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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

F11 receptor

Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. The protein encoded by this immunoglobulin superfamily gene member is an important regulator of tight junction assembly in epithelia. In addition, the encoded protein can act as (1) a receptor for reovirus, (2) a ligand for the integrin LFA1, involved in leukocyte transmigration, and (3) a platelet receptor. Multiple 5' alternatively spliced variants, encoding the same protein, have been identified but their biological validity has not been established. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Occludin, ZO-1, JAM-C, CAN, V1a
Papers using JAMA antibodies
A network of PDZ-containing proteins regulates T cell polarity and morphology during migration and immunological synapse formation
Schwamborn Jens C et al., In BMC Neuroscience, 2004
... The following primary antibodies were used: anti-JAM-A (rabbit) [7], anti-P-H3 (mouse, New England Biolabs), anti-GFAP (mouse, Millipore), anti-Mash1 ...
Papers on JAMA
Effect of junctional adhesion molecule-2 expression on cell growth, invasion and migration in human colorectal cancer.
Jiang et al., Beijing, China. In Int J Oncol, Feb 2016
Aberrant expression of JAM-2 is associated with cancer progression but little work has been carried out in discovering how this affects changes in cell behaviour.
Effects of Bacillus subtilis on Epithelial Tight Junctions of Mice with Inflammatory Bowel Disease.
Li et al., Shenyang, China. In J Interferon Cytokine Res, Jan 2016
Analytic testing (immunohistochemical, western blot, and PCR) revealed progressive increase in TJ protein (claudin-1, occludin, JAM-A, and ZO-1) expression in DSS, DSS+B.
Segmental Differences in Radiation-Induced Alterations of Tight Junction-Related Proteins in Non-Human Primate Jejunum, Ileum and Colon.
Hauer-Jensen et al., Québec, Canada. In Radiat Res, Jan 2016
Western blot analysis revealed increased levels of claudin-2 on day 4 and of JAM-1 on day 7 postirradiation in all three gut segments.
Long Noncoding RNA SPRY4-IT1 Regulates Intestinal Epithelial Barrier Function by Modulating the Expression Levels of Tight Junction Proteins.
Wang et al., Beijing, China. In Mol Biol Cell, Jan 2016
SPRY4-IT1 silencing led to dysfunction of the epithelial barrier in cultured cells by decreasing the stability of mRNAs encoding TJ proteins claudin-1, claudin-3, occludin, and JAM-1 and by repressing their translation.
Nanoscale Imaging Reveals a Tetraspanin-CD9 Coordinated Elevation of Endothelial ICAM-1 Clusters.
Riethmüller et al., Münster, Germany. In Plos One, Dec 2015
Confocal immunofluorescence microscopy proved them positive for ICAM-1, JAM-A, tetraspanin CD9 and f-actin.
ABCG2: the molecular mechanisms of urate secretion and gout.
Woodward, Baltimore, United States. In Am J Physiol Renal Physiol, Oct 2015
JAMA 300: 924-932, 2008; Wang J, Qin T, Chen J, Li Y, Wang L, Huang H, Li J. PLoS One 9: e114259, 2014; Zhu P, Liu Y, Han L, Xu G, Ran JM.
Tight Junctions Go Viral!
Arias et al., Ecatepec, Mexico. In Viruses, Sep 2015
For example, TJ proteins such as JAM-A or some members of the claudin family of proteins are used by members of the Reoviridae family and hepatitis C virus as receptors or co-receptors during their entry into their host cells.
Leukotriene B4-Neutrophil Elastase Axis Drives Neutrophil Reverse Transendothelial Cell Migration In Vivo.
Nourshargh et al., Genève, Switzerland. In Immunity, Jul 2015
We have previously shown that neutrophils can exhibit abluminal-to-luminal migration through EC junctions within mouse cremasteric venules and that this response is elicited following reduced expression and/or functionality of the EC junctional adhesion molecule-C (JAM-C).
Architecture of tight junctions and principles of molecular composition.
