Ultrastructural localization of sialylated glycoconjugates in cells of the salamander olfactory mucosa using lectin cytochemistry

1992 ◽  
Vol 267 (1) ◽  
pp. 113-124 ◽  
Author(s):  
James D. Foster ◽  
Marilyn L. Getchell ◽  
Thomas V. Getchell
Keyword(s):  
Ultrastructural Localization ◽  
Olfactory Mucosa ◽  
Lectin Cytochemistry ◽  
In Cells

scholarly journals Ultrastructural localization of connexins (Cx36, Cx43, Cx45), glutamate receptors and aquaporin-4 in rodent olfactory mucosa, olfactory nerve and olfactory bulb

2005 ◽  
Vol 34 (3-5) ◽  
pp. 307-341 ◽  
Author(s):  
John E. Rash ◽  
Kimberly G. V. Davidson ◽  
Naomi Kamasawa ◽  
Thomas Yasumura ◽  
Masami Kamasawa ◽  
...  
Keyword(s):  
Olfactory Bulb ◽  
Glutamate Receptors ◽  
Ultrastructural Localization ◽  
Olfactory Nerve ◽  
Olfactory Mucosa ◽  
Aquaporin 4

scholarly journals Ultrastructural localization of rRNA shows defective nuclear export of preribosomes in mutants of the Nup82p complex

2001 ◽  
Vol 155 (6) ◽  
pp. 923-936 ◽  
Author(s):  
Pierre-Emmanuel Gleizes ◽  
Jacqueline Noaillac-Depeyre ◽  
Isabelle Léger-Silvestre ◽  
Frédéric Teulières ◽  
Jean-Yves Dauxois ◽  
...  
Keyword(s):  
Nuclear Export ◽  
Ultrastructural Localization ◽  
Small Subunit ◽  
Nuclear Accumulation ◽  
Rrna Processing ◽  
Wild Type ◽  
Tight Control ◽  
Yeast Saccharomyces Cerevisiae ◽  
In Cells

To study the nuclear export of preribosomes, ribosomal RNAs were detected by in situ hybridization using fluorescence and EM, in the yeast Saccharomyces cerevisiae. In wild-type cells, semiquantitative analysis shows that the distributions of pre-40S and pre-60S particles in the nucleolus and the nucleoplasm are distinct, indicating uncoordinated transport of the two subunits within the nucleus. In cells defective for the activity of the GTPase Gsp1p/Ran, ribosomal precursors accumulate in the whole nucleus. This phenotype is reproduced with pre-60S particles in cells defective in pre-rRNA processing, whereas pre-40S particles only accumulate in the nucleolus, suggesting a tight control of the exit of the small subunit from the nucleolus. Examination of nucleoporin mutants reveals that preribosome nuclear export requires the Nup82p–Nup159p–Nsp1p complex. In contrast, mutations in the nucleoporins forming the Nup84p complex yield very mild or no nuclear accumulation of preribosome. Interestingly, domains of Nup159p required for mRNP trafficking are not necessary for preribosome export. Furthermore, the RNA helicase Dbp5p and the protein Gle1p, which interact with Nup159p and are involved in mRNP trafficking, are dispensable for ribosomal transport. Thus, the Nup82p–Nup159p–Nsp1p nucleoporin complex is part of the nuclear export pathways of preribosomes and mRNPs, but with distinct functions in these two processes.

Ultrastructural localization and identification of adrenergic and cholinergic nerve terminals in the olfactory mucosa

1989 ◽  
Vol 225 (3) ◽  
pp. 232-245 ◽  
Author(s):  
Barbara S. Zielinski ◽  
Marilyn L. Getchell ◽  
Randall L. Wenokur ◽  
Thomas V. Getchell
Keyword(s):  
Ultrastructural Localization ◽  
Olfactory Mucosa ◽  
Nerve Terminals ◽  
Cholinergic Nerve ◽  
Cholinergic Nerve Terminals

The cytochemical localization of glucose-6-phosphatase and catalase in cells comprising the root cap of corn

1984 ◽  
Vol 42 ◽  
pp. 260-261
Author(s):  
C.E. McClelen
Keyword(s):  
Zea Mays ◽  
Enzymatic Activity ◽  
Ultrastructural Localization ◽  
Root Cap ◽  
Cytochemical Localization ◽  
Functional Changes ◽  
Different Types ◽  
And Function ◽  
Peripheral Cells ◽  
In Cells

The root cap of corn (Zea mays) is comprised of several different types of cells, each having a unique structure and function. For example, columella cells in the center of the cap are responsible for perceiving gravity. These cells subsequently differentiate into peripheral cells, which are located at the edge of the cap and function in the production and/or secretion of mucopolysaccharides (mucilage). Differences in enzymatic activity and location in cells of the root cap provide key evidence for the nature and site of the functional changes that accompany differentiation.The cytochemical localizations of glucose-6-phosphatase (G-6-Ptase) and catalase were undertaken to define the modifications of enzyme localization associated with cellular differentiation in root caps of Zea mays. G-6-Ptase and catalase were localized using procedures described by Hall. Cytochemistry as performed in this study was consistently specific for the designated enzyme and gave precise ultrastructural localization. Enzymatic precipitate was absent in all controls. Sections were not counterstained to allow for positive identification of staining due to enzymatic activity.

