu
{"title":"Cryo electron microscopy of unstained, unfixed RecA-cssDNA complexes","authors":"Chung-Fu Chang , Debby A. Rankert , Tzyy-Wen Jeng , David G. Morgan, Michael F. Schmid , Wah Chiu","doi":"10.1016/0889-1605(88)90023-7","DOIUrl":"10.1016/0889-1605(88)90023-7","url":null,"abstract":"<div><p>Complexes of RecA protein with φX174 circular single-stranded DNA (cssDNA) with and without ATPγS were rapidly frozen and embedded in a thin layer of vitreous ice. The electron micrographs of these frozen-hydrated complexes clearly show visible helicity. Quantitative image analyses of these micrographs reveal the helical pitch and the axial rise between DNA bases of these complexes. Both of these structural parameters of RecA-cssDNA complexes increase significantly when ATPγS is present. These observations agree qualitatively but not quantitatively with those from negative stained specimens and confirm the general model that the interactions among RecA molecules and between RecA and DNA could change according to the functional states of the RecA-cssDNA complex.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"100 2","pages":"Pages 166-172"},"PeriodicalIF":0.0,"publicationDate":"1988-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90023-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14198186","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":"Concanavalin A binding sites on the surface of Drosophila melanogaster sperm: A fluorescence and ultrastructural study","authors":"Maria Elisa Perotti, Antonella Riva","doi":"10.1016/0889-1605(88)90024-9","DOIUrl":"10.1016/0889-1605(88)90024-9","url":null,"abstract":"<div><p>The distribution of α-<span>d</span>-mannose/α-<span>d</span>-glucose terminal residues in the plasma membrane of <em>Drosophila melanogaster</em> spermatozoon has been investigated by fluorescence and electron microscopy using concanavalin A (Con A) labeling. The results indicate the presence of distinct domains on the sperm surface. Intense binding of Con A to the plasma membrane is highly restricted to the acrosomal region and to the endpiece of the tail. In the former, Con A receptors are not homogeneously distributed, suggesting the presence of microdomains in the acrosomal area. The main part of the tail contains very few Con A binding sites, which are confined to specific areas of the membrane. The sperm surface overlying the nucleus is completely negative. The labeling pattern is unchanged after storage in the female before fertilization. A preliminary analysis of the surface of mature oocytes using fluorochrome-conjugated horseradish peroxidase indicates that <span>d</span>-mannose binding molecules are specifically associated with the chorion of the micropyle anterior part, which might therefore be the site of a preliminary interaction between egg and spermatozoon.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"100 2","pages":"Pages 173-182"},"PeriodicalIF":0.0,"publicationDate":"1988-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90024-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14277162","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":"The projection structure of α-toxin from Staphylococcus aureus in human platelet membranes as analyzed by electron microscopy and image processing","authors":"A. Olofsson, U. Kavéus, M. Thelestam , H. Hebert","doi":"10.1016/0889-1605(88)90026-2","DOIUrl":"https://doi.org/10.1016/0889-1605(88)90026-2","url":null,"abstract":"<div><p>Most strains of <em>Staphylococcus aureus</em> produce α-toxin, a 33-kDa membrane active protein which is considered to be an important virulence factor of this bacterium. When α-toxin interacts with membranes an oligomeric form of the toxin can be seen by electron microscopy as characteristic ring structures in the membrane. A two-dimensional study of these annular structures, incorporated in membranes of human platelets, was performed, introducing a partly new method for rotational alignment of individual particles. It is shown that the averaged oligomer consists of six subunits. At neutral pH the outer diameter of the ring is about 75 Å. The stain-filled pore or cavity in the center has a diameter of about 25 Å. The size of the hexamer is increased if the pH is lowered.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"100 2","pages":"Pages 194-200"},"PeriodicalIF":0.0,"publicationDate":"1988-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90026-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72240445","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":"An electron microscopic study of cauliflower mosaic virus-induced viroplasms: Unusual structures within the viroplasm matrix with possible functional significance in the viral replication cycle","authors":"D. Rodríguez, D. López-Abella, J.R. Díaz-Ruiz","doi":"10.1016/0889-1605(88)90019-5","DOIUrl":"10.1016/0889-1605(88)90019-5","url":null,"abstract":"<div><p>A detailed ultrastructural study has been performed on viroplasms induced by two Cauliflower mosaic virus (CaMV) strains. Thin-sectioning and negative-staining electron microscopy techniques were both used. Examination of purified viroplasms by negative staining has revealed additional details in their ultrastructure. This analysis has consistently revealed a unique, previously undescribed, arc-shaped structure within the viroplasm matrix. Its presence is discussed in relation to a possible functional significance in the CaMV replication cycle.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"100 2","pages":"Pages 118-125"},"PeriodicalIF":0.0,"publicationDate":"1988-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90019-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53916579","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}
