Journal of ultrastructure and molecular structure research最新文献

{"title":"Spermatozoa of megaloptera and raphidioptera (insecta, neuropteroidea)","authors":"B.A. Afzelius ,&nbsp;R. Dallai","doi":"10.1016/0889-1605(88)90008-0","DOIUrl":"10.1016/0889-1605(88)90008-0","url":null,"abstract":"<div><p>Spermatozoa from representatives of two minor insect orders, <em>Sialis lutaria</em>, order Megaloptera, and <em>Raphidia</em> spec., order Raphidioptera, have been examined by electron microscopy. Spermatozoa from both species were seen to have an elongated sperm head and a sperm tail containing axoneme, two mitochondrial derivatives of equal sizes, and two accessory bodies. The acrosome in <em>Sialis</em> has a bilateral symmetry in cross section and is fairly complex in that it has both a thin anterior extra-acrosomal layer, an acrosomal vesicle, and a subacrosomal space. In the acrosomal vesicle there is a filament bundle that makes a U-turn. The centriolar microtubules fray out to surround an attenuated posterior portion of the nucleus. The spermatozoa of <em>Raphidia</em> are very long and thin and have a rather simple acrosome. In this species, too, the microtubules of the centrioles surround the posterior, 1-μm-long, portion of the nucleus. This configuration of the centriolar microtubules is not shared by the other examined insects of the neuropteroid superorder and may be a synapomorphic feature. The data are thus consistent with the opinion that Megaloptera plus Raphidioptera form a sister group to the Neuroptera (Planipennia).</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"101 2","pages":"Pages 185-191"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90008-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53916408","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 volumes 98–101","authors":"","doi":"10.1016/0889-1605(88)90017-1","DOIUrl":"https://doi.org/10.1016/0889-1605(88)90017-1","url":null,"abstract":"","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"101 2","pages":"Pages 253-267"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90017-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72241456","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":"Freeze fracture of sperm and vegetative cells in Zea mays pollen","authors":"D. Southworth ,&nbsp;K.A. Platt-Aloia ,&nbsp;W.W. Thomson","doi":"10.1016/0889-1605(88)90006-7","DOIUrl":"10.1016/0889-1605(88)90006-7","url":null,"abstract":"<div><p>In freeze-fractured pollen of <em>Zea mays</em>, sperm cells were surrounded by concentric paired membranes. The sperm nucleus lacked nuclear pores. Sperm cytoplasm included mitochondria, endoplasmic reticulum, and several classes of single-membrane vesicles. No distinctive fracture patterns were observed on any sperm cell membranes.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"101 2","pages":"Pages 165-172"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90006-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53916124","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":"Cytoskeletal bridges between organelles in sperm flagellum of Triatoma infestans (hemiptera, reduviidae)","authors":"Heidi Dolder","doi":"10.1016/0889-1605(88)90005-5","DOIUrl":"10.1016/0889-1605(88)90005-5","url":null,"abstract":"<div><p>Bridge-like connections between axoneme and mitochondrial derivatives of <em>Triatoma infestans</em> are identical to those of other Heteropterans where they have been identified as a typical characteristic of the spermatozoa of this group of insects. Whole-mount preparations revealed bridge localization in the grooves between mitochondrial cristae. Bridges occur regularly along the axoneme with a spacing of approximately 52 nm and are not in horizontal register on opposite sides of the axoneme. Shearing of flagellar organelles demonstrated strong attachment of bridges directly to the mitochondrial derivatives at one extremity, while at the other, bridges pull out connecting fibers from the axoneme (after sodium citrate treatment).</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"101 2","pages":"Pages 159-164"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90005-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53916037","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":"Process of cytoplasmic elimination during spermiogenesis in two cyprinodontidae (Teleostean fishes)","authors":"Omar Thiom Thiaw ,&nbsp;Xavier Mattei ,&nbsp;Raymond Romand","doi":"10.1016/0889-1605(88)90009-2","DOIUrl":"10.1016/0889-1605(88)90009-2","url":null,"abstract":"<div><p>The mechanism of excess cytoplasm elimination during spermiogenesis was studied in two Cyprinodontidae species <em>Aphysemion riggenbachi</em> and <em>Aphyosemion splendopleure</em>. The cytoplasm is progressively filled with numerous vesicles resulting mainly from the phenomenon of pinocytosis. These vesicles coalesce and give birth to concentric cisternae in the aged spermatid. The residual body is formed by this membranous system.