Zoospore ultrastructure of Olpidium cucurbitacearum (Chytridiales)

1977 ◽  
Vol 55 (24) ◽  
pp. 3063-3074 ◽  
Author(s):  
D. J. S. Barr ◽  
V. E. Hadland-Hartmann
Keyword(s):  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
Transition Zone ◽  
Rough Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Flagellar Apparatus ◽  
Multivesicular Bodies ◽  
Taxonomic Relationship ◽  
Anterior Nucleus

Zoospore ultrastructure of Olpidium cucurbitacearum Barr & Dias is described. Isolates from Ontario and Japan are alike. The elliptical zoospore has an anterior nucleus partially surrounded by lobed and branched mitochondria. In the central part an interconnecting network consisting ofsmooth and rough endoplasmic reticulum, a Golgi complex, microbodies, and multivesicular bodies predominates. Vacuoles are abundant in the posterior. Ribosomes occur throughout the cytoplasm. The flagellar apparatus consists of the following: a short fibrillar rhizoplast connecting both kinetosome and nonfunctional centriole to an electron-opaque bar on the nuclear envelope; an elongated transition zone; and a 9 + 2 flagellum axoneme running much of the length of the zoospore through to the posterior end. Props do not connect the kinetosome to the plasmalemma; however, prop parts connect to the kinetosome, and prop parts connect to the plasmalemma at the posterior end of the zoospore. The taxonomic relationship to other chytrids is discussed; the zoospore is similar to that of O. brassicae (Woronin) Dang, and Rhizophlyctis rosea (deBary &Woronin) Fischer, and somewhat similar to that of Rozella allomycis Foust.

The ultrastructure of the zoospore of Hyphochytrium catenoides

1985 ◽  
Vol 63 (3) ◽  
pp. 497-505 ◽  
Author(s):  
Elizabeth W. Cooney ◽  
Donald J. S. Barr ◽  
William E. Barstow
Keyword(s):  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
Transition Zone ◽  
Multivesicular Bodies ◽  
Dense Matrix ◽  
Flagellar Membrane ◽  
Membrane Bound

The ultrastructure of the zoospore of Hyphochytrium catenoides Karling is described. The zoospore has a single, anterior, tinsel flagellum. The nucleus is elongate and convoluted with an indentation at the anterior end in which the Golgi cisternae are located. There are large lipid globules in the posterior end of the cell. The ribosomes are loosely enclosed by endoplasmic reticulum, the nuclear envelope, and mitochondria. The mitochondria have tubular cristae in a dense matrix. Microbodies are found appressed to the nuclear envelope and also free in the ribosomal region. Endoplasmic reticulum sheets traverse the ribosome region. The vesiculate cytoplasm has several distinct types of membrane-bound inclusions: (i) multivesicular bodies, (ii) vesicles containing presumptive mastigonemes, (iii) vesicles having an electron-dense cortex with an electron-transparent center, and (iv) electron-opaque vesicles whose contents seem condensed and only partially fill the vesicles. The transition zone from the flagellum to the kinetosome has three segments: a distal set of struts extending from the axonemal doublets into the axoneme core, a midsection of electron-opaque rings, and a distinctive "disclike" terminal plate with a thickened portion between the doublets and the flagellar membrane. The three-part rootlet system has (i) a "ribbed" pair of microtubules on one side of the kinetosome, (ii) a curved "ribbed," single microtubule with electron-opaque backing which originates near the nonfunctional centriole, and (iii) a straight doublet of microtubules without ribs extending from the nonfunctional centriole posteriorly to the midregion of the zoospore.

scholarly journals DEVELOPMENT OF ENDOGENOUS PEROXIDASE IN FETAL RAT SUBMANDIBULAR GLAND

1973 ◽  
Vol 21 (1) ◽  
pp. 42-50 ◽  
Author(s):  
SHOHEI YAMASHINA ◽  
TIBOR BARKA
Keyword(s):  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
Submandibular Gland ◽  
Rough Endoplasmic Reticulum ◽  
Peroxidase Activity ◽  
Secretory Granules ◽  
Prenatal Development ◽  
Reaction Products ◽  
Cell Type ◽  
Endogenous Peroxidase

The prenatal development of endogenous peroxidase activity in the submandibular gland of rat was investigated by means of the diaminobenzidine-H2O2 histochemical method. The submandibular gland of a 16-day-old fetus was composed of cords of uniform, undifferentiated cells which contained no secretory granules and revealed no peroxidase activity. Peroxidase activity first appeared at the 17th day of gestation in the cisternae of the rough endoplasmic reticulum and nuclear envelope in a few cells. At the 18th day of gestation cells which exhibited reaction products in the rough endoplasmic reticulum and nuclear envelope also contained secretory granules with a strong peroxidase activity. During the last days of gestation the number of peroxidase positive cells, which contained numerous secretory granules, increased. The peroxidase-containing cells are the immediate precursors of the proacinar cells of early postnatal stages. During the same time period, when the peroxidase-containing cells differentiated, a second cell type also differentiated in the cellular cords. The development of this cell type was marked by the appearance of secretory granules stainable with toluidine blue. Through the prenatal development, this cell type revealed no peroxidase activity and was identified with the terminal tubule cell of the newborn. The morphologic and cytochemical findings indicate that terminal tubule cells and proacinar cells are committed cells; the former differentiate toward 2nd order intercalated duct cells and the latter transform to mature acinar cells.

scholarly journals Glycosyltransferase activities in Golgi complex and endoplasmic reticulum fractions isolated from African trypanosomes.

