Apical membrane receptors on intestinal M cells: potential targets for vaccine delivery

2004 ◽  
Vol 56 (6) ◽  
pp. 721-726 ◽  
Author(s):  
D Brayden
Keyword(s):  
Apical Membrane ◽  
Vaccine Delivery ◽  
Membrane Receptors ◽  
M Cells

M cells expressing the complement C5a receptor are efficient targets for mucosal vaccine delivery

2011 ◽  
Vol 41 (11) ◽  
pp. 3219-3229 ◽  
Author(s):  
Sae-Hae Kim ◽  
Dae-Im Jung ◽  
In-Young Yang ◽  
Ju Kim ◽  
Kyung-Yeol Lee ◽  
...  
Keyword(s):  
Vaccine Delivery ◽  
Mucosal Vaccine ◽  
M Cells ◽  
C5a Receptor ◽  
Complement C5a

scholarly journals Cellular remodeling of HCO3(-)-secreting cells in rabbit renal collecting duct in response to an acidic environment.

1989 ◽  
Vol 109 (3) ◽  
pp. 1279-1288 ◽  
Author(s):  
L M Satlin ◽  
G J Schwartz
Keyword(s):  
Apical Membrane ◽  
Collecting Duct ◽  
Low Ph ◽  
Membrane Receptors ◽  
Intercalated Cells ◽  
Cortical Collecting Duct ◽  
Similar Reduction ◽  
Fourfold Increase ◽  
Principal And Intercalated Cells

The renal cortical collecting duct (CCD) consists of principal and intercalated cells. Two forms of intercalated cells, those cells involved in H+/HCO3- transport, have recently been described. H+-secreting cells are capable of apical endocytosis and have H+ATPase on the apical membrane and a basolateral Cl-/HCO3- exchanger. HCO3(-)-secreting cells bind peanut agglutinin (PNA) to apical membrane receptors and have diffuse or basolateral distribution of H+ATPase; their Cl-/HCO3- exchanger is on the apical membrane. We found that 20 h after acid feeding of rabbits, there was a fourfold increase in number of cells showing apical endocytosis and a numerically similar reduction of cells binding PNA. Incubation of CCDs at pH 7.1 for 3-5 h in vitro led to similar, albeit less pronounced, changes. Evidence to suggest internalization and degradation of the PNA binding sites included a reduction in apical binding of PNA, decrease in pH in the environment of PNA binding, and incorporation of electron-dense PNA into cytoplasmic vesicles. Such remodeling was dependent on protein synthesis. There was also functional evidence for loss of apical Cl-/HCO3- exchange on PNA-labeled cells. Finally, net HCO3- flux converted from secretion to absorption after incubation at low pH. Thus, exposure of CCDs to low pH stimulates the removal/inactivation of apical Cl-/HCO3- exchangers and the internalization of other apical membrane components. Remodeling of PNA-labeled cells may mediate the change in polarity of HCO3- flux observed in response to acid treatment.

Functionalized nanoparticles for targeting the gastrointestinal apical membrane receptors

2016 ◽  
pp. 140-164
Author(s):  
Francisca Araújo ◽  
Carla Pereira ◽  
Hélder A Santos ◽  
Pedro Granja ◽  
Bruno Sarmento
Keyword(s):  
Apical Membrane ◽  
Membrane Receptors ◽  
Functionalized Nanoparticles

β-Cyclodextrin and permeability to water in the bladder of Bufo arenarum

2011 ◽  
Vol 89 (5) ◽  
pp. 311-315 ◽  
Author(s):  
G. Orce ◽  
G. Castillo ◽  
Y. Chanampa
Keyword(s):  
Apical Membrane ◽  
Basolateral Membrane ◽  
Membrane Receptors ◽  
Cholesterol Depletion ◽  
Intracellular Camp ◽  
Osmotic Gradient ◽  
Apical Side ◽  
Solution Bathing ◽  
Membrane Components ◽  
Hydrolysis Of

We measured the effect of β-cyclodextrin (BCD, a cholesterol scavenger) on water flow across the isolated toad bladder exposed to an osmotic gradient (Jw) by a gravimetric technique. BCD, when present in the solution bathing the apical side of the bladder, inhibited the increase in Jw caused by nystatin, a polyene antibiotic that acts by directly binding apical membrane cholesterol. When present in the basolateral bath, BCD inhibited the increase in Jw caused by basolateral exposure to oxytocin (which binds membrane receptors and stimulates the synthesis of cAMP), but did not alter the response to theophylline (which inhibits hydrolysis of cAMP by cyclic nucleotide phosphodiesterase). The present data are consistent with the notion that agents that increase Jw by interacting with membrane receptors, which appear to be clustered in cholesterol-rich domains of the basolateral membrane, are altered by cholesterol depletion, whereas agents that do not interact with receptors or other basolateral membrane components are not affected by this treatment. In either case, cholesterol depletion of the apical membrane does not affect the increase in Jw brought about by an increase in intracellular cAMP concentration.