Anderson et al., Bethesda, United States. In Semin Cell Dev Biol, 2014
In general the architecture can be conceptualized into compartments with the transmembrane barrier proteins (claudins, occludin, JAM-A, etc.), linked to peripheral scaffolding proteins (such as ZO-1, afadin, MAGI1, etc.) which are in turned linked to actin and microtubules through numerous linkers (cingulin, myosins, protein 4.1, etc.).
Analysis of tumour- and stroma-supplied proteolytic networks reveals a brain-metastasis-promoting role for cathepsin S.
Joyce et al., New York City, United States. In Nat Cell Biol, 2014
Cathepsin S specifically mediates blood-brain barrier transmigration through proteolytic processing of the junctional adhesion molecule, JAM-B.
Dysregulation of JAM-A plays an important role in human tumor progression.
Chen et al., Wuhan, China. In Int J Clin Exp Pathol, 2013
Junctional adhesion molecule A (JAM-A) is a transmembrane protein that belongs to the immunoglobulin (Ig) superfamily.
Platelets and their chemokines in atherosclerosis-clinical applications.
Schmitt et al., München, Germany. In Front Physiol, 2013
Platelet surface molecules GPIIb/IIIa, GP1bα, P-selectin, JAM-A and the CD40/CD40L dyade are crucially involved in the interaction with endothelial cells, leukocytes and matrix molecules affecting atherogenesis.
Compromised intestinal epithelial barrier induces adaptive immune compensation that protects from colitis.
Parkos et al., Atlanta, United States. In Immunity, 2012
Mice lacking junctional adhesion molecule A (JAM-A, encoded by F11r) exhibit enhanced intestinal epithelial permeability, bacterial translocation, and elevated colonic lymphocyte numbers, yet do not develop colitis.
Relocalization of junctional adhesion molecule A during inflammatory stimulation of brain endothelial cells.
Andjelkovic et al., Ann Arbor, United States. In Mol Cell Biol, 2012
The chemokine (C-C motif) ligand 2 (CCL2) induced JAM-A redistribution from the interendothelial cell area to the apical surface of brain endothelial cells.
CASK interacts with PMCA4b and JAM-A on the mouse sperm flagellum to regulate Ca2+ homeostasis and motility.
Martin-Deleon et al., Newark, United States. In J Cell Physiol, 2012
CASK negatively regulates PMCA4b by directly binding to it and JAM-A positively regulates it indirectly through CASK
JAM-A protects from thrombosis by suppressing integrin αIIbβ3-dependent outside-in signaling in platelets.
Naik et al., Newark, United States. In Blood, 2012
JAM-A normally limits platelet accumulation by inhibiting integrin outside-in signaling thus preventing premature platelet activation.
aPKC phosphorylates JAM-A at Ser285 to promote cell contact maturation and tight junction formation.
Ebnet et al., Münster, Germany. In J Cell Biol, 2012
Data suggest that aPKC phosphorylates JAM-A at S285 to regulate cell-cell contact maturation, TJ formation, and single lumen specification.
The junctional adhesion molecule JAM-C regulates polarized transendothelial migration of neutrophils in vivo.
Nourshargh et al., London, United Kingdom. In Nat Immunol, 2011
We noted these events in inflammation after ischemia-reperfusion injury, characterized by lower expression of junctional adhesion molecule C (JAM-C) at EC junctions, and they were enhanced by blockade or genetic deletion of JAM-C in ECs.
Transcription and translation of human F11R gene are required for an initial step of atherogenesis induced by inflammatory cytokines.
Babinska et al., New York City, United States. In J Transl Med, 2010
de novo synthesis of F11R in endothelial cells (EC) is required for the adhesion of platelets to inflamed ECs.
Tumour angiogenesis is reduced in the Tc1 mouse model of Down's syndrome.
Hodivala-Dilke et al., London, United Kingdom. In Nature, 2010
Examination of the genes on the segment of Hsa21 in Tc1 mice identified putative anti-angiogenic genes (ADAMTS1and ERG) and novel endothelial cell-specific genes, never previously shown to be involved in angiogenesis (JAM-B and PTTG1IP), that, when overexpressed, are responsible for inhibiting angiogenic responses to VEGF.
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