1984 ◽  
Vol 99 (2) ◽  
pp. 569-577 ◽  
Author(s):  
D J Grab ◽  
S Ito ◽  
U A Kara ◽  
L Rovis
Keyword(s):  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Smooth Endoplasmic Reticulum ◽  
Surface Glycoprotein ◽  
Relative Distribution ◽  
African Trypanosomes ◽  
Independent Form ◽  
Variable Surface ◽  
Dependent Form

Highly enriched Golgi complex and endoplasmic reticulum fractions were isolated from total microsomes obtained from Trypanosoma brucei, Trypanosoma congolense, and Trypanosoma vivax, and tested for glycosyltransferase activity. Purity of the fractions was assessed by electron microscopy as well as by biochemical analysis. The relative distribution of all the glycosyltransferases was remarkably similar for the three species of African trypanosomes studied. The Golgi complex fraction contained most of the galactosyltransferase activity followed by the smooth and rough endoplasmic reticulum fractions. The dolichol-dependent mannosyltransferase activities were highest for the rough endoplasmic reticulum, lower for the smooth endoplasmic reticulum, and lowest for the Golgi complex. Although the dolichol-independent form of N-acetylglucosaminyltransferase was essentially similar in all the fractions, the dolichol-dependent form of this enzyme was much higher in the endoplasmic reticulum fractions than in the Golgi complex fraction. Inhibition of this latter activity in the smooth endoplasmic reticulum fraction by tunicamycin A1 suggests that core glycosylation of the variable surface glycoprotein may occur in this organelle and not in the rough endoplasmic reticulum as previously assumed.

scholarly journals Endoplasmic reticulum-to-Golgi transitions upon herpes virus infection

F1000Research ◽  
2018 ◽  
Vol 6 ◽  
pp. 1804 ◽  
Author(s):  
Peter Wild ◽  
Andres Kaech ◽  
Elisabeth M. Schraner ◽  
Ladina Walser ◽  
Mathias Ackermann
Keyword(s):  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
Golgi Complex ◽  
Nuclear Membrane ◽  
Progeny Virus ◽  
Cytoplasmic Matrix ◽  
Outer Nuclear Membrane ◽  
Nuclear Membranes ◽  
Perinuclear Space ◽  
Hsv 1

Background: Herpesvirus capsids are assembled in the nucleus, translocated to the perinuclear space by budding, acquiring tegument and envelope, or released to the cytoplasm via impaired nuclear envelope. One model proposes that envelopment, “de-envelopment” and “re-envelopment” is essential for production of infectious virus. Glycoproteins gB/gH were reported to be essential for de-envelopment, by fusion of the “primary” envelope with the outer nuclear membrane. Yet, a high proportion of enveloped virions generated from genomes with deleted gB/gH were found in the cytoplasm and extracellular space, suggesting the existence of alternative exit routes.Methods: We investigated the relatedness between the nuclear envelope and membranes of the endoplasmic reticulum and Golgi complex, in cells infected with either herpes simplex virus 1 (HSV-1) or a Us3 deletion mutant thereof, or with bovine herpesvirus 1 (BoHV-1) by transmission and scanning electron microscopy, employing freezing technique protocols.Results:  The Golgi complex is a compact entity in a juxtanuclear position covered by a membrane on thecisface. Golgi membranes merge with membranes of the endoplasmic reticulum forming an entity with the perinuclear space. All compartments contained enveloped virions. After treatment with brefeldin A, HSV-1 virions aggregated in the perinuclear space and endoplasmic reticulum, while infectious progeny virus was still produced.Conclusions: The data suggest that virions derived by budding at nuclear membranes are intraluminally transported from the perinuclear space via Golgi -endoplasmic reticulum transitions into Golgi cisternae for packaging. Virions derived by budding at nuclear membranes are infective like Us3 deletion mutants, which  accumulate in the perinuclear space. Therefore, i) de-envelopment followed by re-envelopment is not essential for production of infective progeny virus, ii) the process taking place at the outer nuclear membrane is budding not fusion, and iii) naked capsids gain access to the cytoplasmic matrix via impaired nuclear envelope as reported earlier.

scholarly journals Expression of Enamel Proteins in Rough Endoplasmic Reticulum and Golgi Complex in Human Dental Germs

2017 ◽  
Vol 35 (2) ◽  
pp. 435-441
Author(s):  
Francisco Javier Gutiérrez-Cantú ◽  
Alma Lilián Guerrero-Barrera ◽  
Wulfrano Sánchez Meraz ◽  
Amaury de Jesús Pozos-Guillen ◽  
Héctor Flores-Reyes ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Enamel Proteins

scholarly journals The beads in the Golgi complex-endoplasmic reticulum region.