Ultrastructural localization of polyphenoloxidase and peroxidase in roots and hypocotyls of cotton seedlings

1978 ◽  
Vol 56 (14) ◽  
pp. 1579-1587 ◽  
Author(s):  
W. C. Mueller ◽  
C. H. Beckman
Keyword(s):  
Cell Walls ◽  
Ultrastructural Localization ◽  
Endodermal Cell ◽  
Phenolic Metabolism ◽  
Enzyme Systems ◽  
In Cells

Polyphenoloxidase and peroxidase were localized and differentiated from each other in the roots and hypocotyls of cotton when these tissues were treated with dihydroxyphenylalanine (DOPA) and diaminobenizidine (DAB), respectively. The DOPA reaction occurred in the thylakoids of plastids from the endodermis of the root and in plastids from several tissues of the hypocotyl. The reaction was inhibited by diethyldithiocarbamate (DIECA), but catalase had no effect. An intense DAB reaction occurred in the epidermal, subepidermal, and endodermal cell walls of both roots and hypocotyls with a lesser reaction in the cortex and stele. DAB also caused a reaction in the microbodies in cells of all tissues, but a reaction could not be detected in other organelles. Aminotriazole (AT) inhibited the reaction in the microbodies but not in the cell walls, whereas the reaction was prevented entirely if H2O2 was eliminated from the medium. These results indicate that the two enzyme systems are localized in different and discrete areas in the cotton tissue and that the plastids are intimately involved in phenolic metabolism.

Ultrastructural localization of specific nucleoprotein fractions

1978 ◽  
Vol 36 (2) ◽  
pp. 204-205
Author(s):  
G. L. Brown
Keyword(s):  
Gel Electrophoresis ◽  
Mouse Liver ◽  
Polyacrylamide Gel Electrophoresis ◽  
Ultrastructural Localization ◽  
Polyacrylamide Gel ◽  
Acid Extraction ◽  
Acid Solutions ◽  
Low Salt ◽  
Liver Nuclei ◽  
Phosphate Groups

Bismuth (Bi) stains nucleoproteins (NPs) by interacting with available amino and primary phosphate groups. These two staining mechanisms are distinguishable by glutaraldehyde crosslinking (Fig. 1,2).Isolated mouse liver nuclei, extracted with salt and acid solutions, fixed in either formaldehyde (form.) or gl utaraldehyde (glut.) and stained with Bi, were viewed to determine the effect of the extractions on Bi stainina. Solubilized NPs were analyzed by SDS-polyacrylamide gel electrophoresis.Extraction with 0.14 M salt does not change the Bi staining characteristics (Fig. 3). 0.34 M salt reduces nucleolar (Nu) staining but has no effect on interchromatinic (IC) staining (Fig. 4). Proteins responsible for Nu and glut.- insensitive IC staining are removed when nuclei are extracted with 0.6 M salt (Fig. 5, 6). Low salt and acid extraction prevents Bi-Nu staining but has no effect on IC staining (Fig. 7). When nuclei are extracted with 0.6 M salt followed by low salt and acid, all Bi-staining components are removed (Fig. 8).

Ultrastructural Localization of Acid Mucosubstance in Skeletal Muscle

1967 ◽  
Vol 25 ◽  
pp. 52-53 ◽  
Author(s):  
William J. Dougherty ◽  
Samuel S. Spicer
Keyword(s):  
Striated Muscle ◽  
Divalent Cations ◽  
Ultrastructural Localization ◽  
Major Elements ◽  
Frozen Sections ◽  
Thorium Dioxide ◽  
Iron Solution ◽  
Coupling System ◽  
Psoas Muscles ◽  
Formalin Fixed

In recent years, considerable attention has focused on the morphological nature of the excitation-contraction coupling system of striated muscle. Since the study of Porter and Palade, it has become evident that the sarcoplastic reticulum (SR) and transverse tubules constitute the major elements of this system. The problem still exists, however, of determining the mechamisms by which the signal to interdigitate is presented to the thick and thin myofilaments. This problem appears to center on the movement of Ca++ions between myofilaments and SR. Recently, Philpott and Goldstein reported acid mucosubstance associated with the SR of fish branchial muscle using the colloidal thorium dioxide technique, and suggested that this material may serve to bind or release divalent cations such as Ca++. In the present study, Hale's iron solution adapted to electron microscopy was applied to formalin-fixed myofibrils isolated from glycerol-extracted rabbit psoas muscles and to frozen sections of formalin-fixed rat psoas muscles.

Immunoenzymatic demonstration of the simultaneous presence of transferrin, hemopexin and albumin in a same hepatocyte and their ultrastructural localization

1978 ◽  
Vol 36 (2) ◽  
pp. 88-89
Author(s):  
M. Kraemer ◽  
J. Foucrier ◽  
J. Vassy ◽  
M.T. Chalumeau
Keyword(s):  
Plasma Proteins ◽  
Rat Hepatocytes ◽  
Ultrastructural Localization ◽  
Carrier Proteins ◽  
Normal Cells ◽  
Adult Rat ◽  
Adult Rat Hepatocytes ◽  
Monospecific Antisera ◽  
Different Levels

Some authors using immunofluorescent techniques had already suggested that some hepatocytes are able to synthetize several plasma proteins. In vitro studies on normal cells or on cells issued of murine hepatomas raise the same conclusion. These works could be indications of an hepatocyte functionnal non-specialization, meanwhile the authors never give direct topographic proofs suitable with this hypothesis.The use of immunoenzymatic techniques after obtention of monospecific antisera had seemed to us useful to bring forward a better knowledge of this problem. We have studied three carrier proteins (transferrin = Tf, hemopexin = Hx, albumin = Alb) operating at different levels in iron metabolism by demonstrating and localizing the adult rat hepatocytes involved in their synthesis.Immunological, histological and ultrastructural methods have been described in a previous work.

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