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"101 2","pages":"Pages 192-198"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90009-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53916447","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":"Sites of leucine, arginine, and glycine accumulation in the absorptive trichomes of a carnivorous bromeliad","authors":"T. Page Owen Jr.,&nbsp;William W. Thomson","doi":"10.1016/0889-1605(88)90012-2","DOIUrl":"10.1016/0889-1605(88)90012-2","url":null,"abstract":"<div><p>Ultrastructural localization of leucine, arginine, and glycine in the nutrient absorptive trichomes of the bromeliad <em>Brocchinia reducta</em> was achieved through a precipitation reaction with osmium tetroxide. Leaves incubated with amino acid solutions, then fixed with glutaraldehyde and postfixed with OsO₄ exhibited within the trichomes site specific accumulations of an electron-dense precipitate which were absent in distilled water-incubated controls. Four regions of leucine accumulation occurred: (i) in the outer trichome walls, (ii) within mitochondrial cristae, (iii) on the surface of lipid bodies, and (iv) in tubular invaginations of the inner envelope membrane of plastids. Glycine-incubated leaves had dense deposits in the mitochondrial matrix. Arginine-treated tissue had deposits only within the outer trichome walls. The initial glutaraldehyde fixation stabilized accumulations of the amino acid by reacting with the primary amine groups to form a Schiff's base. Subsequent OsO₄ postfixation was presumably oxidative with OsO₄ being reduced to an insoluble form.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"101 2","pages":"Pages 215-223"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90012-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53916468","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":"Etude ultrastructurale du spermatozoïde du coelacanthe: Latimeria chalumnae","authors":"Xavier Mattei ,&nbsp;Yves Siau ,&nbsp;Bernard Seret","doi":"10.1016/0889-1605(88)90015-8","DOIUrl":"10.1016/0889-1605(88)90015-8","url":null,"abstract":"<div><p>The study of the ultrastructure of the <em>Latimeria chalumnae</em> spermatozoon was carried out using the C3 coelacanth fished on September 24 1953 and preserved in 10% formalin at the Muséum National d'Histoire Naturelle in Paris. The spermatozoon has a tapered acrosome 2.5 μm long. The nucleus is 25 μm in lenght. Its posterior region, which is thinner for about 5 μm, is surrounded by a mitochondrial sheath. The nucleus is lengthwise crossed by a canal which contains three rods which extend to the anterior tip of the acrosome. The two centrioles are located at the base of the nucleus and arranged perpendicular to each other. The flagellum contains a 9 + 2 pattern axoneme and two longitudinal elements opposed to doublets 3 and 8. The ultrastructure of the <em>Latimeria</em> spermatozoon does not show a clear relationship between this fish and another group of fishes or tetrapods.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"101 2","pages":"Pages 243-251"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90015-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53916538","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":"Morphological organization of glycoprotein containing cell surface structures in yeast","authors":"Paul Walther ,&nbsp;Anne-Marie Schweingruber ,&nbsp;Martin Müller,&nbsp;M. Ernst Schweingruber","doi":"10.1016/0889-1605(88)90002-X","DOIUrl":"10.1016/0889-1605(88)90002-X","url":null,"abstract":"<div><p>Yeast cells (<em>Schizosaccaromyces pombe and Saccharomyces cerevisiae</em>) that are rapidly cryofixed without cryoprotectants reveal hair-like structures, called fimbriae, on their surfaces. The anchorage point of <em>S. pombe</em> fimbriae can be located either very close to the plasma membrane or in a more peripheral cell wall layer. They can de detached with aqueous ethanol, and biochemical and immunological data indicate that glycoproteins including acid phosphatase constitute a major component of the fimbriae. Mutants of <em>S. cerevisiae</em> lacking the outer heterogeneous mannose chains reveal an altered cell surface morphology. Typical fimbriae are absent. In cells of <em>S. pombe</em> that just have divided, fimbriae are not visible on the newly generated wall. This suggests that fimbriae assembly occurs after division has taken place. Fimbriae seem to be involved in the cell-cell recognition and/or aggregation process.