scholarly journals Glycocalyx on Rabbit Intestinal M Cells Displays Carbohydrate Epitopes from Muc2

2001 ◽  
Vol 69 (2) ◽  
pp. 1061-1071 ◽  
Author(s):  
Hugues Lelouard ◽  
Hubert Reggio ◽  
Christian Roy ◽  
Alain Sahuquet ◽  
Paul Mangeat ◽  
...  
Keyword(s):  
Apical Membrane ◽  
Lymphoid Tissues ◽  
M Cells ◽  
Apical Surface ◽  
M Cell ◽  
Luminal Membrane ◽  
Carbohydrate Epitopes ◽  
Intestinal Mucin ◽  
Rabbit Appendix

ABSTRACT It is essential to investigate the apical surface properties of both M cells and dome enterocytes to understand the mechanisms involved in the binding of pathogens to M cells. In rabbit appendix tissue, monoclonal antibodies (MAbs) highlight differences between M cells (MAb 58) and dome enterocytes (MAb 214). Such antibodies ultimately recognized intestinal mucin-related epitopes. To further characterize these differences, the labeling patterns obtained with these MAbs were compared to those obtained with other antibodies to intestinal mucins on dissected domes from all gut-associated lymphoid tissues. A glycoprotein recognized by MAb 58 was purified on a CsCl isopycnic density gradient and microsequenced, and its mRNA expression was localized by in situ hybridization. It was identified as the rabbit homologue of human Muc2, i.e., the major mucin secreted in intestine tissue. Two other Muc2 carbohydrate epitopes were also expressed on M cells, although Muc2 mRNA was not detected. All results indicated that M cells express, on their apical membrane, glycoconjugates bearing at least three glycosidic epitopes from Muc2. MAb 214 and MAb 6G2, which recognized a partially characterized mucin expressed on dome enterocytes, were negative markers for M cells in rabbit gut-associated lymphoid tissues. We propose that the presence, on the surface of M cells, of carbohydrates also expressed on Muc2, together with the absence of an enterocyte-associated mucin, could favor pathogen attachment and accessibility to the M-cell luminal membrane.

Role of PKC isozymes in water transport in toad urinary bladder

1991 ◽  
Vol 49 ◽  
pp. 302-303
Author(s):  
A.J. Mia ◽  
L.X. Oakford ◽  
T. Yorio
Keyword(s):  
Urinary Bladder ◽  
Apical Membrane ◽  
Membrane Surface ◽  
Protein A ◽  
Cell Types ◽  
Leukemic Cells ◽  
Toad Urinary Bladder ◽  
Pkc Isozymes ◽  
Antibody Labeling

Protein kinase C (PKC) isozymes, when activated, are translocated to particulate membrane fractions for transport to the apical membrane surface in a variety of cell types. Evidence of PKC translocation was demonstrated in human megakaryoblastic leukemic cells, and in cardiac myocytes and fibroblasts, using FTTC immunofluorescent antibody labeling techniques. Recently, we reported immunogold localizations of PKC subtypes I and II in toad urinary bladder epithelia, following 60 min stimulation with Mezerein (MZ), a PKC activator, or antidiuretic hormone (ADH). Localization of isozyme subtypes I and n was carried out in separate grids using specific monoclonal antibodies with subsequent labeling with 20nm protein A-gold probes. Each PKC subtype was found to be distributed singularly and in discrete isolated patches in the cytosol as well as in the apical membrane domains. To determine if the PKC isozymes co-localized within the cell, a double immunogold labeling technique using single grids was utilized.

On the Precipice: Private-Sector Vaccine Delivery

2006 ◽  
Vol 40 (4) ◽  
pp. 23
Author(s):  
STUART A. COHEN
Keyword(s):  
Private Sector ◽  
Vaccine Delivery

Earlier Is Better for Vaccine Delivery in Teens

2007 ◽  
Vol 41 (4) ◽  
pp. 20-21
Author(s):  
DIANA MAHONEY
Keyword(s):  
Vaccine Delivery
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