{"title":"Nuclear compactness as assessed by ferrtin permeation: A critical evaluation of the method","authors":"M. Carmo-Fonseca","doi":"10.1016/0889-1605(88)90077-8","DOIUrl":"https://doi.org/10.1016/0889-1605(88)90077-8","url":null,"abstract":"<div><p>The fracture-permeation method was applied in order to assess changes in nuclear compactness associated with different metabolic conditions. Rat ventral prostate was used as a model because transcription in the secretory cells of this organ is highly dependent on androgens. Two major problems that raise important questions concerning the validity of the method were encountered: (1) poorly preserved cells are massively permeated by ferritin and (2) within the same experimental group the permeation pattern was quite variable. In order to objectify such variability, the percentage of permeated nuclear cross-fractures was quantified. Different permeation patterns could be detected in nuclei from normal, castrated, and testosterone-treated prostatic cells, possibly reflecting changes in chromatin compactness.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"101 1","pages":"Pages 4-12"},"PeriodicalIF":0.0,"publicationDate":"1988-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90077-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72282760","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":"Polymerization of turtle α-macroglobulin through newly exposed sulfhydryls reveals the location of ex-thiolester bonds","authors":"Toshiya Osada, Masaaki Nishigai, Atsushi Ikai","doi":"10.1016/0889-1605(88)90082-1","DOIUrl":"https://doi.org/10.1016/0889-1605(88)90082-1","url":null,"abstract":"<div><p>Green turtle α-macroglobulin, which has previously been shown to contain thiolester bonds, formed linear polymers after being treated with proteinases. Biochemical analyses showed that the polymerization proceeded through disulfide-bond formation between monomers. The only sulfhydryl groups available for such polymerization after proteinase treatment were these created as the product of thiolester hydrolysis. Electron micrographs of polymers revealed H-shaped monomeric units aligned lengthwise in linear polymers. The average length per monomeric unit in the polymer estimated from the discrete distribution of polymer lengths was approximately 80% of the average length of free monomers, indicating that monomers overlapped each other within a region of about 4 nm. From such observations we concluded that the newly produced sulfhydryl groups were located on the four arms of the H-shaped molecule. The location of sulfhydryls can be taken as the site of the exposure of thiolesters which were originally sequestered in the hydrophobic interior of the molecule. Since the structure of turtle α-macroglobulin is very similar to that of human serum <em>α</em><sub>2</sub>-macroglobulin the results predict a similar location of sulfhydryls in human <em>α</em><sub>2</sub>-macroglobulin after proteinase treatment. The observed polymerization property is unique to sea turtle α-macroglobulin and has not been observed with human <em>α</em><sub>2</sub>-macroglobulin or other homologous proteins.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"101 1","pages":"Pages 62-74"},"PeriodicalIF":0.0,"publicationDate":"1988-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90082-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72282762","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":"Polarity and length of actin filaments at the fascia adherens of the cardiac intercalated disk","authors":"M. Yamaguchi, S. Yamano, M. Muguruma, R.M. Robson","doi":"10.1016/0889-1605(88)90040-7","DOIUrl":"10.1016/0889-1605(88)90040-7","url":null,"abstract":"<div><p>Digestion of canine and bovine intercalated disks with a calcium-activated protease (CAF) removes the electron-dense material similar to that found at the Z-line and presumably consisting primarily of α-actinin. The major filaments exposed by CAF are actin, andthe polarity is away from the intercalated disk, as was confirmed by decoration with heavy meromyosin. The length of actin filaments associated with the fascia adherens region at the concave region is 1.2- to 2.2-fold that of actin filaments (I-filaments) in the sarcomere and varies depending on the interdigitation of the membrane at the cell junction. Actin filaments at the intercalated disk seem to be attached (or very close) to the membrane in a direct, rather than looping, manner.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"100 3","pages":"Pages 235-244"},"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)90040-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13991164","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":"Author index for volume 100","authors":"","doi":"10.1016/0889-1605(88)90046-8","DOIUrl":"https://doi.org/10.1016/0889-1605(88)90046-8","url":null,"abstract":"","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"100 3","pages":"Page 308"},"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)90046-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72280771","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":"Plasmalemma deposits in tissues infected with lettuce infectious yellows virus","authors":"Robin L. Pinto, Lynn L. Hoefert, Gail L. Fail","doi":"10.1016/0889-1605(88)90041-9","DOIUrl":"10.1016/0889-1605(88)90041-9","url":null,"abstract":"<div><p>Lettuce infectious yellows virus (LIYV) is a phloem-associated virus that is whitefly-transmitted. The physical characteristics and cytopathology of this virus are similar to those of other members of the Closterovirus group. One unique ultrastructural effect of the infection is the formation of conical deposits on the plasmalemmae of phloem parenchyma cells. The electron-dense deposits are osmiophilic stacks of membrane lamellae spaced at 7 nm. Flexuous virions extend between these deposits from the cytoplasm through plasmodesmata and into adjacent sieve elements. We hypothesize that these plasmalemma deposits may facilitate movement of LIYV into other phloem parenchyma cells for further replication or into sieve elements for rapid transport throughout the host.