1976 ◽  
Vol 70 (2) ◽  
pp. 384-394 ◽  
Author(s):  
M Locke ◽  
P Huie
Keyword(s):  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Insect Cell ◽  
Cell Types ◽  
Feulgen Staining ◽  
Clear Halo ◽  
Bismuth Salts ◽  
Transition Vesicles

The region between the rough endoplasmic reticulum (ER) and the Golgi complex has been studied in a variety of insect cell types in an attempt to find a marker for the exit gate or gates from the ER. We have found that the smooth surface of the rough endoplasmic reticulum near Golgi complex transitional elements has beadlike structures arranged in rings at the base of transition vesicles. They occur in all insect cell types and a variety of other organisms. The beads can be seen only after staining in bismuth salts. They are 10-12 nm in diameter and are separated from the membrane and one another by a clear halo giving them a center to center spacing of about 27 nm. The beads are not sensitive to nucleases under conditions which disrupt ribosomes or remove all Feulgen staining material from the nucleus. Under conditions similar to those used to stain tissue, bismuth does not react in vitro with nucleic acids. The component of the beads that stains preferentially with bismuth is therefore probably not nucleic acid.

scholarly journals Endoplasmic reticulum-to-Golgi transitions upon herpes virus infection

F1000Research ◽  
2017 ◽  
Vol 6 ◽  
pp. 1804 ◽  
Author(s):  
Peter Wild ◽  
Andres Kaech ◽  
Elisabeth M. Schraner ◽  
Ladina Walser ◽  
Mathias Ackermann
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
Golgi Complex ◽  
Progeny Virus ◽  
Perinuclear Space ◽  
Exit Route ◽  
Scanning Electron ◽  
Hsv 1

Background: Herpesvirus capsids are assembled in the nucleus before they are translocated to the perinuclear space by budding, acquiring tegument and envelope, or releasing to the cytoplasm in a “naked” state via impaired nuclear envelope. One model proposes that envelopment, “de-envelopment” and “re-envelopment” are essential steps for production of infectious virus. Glycoproteins gB/gH were reported to be essential for de-envelopment, by fusion of the “primary” envelope with the outer nuclear membrane. Yet, a high proportion of enveloped virions generated from genomes with deleted gB/gH were found in the cytoplasm and extracellular space, suggesting the existence of an alternative exit route.Methods: We investigated the relatedness between the nuclear envelope and membranes of the endoplasmic reticulum and Golgi complex, in cells infected with either herpes simplex virus 1 (HSV-1) or a Us3 deletion mutant thereof, or with bovine herpesvirus 1 (BoHV-1) by transmission and scanning electron microscopy, employing freezing technique protocols that lead to improved spatial and temporal resolution.Results: Scanning electron microscopy showed the Golgi complex as a compact entity in a juxtanuclear position covered by a membrane on thecisface. Transmission electron microscopy revealed that Golgi membranes merge with membranes of the endoplasmic reticulum forming an entity with the perinuclear space. All compartments contained enveloped virions. After treatment with brefeldin A, HSV-1 virions aggregated in the perinuclear space and endoplasmic reticulum, while infectious progeny virus was still produced.Conclusions: The data strongly suggest that virions are intraluminally transported from the perinuclear space via Golgi complex-endoplasmic reticulum transitions into Golgi cisternae for packaging into transport vacuoles. Furthermore, virions derived by budding at nuclear membranes are infective as has been shown for HSV-1 Us3 deletion mutants, which almost entirely accumulate in the perinuclear space. Therefore, de-envelopment followed by re-envelopment is not essential for production of infective progeny virus.

Localization of Alkaline Phosphatase in Marrow Cells

1973 ◽  
Vol 31 ◽  
pp. 692-693
Author(s):  
Anne D. Geddes ◽  
Mary E. Kirchen ◽  
G. June Marshall
Keyword(s):  
Alkaline Phosphatase ◽  
Endoplasmic Reticulum ◽  
Light Microscopy ◽  
Rough Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Significant Marker ◽  
Leukocyte Alkaline Phosphatase ◽  
Marrow Cells

Leukocyte alkaline phosphatase(LAP) is potentially a significant marker for following the maturation sequence of normal and abnormal neutrophils. This enzyme can be localized in the rough endoplasmic reticulum (rer) and in the Golgi complex of immature neutrophils but it has been very difficult to demonstrate LAP activity in the granules of mature neutrophils. This observation presents a dilemma since LAP is present in higher concentrations in mature as opposed to immature neutrophils as demonstrated by biochemical and light microscopy methods.In an attempt to solve this problem, variations on the routine methods for demonstrating LAP activity were explored. Acetone, formaldehyde, methanol and gluteraldehyde were used as fixatives.

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