Fluorescent retrograde double labeling: axonal branching in the ascending raphe and nigral projections

Science ◽  
1979 ◽  
Vol 204 (4395) ◽  
pp. 873-875 ◽  
Author(s):  
D van der Kooy ◽  
H. Kuypers
Keyword(s):  
Double Labeling ◽  
Axonal Branching

Axonal branching of the olivocerebellar projection in the rat: A double-labeling study

1989 ◽  
Vol 284 (1) ◽  
pp. 48-59 ◽  
Author(s):  
A. W. Hrycyshyn ◽  
H. Ghazi ◽  
B. A. Flumerfelt
Keyword(s):  
Double Labeling ◽  
Axonal Branching

Axonal branching of basal forebrain projections to the neocortex: a double-labeling study in the cat

1986 ◽  
Vol 375 (1) ◽  
pp. 176-181 ◽  
Author(s):  
Marea K. Boylan ◽  
Robin S. Fisher ◽  
Chester D. Hull ◽  
Nathaniel A. Buchwald ◽  
Michael S. Levine
Keyword(s):  
Basal Forebrain ◽  
Double Labeling ◽  
Axonal Branching

Double-labeling study of axonal branching within the lateral reticulocerebellar projection in the rat

1987 ◽  
Vol 258 (3) ◽  
pp. 378-386 ◽  
Author(s):  
H. Ghazi ◽  
A. W. Hrycyshyn ◽  
B. A. Flumerfelt
Keyword(s):  
Double Labeling ◽  
Axonal Branching

Gold labeling of teichoic acid on adjacent surfaces of staphylococcus aureus

1990 ◽  
Vol 48 (3) ◽  
pp. 578-579
Author(s):  
Margaret Hukee
Keyword(s):  
Staphylococcus Aureus ◽  
Teichoic Acid ◽  
Protein Labeling ◽  
Minimal Amount ◽  
Section Thickness ◽  
Double Labeling ◽  
Parallel Surfaces ◽  
Supporting Membrane

Gold labeling of two antigens (double labeling) is often done on two section surfaces separated by section thickness. Whether labeling is done on both sides of the same section or on two parallel surfaces separated by section thickness (PSSST), comparable results are dependent on an equal number of epitopes being exposed at each surface. We propose a method to study protein labeling within the same field of proteins, by examining two directly adjacent surfaces that were split during sectioning. The number of labeling sites on adjacent surfaces (AS) were compared to sites on PSSST surfaces in individual bacteria.Since each bacteria needed to be recognizable in all three section surfaces, one-hole grids were used for labeling. One-hole grids require a supporting membrane and excessive handling during labeling often ruptures the membrane. To minimize handling, a labeling chamber was designed that is inexpensive, disposable, minimizes contamination, and uses a minimal amount of solution.

Expression and distribution of the Na+- HCO 3 − cotransporter in human pancreas

1999 ◽  
Vol 277 (2) ◽  
pp. G487-G494 ◽  
Author(s):  
Christopher R. Marino ◽  
Virginia Jeanes ◽  
Walter F. Boron ◽  
Bernhard M. Schmitt
Keyword(s):  
Northern Blot ◽  
Islet Cells ◽  
Rat Kidney ◽  
Physiological Role ◽  
Human Pancreas ◽  
Transmembrane Conductance Regulator ◽  
Transmembrane Conductance ◽  
Cellular Mechanisms ◽  
Double Labeling ◽  
Normal Human

The cellular mechanisms of [Formula: see text] secretion in the human pancreas are unclear. Expression of a Na+-[Formula: see text]cotransporter (NBC) mRNA has been observed recently, but the distribution and physiological role of the NBC protein are not known. Here we examined the expression and localization of NBC in human pancreas by Northern blot, immunoblot, and immunofluorescence microscopy. Rat kidney NBC probes detected a single 9.5-kb band by Northern blot. On immunoblots, two polyclonal antisera directed against different epitopes of rat kidney NBC identified a single ∼130-kDa protein. In cryosections of normal human pancreas, both antisera labeled basolateral membranes of large, morphologically identifiable ducts and produced a distinct labeling pattern in the remainder of the parenchyma. In double-labeling experiments, NBC immunoreactivity in the parenchyma colocalized with the Na+-K+pump, a basolateral marker. In contrast, NBC and cystic fibrosis transmembrane conductance regulator, an apical membrane marker, were detected within the same histological structures but at different subcellular localizations. The NBC antisera did not label acinar or islet cells. Our observations suggest that secretion of[Formula: see text] by human pancreatic duct cells involves the basolateral uptake of Na+and[Formula: see text] via NBC, an electrogenic Na+-[Formula: see text]cotransporter.

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