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"100 3","pages":"Pages 245-254"},"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)90041-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53916830","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":"Intracellular crystal formation in Bacteroides nodosus","authors":"Paul M. Hine","doi":"10.1016/0889-1605(88)90043-2","DOIUrl":"10.1016/0889-1605(88)90043-2","url":null,"abstract":"<div><p>An intracellular crystalline structure was found in at least two strains of <em>Bacteroides nodosus</em>. The inclusion appeared to be associated with good growth of the organism under optimum conditions following selective passage of rough colonies containing highly fimbriate cells. Several morphological forms of the inclusion were noted. Indiscriminate subculture of crystal-forming cultures led to the loss of this particular property indicating a genetically controlled system of either bacterial or bacteriophage origin.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"100 3","pages":"Pages 263-268"},"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)90043-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13991165","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":"Sequential appearance of capsid protein and cylindrical inclusion protein in root-tip cells following infection with passion fruit woodiness virus","authors":"Na-Sheng Lin , Nancy Wang , Yau-Heiu Hsu","doi":"10.1016/0889-1605(88)90037-7","DOIUrl":"10.1016/0889-1605(88)90037-7","url":null,"abstract":"<div><p>Early events in passion fruit woodiness virus (PWV) infection of root-tip cells of tobacco (<em>Nicotiana benthamiana</em>) were examined by immunoelectron microscopy with antisera prepared specifically against the capsid protein (CP) and cylindrical inclusion protein (CIP) of the virus. Capsid protein was first detected on the cytoplasmic virus-specific vesicles coincident with first appearance of virions, but virions were not visible at every location that was stained. Early configurations of cylindrical inclusions (CI) were first observed on the surface of endoplasmic reticulum. At a later stage when aggregates of PWV were present, PWV virions were intimately associated with CIs either within the cytoplasm or attached perpendicularly to the cell wall. Most PWV aggregates were bound to cytoplasmic membranous structures in cells at a late stage of infection. Antiserum against CP partially reacted with CIs at advanced stages of infection. On the other hand, antiserum against CIP reacted only with CIs, but not with PWV virions. Both CP and CIP could also be detected in the plasmodesmata of infected cells.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"100 3","pages":"Pages 201-211"},"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)90037-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53916799","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 fortieth anniversary meeting of the scandinavian society for electron microscopy","authors":"","doi":"10.1016/0889-1605(88)90045-6","DOIUrl":"https://doi.org/10.1016/0889-1605(88)90045-6","url":null,"abstract":"","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"100 3","pages":"Pages 278-307"},"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)90045-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72245412","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}
Shinsuke Kanamura, Kazuo Kanai, Youko Asaka, Jun Watanabe
{"title":"Inhibitory effect of phenobarbital on peroxisome biogenesis in mouse hepatocytes","authors":"Shinsuke Kanamura, Kazuo Kanai, Youko Asaka, Jun Watanabe","doi":"10.1016/0889-1605(88)90044-4","DOIUrl":"10.1016/0889-1605(88)90044-4","url":null,"abstract":"<div><p>Peroxisomes in hepatocytes from mice administered 35, 50, or 100 mg/kg of phenobarbital (PB) were analyzed by quantitative electron microscopy. In perivenular hepatocytes, the volume of peroxisomes per unit cytoplasmic volume decreased to 78 or 57% of that of control animals by administration of 50 or 100 mg/kg. Their average volume also decreased to 78 or 64% of that in control animals in animals injected with 35 or 50 mg/kg. Further, cytochemical catalase activity appeared decreased in peroxisomes of hepatocytes of this zone after administration of 50 or 100 mg/kg. These suggest an inhibitory action of PB administration of biogenesis of peroxisomes in perivenular hepatocytes. In periportal hepatocytes, however, the volume density, average volume, and cytochemical catalase activity of peroxisomes did not change by administration of any doses of PB. Thus, PB administration appears to produce no inhibitory effect on the peroxisome biogenesis in periportal hepatocytes. On the other hand, the number of peroxisomes per unit cyto-plasmic volume increased in both periportal and perivenular hepatocytes in animals injected with 50 mg/kg, although it returned to the level of control animals by injection of 100 mg/kg. The inhibitory effect of PB on the peroxisome neogenesis in perivenular hepatocytes may be related to the marked smooth endoplasmic reticulum proliferation by administration of this drug.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"100 3","pages":"Pages 269-277"},"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)90044-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14372009","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":"Vitreous humor of chicken contains two fibrillar systems: An analysis of their structure","authors":"David W. Wright, Richard Mayne","doi":"10.1016/0889-1605(88)90039-0","DOIUrl":"10.1016/0889-1605(88)90039-0","url":null,"abstract":"<div><p>An analysis of the structure of chicken vitreous humor after brief homogenization of the tissue was performed. Electron micrographs prepared after rotary shadowing with platinum showed the presence of two distinct fibrils. The collagen fibril was coated by glycosaminoglycan which could be removed by chondroitinase ABC digestion. In addition, individual molecules of tenascin were observed wrapped around some of the collagen fibrils. A second beaded fibril was present and several fine filaments were observed to extend from each bead. The beaded fibril is formed by the overlap of these filaments, and beaded fibrils were observed in either a “closed” or an “open” form dependent on whether all of the filaments are brought together to form the overlap. A schematic diagram is presented for the structure of the beaded fibril. The potential relationship of the beaded fibril to the zonular fibrils and the elastin microfibrils is briefly discussed.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"100 3","pages":"Pages 224-234"},"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)90039-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13616306","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}