Immunogold cytochemistry in neuroscience

2013 ◽  
Vol 16 (7) ◽  
pp. 798-804 ◽  
Author(s):  
Mahmood Amiry-Moghaddam ◽  
Ole Petter Ottersen
Keyword(s):  
Immunogold Cytochemistry

scholarly journals Structures linking microfilament bundles to the membrane at focal contacts

1993 ◽  
Vol 122 (2) ◽  
pp. 485-496 ◽  
Author(s):  
SJ Samuelsson ◽  
PW Luther ◽  
DW Pumplin ◽  
RJ Bloch
Keyword(s):  
Single Bundle ◽  
Actin Microfilaments ◽  
Lateral Interactions ◽  
Membrane Interactions ◽  
Membrane Particles ◽  
Focal Contacts ◽  
Microfilament Bundles ◽  
Immunogold Cytochemistry ◽  
Beta 1 Integrin

We used quick-freeze, deep-etch, rotary replication and immunogold cytochemistry to identify a new structure at focal contacts. In Xenopus fibroblasts, elongated aggregates of particles project from the membrane to contact bundles of actin microfilaments. Before terminating, a single bundle of microfilaments interacts with several aggregates that appear intermittently over a distance of several microns. Aggregates are enriched in proteins believed to mediate actin-membrane interactions at focal contacts, including beta 1-integrin, vinculin, and talin, but they appear to contain less alpha-actinin and filamin. We also identified a second, smaller class of aggregates of membrane particles that contained beta 1-integrin but not vinculin or talin and that were not associated with actin microfilaments. Our results indicate that vinculin, talin, and beta 1-integrin are assembled into distinctive structures that mediate multiple lateral interactions between microfilaments and the membrane at focal contacts.

scholarly journals High-resolution immunogold cytochemistry indicates that AQP4 is concentrated along the basal membrane of parietal cell in rat stomach

FEBS Letters ◽  
1999 ◽  
Vol 459 (3) ◽  
pp. 305-309 ◽  
Author(s):  
Akikazu Fujita ◽  
Yoshiyuki Horio ◽  
Søren Nielsen ◽  
Erlend A Nagelhus ◽  
Fumiaki Hata ◽  
...  
Keyword(s):  
High Resolution ◽  
Parietal Cell ◽  
Basal Membrane ◽  
Rat Stomach ◽  
Immunogold Cytochemistry

scholarly journals Localization of myosin IC and myosin II in Acanthamoeba castellanii by indirect immunofluorescence and immunogold electron microscopy.

1990 ◽  
Vol 111 (5) ◽  
pp. 1895-1904 ◽  
Author(s):  
I C Baines ◽  
E D Korn
Keyword(s):  
Electron Microscopy ◽  
Plasma Membrane ◽  
Indirect Immunofluorescence ◽  
Synthetic Peptide ◽  
Myosin Ii ◽  
Phosphorylation Site ◽  
Acanthamoeba Castellanii ◽  
Immunogold Electron Microscopy ◽  
Membrane Phospholipids ◽  
Immunogold Cytochemistry

Polyclonal antisera have been raised against purified Acanthamoeba myosin II and to a synthetic 26 amino acid peptide that corresponds in sequence to the phosphorylation site of Acanthamoeba myosin IC. These antisera are specific for their respective antigens as determined by immunoblotting after SDS-PAGE of total cell lysates. By using the antisera, localization studies were performed by indirect immunofluorescence and by immunogold electron microscopy. Myosin II occurred in the cell cytoplasm and appeared to be concentrated in the cortex. Immunogold cytochemistry revealed at high resolution that myosin II is organized into rodlike filaments approximately 200 nm long. The antibody raised against the myosin IC synthetic peptide recognized both the plasma membrane and the membrane of the contractile vacuole. The plasma membrane staining was labile to treatment with saponin suggesting an intimate association of the myosin IC with membrane phospholipids. Immunogold cytochemistry with the antimyosin IC synthetic peptide showed that the myosin IC is closely associated with the membrane bilayer.

Variation in ultrastructure of mucoid coat and shell membrane secretion of a dasyurid marsupial

1996 ◽  
Vol 8 (4) ◽  
pp. 645 ◽  
Author(s):  
CT Roberts ◽  
WG Breed
Keyword(s):  
Electron Density ◽  
Polyclonal Antibodies ◽  
Secretory Granules ◽  
Granular Structure ◽  
Sminthopsis Crassicaudata ◽  
Shell Membrane ◽  
Early Embryos ◽  
Immunogold Cytochemistry ◽  
Ultrastructural Appearance ◽  
Electron Lucent

In the dasyurid marsupial Sminthopsis crassicaudata, the shell membrane of cleaving embryos has a compact granular structure but becomes fibrous around blastocysts. Polyclonal antibodies were raised against the extracellular coats, mucoid and shell membrane, of oocytes and early embryos. Immunogold cytochemistry resulted in labelling of secretory granules in the epithelia of both the ampulla and isthmus of the oviduct, although the secretory granules of these two regions differed in their ultrastructural appearance. Those in the ampulla were heterogeneous with areas of varying electron density, whereas those in the isthmus were electron dense and homogeneous. Shell membrane precursors were found in secretory granules in the epithelia of the uterotubal junction and endometrial glands and were electron lucent.

scholarly journals Specialized Membrane Domains for Water Transport in Glial Cells: High-Resolution Immunogold Cytochemistry of Aquaporin-4 in Rat Brain

1997 ◽  
Vol 17 (1) ◽  
pp. 171-180 ◽  
Author(s):  
Søren Nielsen ◽  
Erlend Arnulf Nagelhus ◽  
Mahmood Amiry-Moghaddam ◽  
Charles Bourque ◽  
Peter Agre ◽  
...  
Keyword(s):  
High Resolution ◽  
Rat Brain ◽  
Water Transport ◽  
Glial Cells ◽  
Aquaporin 4 ◽  
Membrane Domains ◽  
Immunogold Cytochemistry

Immunogold cytochemistry of cytochromes P-450 in porcine adrenal cortex

1987 ◽  
Vol 86 (6) ◽  
pp. 551-557 ◽  
Author(s):  
H. J. Geuze ◽  
J. W. Slot ◽  
K. Yanagibashi ◽  
J. A. McCracken ◽  
A. L. Schwartz ◽  
...  
Keyword(s):  
Adrenal Cortex ◽  
Immunogold Cytochemistry
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