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"101 2","pages":"Pages 123-136"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90002-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53915975","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":"Some aspects of the structural organization of the spinal cord of Gymnotus carapo (Teleostei, gymnotiformes) II. The motoneurons","authors":"O. Trujillo-Cenóz,&nbsp;C. Bertolotto","doi":"10.1016/0889-1605(88)90013-4","DOIUrl":"10.1016/0889-1605(88)90013-4","url":null,"abstract":"<div><p>The use of horseradish peroxidase as neuronal marker has allowed us to distinguish in the spinal cord of the weakly electric fish <em>Gymnotus carapo</em> two main populations of motoneurons: the periependymal motoneurons which innervate the axial musculature and the ventral motoneurons which innervate the appendicular muscles. The ventral horns were explored by means of conventional staining procedures and divided into four dorsoventral zones (I–IV). The largest motoneurons lying in the periependymal gray have been tentatively identified as the “primary motoneurons” (PM) of this species. The PMs are located forming two columss at each side of the central canal. They are characterized by their large size (50–75 μm), the occurrence of four or five thick dendritic trunks, and the peculiar intraspinal pathways of their axons. The dendritic trunks originate exclusively from the lateral surface of each neuron and project toward the ipsilateral, most dorsal neuropiles of the ventral horns (zones I and II). The axons follow ventromedial courses, close to the ipsilateral Mauthner fiber. The ventral motoneurons innervating the muscles of the anal fin are located within zones III and IV of the anterior horns. They are arranged in groups distributed along the cord; each group consits of 15–20 small- and medium-size neurons. The muscles of the pectoral fins receive their innervation from motoneurons lying in the ventral portion of the transitional zone between the medulla and the spinal cord. Three kinds of nerve terminals have been found impinging on the motoneuron somata and dendrites: (a) terminals with the fine structural characteristics of chemical synapses, (b) terminals identified as “mixed junctions” (chemical and electrical), and (c) terminals containing flat vesicles (proposed as serving inhibitory functions). Adjacent nerve terminals show zones in which the plasma membranes lie closely apposed. At these levels there are membrane pentalaminar patches (gap junctions) similar to those found at the level of the mixed junctions. These patches may facilitate, by means of electrotonic coupling, the synchronized activity of several synaptic terminals. The functional properties of the motoneurons of <em>Gymnotus</em> remain unexplored. These morphological studies have been initiated to support forthcoming electrophysiological investigations.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"101 2","pages":"Pages 224-235"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90013-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53916496","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":"Effects of tunicamycin and monensin on the distribution of highly phosphorylated proteins in cells infected with herpes simplex virus type 1","authors":"Carmen Lopez-Iglesias ,&nbsp;Francine Puvion-Dutilleul","doi":"10.1016/0889-1605(88)90007-9","DOIUrl":"10.1016/0889-1605(88)90007-9","url":null,"abstract":"<div><p>New aspects of the distribution of highly phosphorylated proteins in cells infected with herpes simplex virus type 1 (HSV-1) were investigated at the ultrastructural level by the use of drugs which inhibit the glycosylation of viral proteins. The highly phosphorylated proteins were localized by the bismuth tartrate procedure applied on sections of glutaraldehyde-fixed cells embedded in Lowicryl. The drugs employed were tunicamycin, which alters the glycosylation activity of the rough endoplasmic reticulum (RER), and monensin, which blocks the migration of vesicles of the Golgi apparatus (GA) thereby impairing the glycosylation function of the GA. Tunicamycin induced proliferation of RER and the accumulation of highly phosphorylated proteins on its membranes and also impaired GA vesicle maturation and inhibited the usual accumulation of phosphorylated proteins within them. Monensin induced proliferation of the nuclear envelope, including both outer and inner membranes, with bismuth bound to staggered segments of the latter, and also affected the GA in that bismuth-binding proteins were accumulated on the external surface of the swollen vesicles instead of the lumen. These data suggests that an injury of one membrane system, RER or GA, engenders consequential effects on the other. This also supports evidence for an interrelationship between post-translational glycosylation and phosphorylation of proteins in HSV infection.</p></div>","PeriodicalId":77743,"journal":{"name":"Journal of ultrastructure and molecular structure research","volume":"101 2","pages":"Pages 173-184"},"PeriodicalIF":0.0,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0889-1605(88)90007-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13625777","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}