scholarly journals JAM-C Is a Component of Desmosomes and a Ligand for CD11b/CD18-mediated Neutrophil Transepithelial Migration

2004 ◽  
Vol 15 (8) ◽  
pp. 3926-3937 ◽  
Author(s):  
Ke Zen ◽  
Brian A. Babbin ◽  
Yuan Liu ◽  
John B. Whelan ◽  
Asma Nusrat ◽  
...  
Keyword(s):  
Structure Function ◽  
Family Member ◽  
Tight Junctions ◽  
Specific Binding ◽  
Intercellular Junctions ◽  
Protein Family ◽  
Intestinal Epithelia ◽  
Adhesive Interactions

Neutrophil (PMN) transepithelial migration is dependent on the leukocyte β2integrin CD11b/CD18, yet the identity of epithelial counterreceptors remain elusive. Recently, a JAM protein family member termed JAM-C was implicated in leukocyte adhesive interactions; however, its expression in epithelia and role in PMN-epithelial interactions are unknown. Here, we demonstrate that JAM-C is abundantly expressed basolaterally in intestinal epithelia and localizes to desmosomes but not tight junctions. Desmosomal localization of JAM-C was further confirmed by experiments aimed at selective disruption of tight junctions and desmosomes. In assays of PMN transepithelial migration, both JAM-C mAbs and JAM-C/Fc chimeras significantly inhibited the rate of PMN transmigration. Additional experiments revealed specific binding of JAM-C to CD11b/CD18 and provided evidence of other epithelial ligands for CD11b/CD18. These findings represent the first demonstration of direct adhesive interactions between PMN and epithelial intercellular junctions (desmosomes) that regulate PMN transepithelial migration and also suggest that JAM-C may play a role in desmosomal structure/function.

scholarly journals Neutrophil Migration across Tight Junctions Is Mediated by Adhesive Interactions between Epithelial Coxsackie and Adenovirus Receptor and a Junctional Adhesion Molecule-like Protein on Neutrophils

2005 ◽  
Vol 16 (6) ◽  
pp. 2694-2703 ◽  
Author(s):  
Ke Zen ◽  
Yuan Liu ◽  
Ingrid C. McCall ◽  
Tao Wu ◽  
Winston Lee ◽  
...  
Keyword(s):  
Tight Junctions ◽  
Adhesion Molecule ◽  
Specific Binding ◽  
Neutrophil Migration ◽  
Independent Manner ◽  
Coxsackie And Adenovirus Receptor ◽  
Cell Monolayers ◽  
Adhesive Interactions ◽  
Multistep Model ◽  
Adenovirus Receptor

Neutrophil (polymorphonuclear leukocytes [PMN]) transepithelial migration during inflammatory episodes involves a complex series of adhesive interactions and signaling events. Previous studies have shown that key adhesive interactions between leukocyte CD11b/CD18 and basally expressed fucosylated glycoproteins followed by binding to desmosomal-associated JAM-C are key elements of the transmigration response. Here we provide the first evidence that PMN-expressed junctional adhesion molecule-like protein (JAML) regulates transmigration via binding interactions with epithelial coxsackie and adenovirus receptor (CAR). Experiments with a JAML fusion protein revealed specific binding of JAML to epithelial CAR expressed at tight junctions in T84 cell monolayers and normal human colonic mucosa. Furthermore, JAML-CAR binding is mediated via the membrane distal immunoglobulin (Ig) loop of CAR and the membrane proximal Ig loop of JAML. PMN bound to immobilized CAR but not JAML in a divalent cation-independent manner. Lastly, in assays of PMN transepithelial migration, JAML/CAR fusion proteins and their antibodies significantly inhibited transmigration in a specific manner. Taken together, these results indicate that JAML and CAR are a novel pair of adhesion molecules that play an important role in modulating PMN migration cross epithelial tight junctions. These findings add a new element to a multistep model of PMN transepithelial migration and may provide new targets for anti-inflammatory therapies.