George Karkavelas , Nicholas A. Kefalides , Peter S. Amenta , Antonio Martinez-Hernandez
{"title":"Comparative ultrastructural localization of collagen types III, IV, VI and laminin in rat uterus and kidney","authors":"George Karkavelas , Nicholas A. Kefalides , Peter S. Amenta , Antonio Martinez-Hernandez","doi":"10.1016/0889-1605(88)90021-3","DOIUrl":"10.1016/0889-1605(88)90021-3","url":null,"abstract":"<div><p>Antibodies against collagen types III and VI have been localized by electron immunohistochemistry with two different techniques in normal rat uterus and kidney. Antibodies directed against two components of the extracellular matrix with known localization, laminin and type IV collagen, were used as controls for the specificity of the localization. The results demonstrate that types III and VI are found in the interstitium as fine (10- to 15-nm), beaded fibrils and filaments (6- to 10-nm), respectively. Both are often found associated with thick, crossbanded type I collagen fibers (30- to 35-nm) and occasionally associated with some basement membranes adjacent to the interstitium. Further, the findings suggest that collagens III and VI may connect the various components of the extracellular matrix, such as type I fibers with basement membranes and other structures, thus forming an integrated functional unit.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"100 2","pages":"Pages 137-155"},"PeriodicalIF":0.0,"publicationDate":"1988-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90021-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14353741","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}
Z. Xu , B.A. Afzelius , L. Stigendal , A.-C. Teger-Nilsson
{"title":"Ultrastructure and function of thrombocytes in a family with congenital bleeding tendency","authors":"Z. Xu , B.A. Afzelius , L. Stigendal , A.-C. Teger-Nilsson","doi":"10.1016/0889-1605(88)90020-1","DOIUrl":"10.1016/0889-1605(88)90020-1","url":null,"abstract":"<div><p>Freshly isolated blood from controls and from three members of a family with congenital bleeding tendency were examined with respect to ultrastructure of platelets. The fixation protocol, which included tannic acid, permitted the visualization of substructures in the marginal bundle. Whereas nearly all platelets from the controls had a discoid shape, those from one of the patients (mother of the other two cases) were mostly flat or else roundish with two or three marginal bundles in different orientations. One portion of the thrombocyte fraction of each person was briefly exposed to adenosine diphosphate in order to activate the platelets and thereby to induce shape changes. Most platelets from the controls reacted as expected by rounding up and by projecting some pseudopods. A certain percentage (between 10 and 20%) of the microtubules in these activated platelets had 14 or even 15 protofilaments. The platelets from patients (and in particular the mother) either reacted by an abnormal bulging of the cytoplasm or did not react visibly at all. The microtubules retained their 13-subunit composition or in the abnormally reacted ones often had an open C-shaped cross-sectional profile. The bleeding tendency in this family might be due to a defect in the cytoskeleton of the platelet making it unable to react properly to stimuli.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"100 2","pages":"Pages 126-136"},"PeriodicalIF":0.0,"publicationDate":"1988-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90020-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14353740","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":"Nodulous corpuscles and mitochondrial inclusions in sertoli cells of deer hybrids","authors":"Francis Hrudka","doi":"10.1016/0889-1605(88)90018-3","DOIUrl":"10.1016/0889-1605(88)90018-3","url":null,"abstract":"<div><p>Unusual transformations of endoplasmic reticulum and mitochondria were identified in the Sertoli cells of deer hybrids. A portion of the mitochondrial population was converted from the common, flexible mitochondrial form into stiff rods, with an increased volume of the matrix and relative paucity of cristae. The matrix displayed arrays of tubuloid elements or precursors at various stages of assembly. The second and more conspicuous adaptation concerned the agranular endoplasmic reticulum, which frequently transformed into oval or elongate, often interconnected bodies. These bodies consisted of a dozen or more concentrically arranged fenestrated cisternae and a variable amount of glycogen in between. An integral and distinctive feature of the cisternous bodies was nodes, together constituting the so-called nodulous corpuscles (NC). The nodes appeared as a dense meshwork or lattice, which has the potential to generate a new set of cisternae and NC that interconnect into a chain or tridimensional complex. The course of NC evolution from precursors to mature complexes is proposed. Both organelle adaptations occurred independently and in only Sertoli cells. They are believed to be a product of hybridization in deer.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"100 2","pages":"Pages 107-117"},"PeriodicalIF":0.0,"publicationDate":"1988-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90018-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14353084","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}