Caveolae (plasmalemmal vesicles)

2012 ◽  
Keyword(s):  
Plasmalemmal Vesicles

scholarly journals Distribution of sialoglycoconjugates on the luminal surface of the endothelial cell in the fenestrated capillaries of the pancreas.

1985 ◽  
Vol 33 (5) ◽  
pp. 474-476 ◽  
Author(s):  
V Muresan ◽  
M C Constantinescu
Keyword(s):  
Endothelial Cell ◽  
Vascular Endothelium ◽  
Binding Sites ◽  
Sodium Periodate ◽  
Luminal Surface ◽  
Nonspecific Binding ◽  
Coated Pits ◽  
Neuraminidase Treatment ◽  
Plasmalemmal Vesicles ◽  
Endothelial Surface

Sialic acid-bearing molecules on the luminal surface of the vascular endothelium in mouse and rat pancreatic capillaries were detected electron microscopically by using a procedure with ferritin hydrazide (FH), after preferential oxidation of sialyl residues with sodium periodate. The distribution of FH on the endothelial surface demonstrated the existence of microdomains with various densities of sialoglycoconjugates oxidizable by sodium periodate and accessible to the tracer. On the plasmalemma proper, FH binding sites were heterogeneously distributed. Their concentration on various microdomains decreased as follows: plasmalemma proper greater than coated pits greater than stomal diaphragms of plasmalemmal vesicles and transendothelial channels, and fenestral diaphragms. The membrane of plasmalemmal vesicles and transendothelial channels was not labeled by FH. Nonspecific binding of FH to the nonoxidized endothelial surface or that oxidized after neuraminidase treatment was relatively low.

scholarly journals Binding and transcytosis of glycoalbumin by the microvascular endothelium of the murine myocardium: evidence that glycoalbumin behaves as a bifunctional ligand.

1988 ◽  
Vol 107 (5) ◽  
pp. 1729-1738 ◽  
Author(s):  
D Predescu ◽  
M Simionescu ◽  
N Simionescu ◽  
G E Palade
Keyword(s):  
Intercellular Junctions ◽  
Concomitant Administration ◽  
Multivesicular Bodies ◽  
Microvascular Endothelium ◽  
Coated Pits ◽  
Gold Complexes ◽  
Plasmalemmal Vesicles ◽  
Bifunctional Ligand ◽  
Albumin Molecule

The binding and transport of glycoalbumin (gA) by the endothelium of murine myocardial microvessels were studied by perfusing in situ 125I-gA or gA-gold complexes (gA-Au) and examining the specimens by radioassays and EM, respectively. After a 3-min perfusion, the uptake of radioiodinated gA is 2.2-fold higher than that of native albumin; it is partially (approximately 55%) competed by either albumin or D-glucose, and almost completely abolished by the concomitant administration of both competitors or by gA. D-mannose and D-galactose are not effective competitors. Unlike albumin-gold complexes that bind restrictively to plasmalemmal vesicles, gA-Au labels the plasma-lemma proper, plasmalemmal vesicles open on the lumen, and most coated pits. Competing albumin prevents gA-Au binding to the membrane of plasmalemmal vesicles, while glucose significantly reduces the ligand binding to plasmalemma proper. Competition with albumin and glucose gives additive effects. Transcytosis of gA-Au, already detected at 3 min, becomes substantial by 30 min. No tracer exit via intercellular junctions was detected. gA-Au progressively accumulates in multivesicular bodies. The results of the binding and competition experiments indicate that the gA behaves as a bifunctional ligand which is recognized by two distinct binding sites: one, located on the plasma membrane, binds as a lectin the glucose residues of gA; whereas the other, confined to plasmalemmal vesicles, recognizes presumably specific domains of the albumin molecule.

Internalization via plasmalemmal vesicles: a route for antidesmoplakin autoantibodies into cultured human keratinocytes

2003 ◽  
Vol 12 (5) ◽  
pp. 546-554 ◽  
Author(s):  
Karla Cauza ◽  
Gabriele Hinterhuber ◽  
Ulrike Mann ◽  
Reinhard Horvat ◽  
Klemens Rappersberger ◽  
...  
Keyword(s):  
Human Keratinocytes ◽  
Plasmalemmal Vesicles
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