The Nuclei of origin of monoaminergic, peptidergic, and cholinergic afferents to the cat nucleus reticularis magnocellularis: A double-labeling study with cholera toxin as a retrograde tracer

1988 ◽  
Vol 277 (1) ◽  
pp. 1-20 ◽  
Author(s):  
Pierre-Herv� Luppi ◽  
Kazuya Sakai ◽  
Patrice Fort ◽  
Denise Salvert ◽  
Michel Jouvet
Keyword(s):  
Cholera Toxin ◽  
Double Labeling ◽  
Retrograde Tracer ◽  
Nucleus Reticularis

scholarly journals Endocytosis of exogenous GM1 ganglioside and cholera toxin by neuroblastoma cells.

1983 ◽  
Vol 3 (1) ◽  
pp. 91-101 ◽  
Author(s):  
N K Gonatas ◽  
A Stieber ◽  
J Gonatas ◽  
T Mommoi ◽  
P H Fishman
Keyword(s):  
Cholera Toxin ◽  
Neuroblastoma Cells ◽  
Double Labeling ◽  
Electron Microscope Autoradiography ◽  
Density Distributions ◽  
Quantitative Studies ◽  
Covalently Linked ◽  
The Relationship ◽  
Cytochemical Marker ◽  
In Cells

Cholera toxin (CT) covalently linked to horseradish peroxidase (HRP) is a specific cytochemical marker for its receptor, the monosialoganglioside GM1. The binding and endocytosis of exogenous [3H]GM1 by cultured murine neuroblastoma cells (line 2A [CCl-131] ), which contain predominantly GM3, was examined by quantitative electron microscope autoradiography. The relationship between exogenous receptor, [3H]GM1, and CT HRP was studied in double labeling experiments consisting of autoradiographic demonstration of [3H]GM1 and cytochemical visualization of HRP. Exogenous [3H]GM1 was not degraded after its endocytosis by cells for 2 h at 37 degrees C. Quantitative studies showed similar grain density distributions in cells treated with [3H]GM1 alone and in cells treated with [3H]GM1 followed by CT-HRP. Qualitative studies conducted in double labeling experiments showed autoradiographic grains over the peroxidase-stained plasma membrane, lysosomes, and vesicles at the trans aspect of the Golgi apparatus. The findings indicate that exogenous glycolipid is associated with the plasmid membrane of deficient cells and undergoes endocytosis. The quantitative ultra-structural autoradiographic studies are consistent with the hypothesis that the spontaneous endocytosis of exogenous [3H]GM1 controls the subsequent uptake of CT-HRP.

Endocytosis of exogenous GM1 ganglioside and cholera toxin by neuroblastoma cells

1983 ◽  
Vol 3 (1) ◽  
pp. 91-101
Author(s):  
N K Gonatas ◽  
A Stieber ◽  
J Gonatas ◽  
T Mommoi ◽  
P H Fishman
Keyword(s):  
Cholera Toxin ◽  
Neuroblastoma Cells ◽  
Double Labeling ◽  
Electron Microscope Autoradiography ◽  
Density Distributions ◽  
Quantitative Studies ◽  
Covalently Linked ◽  
The Relationship ◽  
Cytochemical Marker ◽  
In Cells

Cholera toxin (CT) covalently linked to horseradish peroxidase (HRP) is a specific cytochemical marker for its receptor, the monosialoganglioside GM1. The binding and endocytosis of exogenous [3H]GM1 by cultured murine neuroblastoma cells (line 2A [CCl-131] ), which contain predominantly GM3, was examined by quantitative electron microscope autoradiography. The relationship between exogenous receptor, [3H]GM1, and CT HRP was studied in double labeling experiments consisting of autoradiographic demonstration of [3H]GM1 and cytochemical visualization of HRP. Exogenous [3H]GM1 was not degraded after its endocytosis by cells for 2 h at 37 degrees C. Quantitative studies showed similar grain density distributions in cells treated with [3H]GM1 alone and in cells treated with [3H]GM1 followed by CT-HRP. Qualitative studies conducted in double labeling experiments showed autoradiographic grains over the peroxidase-stained plasma membrane, lysosomes, and vesicles at the trans aspect of the Golgi apparatus. The findings indicate that exogenous glycolipid is associated with the plasmid membrane of deficient cells and undergoes endocytosis. The quantitative ultra-structural autoradiographic studies are consistent with the hypothesis that the spontaneous endocytosis of exogenous [3H]GM1 controls the subsequent uptake of CT-HRP.

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