scholarly journals Cloning and expression of a novel cysteine-rich secreted protein family member expressed in thyroid and pancreatic mesoderm within the chicken embryo

2001 ◽  
Vol 102 (1-2) ◽  
pp. 223-226 ◽  
Author(s):  
Devyn M. Smith ◽  
Lisa A. Collins-Racie ◽  
Valeria A. Marigo ◽  
Drucilla J. Roberts ◽  
Nicole M. Davis ◽  
...  
Keyword(s):  
Family Member ◽  
Chicken Embryo ◽  
Protein Family ◽  
Cloning And Expression ◽  
Secreted Protein

Tight junctions

1998 ◽  
Vol 111 (5) ◽  
pp. 541-547 ◽  
Author(s):  
M.S. Balda ◽  
K. Matter
Keyword(s):  
Endothelial Cells ◽  
Cell Growth ◽  
Tight Junctions ◽  
Diffusion Barrier ◽  
Basolateral Membrane ◽  
Intercellular Junctions ◽  
Cellular Level ◽  
Cellular Processes ◽  
Cell Growth And Differentiation ◽  
Membrane Components

Tight junctions are the most apical intercellular junctions of epithelial and endothelial cells and create a regulatable semipermeable diffusion barrier between individual cells. On a cellular level, they form an intramembrane diffusion fence that restricts the intermixing of apical and basolateral membrane components. In addition to these well defined functions, more recent evidence suggests that tight junctions are also involved in basic cellular processes like the regulation of cell growth and differentiation.

scholarly journals Capped mRNA Degradation Intermediates Accumulate in the Yeast spb8-2 Mutant

1998 ◽  
Vol 18 (9) ◽  
pp. 5062-5072 ◽  
Author(s):  
Ronald Boeck ◽  
Bruno Lapeyre ◽  
Christine E. Brown ◽  
Alan B. Sachs
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Family Member ◽  
Gene Deletion ◽  
Binding Protein ◽  
Mrna Degradation ◽  
Protein Family ◽  
Suppressor Mutation ◽  
Mrna Decapping ◽  
Mrna Species ◽  
Degradation Intermediates

ABSTRACT mRNA in the yeast Saccharomyces cerevisiae is primarily degraded through a pathway that is stimulated by removal of the mRNA cap structure. Here we report that a mutation in the SPB8(YJL124c) gene, initially identified as a suppressor mutation of a poly(A)-binding protein (PAB1) gene deletion, stabilizes the mRNA cap structure. Specifically, we find that thespb8-2 mutation results in the accumulation of capped, poly(A)-deficient mRNAs. The presence of this mutation also allows for the detection of mRNA species trimmed from the 3′ end. These data show that this Sm-like protein family member is involved in the process of mRNA decapping, and they provide an example of 3′-5′ mRNA degradation intermediates in yeast.

scholarly journals The prion protein family member Shadoo induces spontaneous ionic currents in cultured cells

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Antal Nyeste ◽  
Claudia Stincardini ◽  
Petra Bencsura ◽  
Milica Cerovic ◽  
Emiliano Biasini ◽  
...  
Keyword(s):  
Family Member ◽  
Prion Protein ◽  
Cultured Cells ◽  
Ionic Currents ◽  
Protein Family

scholarly journals Expression of the Prion Protein Family Member Shadoo Causes Drug Hypersensitivity That Is Diminished by the Coexpression of the Wild Type Prion Protein

2015 ◽  
Vol 291 (9) ◽  
pp. 4473-4486 ◽  
Author(s):  
Antal Nyeste ◽  
Petra Bencsura ◽  
István Vida ◽  
Zoltán Hegyi ◽  
László Homolya ◽  
...  
Keyword(s):  
Family Member ◽  
Prion Protein ◽  
Drug Hypersensitivity ◽  
Protein Family ◽  
Wild Type
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