| CADM1 enhances intestinal barrier function in a rat model of mild inflammatory bowel disease by inhibiting the STAT3 signaling pathway. | CADM1 enhances intestinal barrier function in a rat model of mild inflammatory bowel disease by inhibiting the STAT3 signaling pathway.
Sun S, Liu W, Li Y. | 07/31/2021 |
| proteins. Our results highlight a previously unexplored role for MPP2 at postsynaptic sites as a scaffold that links SynCAM1 cell adhesion molecules to core proteins of the postsynaptic density. | MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1 cell adhesion molecules to core components of the postsynaptic density.
Rademacher N, Schmerl B, Lardong JA, Wahl MC, Shoichet SA., Free PMC Article | 05/19/2018 |
| miR-21 overexpression promotes cardiac fibrosis via STAT3 signaling pathway by decrease CADM1 expression, indicating miR-21 as an important signaling molecule for cardiac fibrotic remodeling and atrial fibrillation. | miR-21 enhances cardiac fibrotic remodeling and fibroblast proliferation via CADM1/STAT3 pathway.
Cao W, Shi P, Ge JJ., Free PMC Article | 10/7/2017 |
| Our results suggest that, as in the CNS, CADM1 interactions drive exocytic site assembly and promote actin network formation. These results support the broader hypothesis that the effects of cell-cell contact on beta-cell maturation and function are mediated by the same extracellular protein interactions that drive the formation of the presynaptic exocytic machinery. These interactions may be therapeutic targets for re... | Extracellular CADM1 interactions influence insulin secretion by rat and human islet β-cells and promote clustering of syntaxin-1.
Zhang C, Caldwell TA, Mirbolooki MR, Duong D, Park EJ, Chi NW, Chessler SD., Free PMC Article | 06/10/2017 |
| increased CADM1 shedding appeared to contribute to the development of emphysema by generating alphaCTF and the ICD in lung epithelial cells. | The intracellular domain of cell adhesion molecule 1 is present in emphysematous lungs and induces lung epithelial cell apoptosis.
Hagiyama M, Yoneshige A, Inoue T, Sato Y, Mimae T, Okada M, Ito A., Free PMC Article | 04/23/2016 |
| SynCAM 1 acts in developing neurons to shape migrating growth cones and contributes to the adhesive differentiation of their axo-dendritic contacts | SynCAM 1 participates in axo-dendritic contact assembly and shapes neuronal growth cones.
Stagi M, Fogel AI, Biederer T., Free PMC Article | 11/13/2015 |
| SynCAM1 mRNA levels seem to reflect the loss and restoration of synapses on motoneurons; expression of SynCAM1 and neuroligins is regulated by different mechanisms during regeneration. | SynCAM1 expression correlates with restoration of central synapses on spinal motoneurons after two different models of peripheral nerve injury.
Zelano J, Berg A, Thams S, Hailer NP, Cullheim S. | 11/13/2015 |
| Results identify erythrocyte protein band 4.1-like 3 (protein 4.1B) as an intracellular effector molecule of Synaptic Cell Adhesion Molecule 1 (SynCAM1) that is sufficient to recruit NMDA-type receptors (NMDARs) to SynCAM1 adhesion sites in COS7 cells. | SynCAM1 recruits NMDA receptors via protein 4.1B.
Hoy JL, Constable JR, Vicini S, Fu Z, Washbourne P., Free PMC Article | 11/13/2015 |
| Our results define SynCAM proteins as components of novel heterophilic transsynaptic adhesion complexes that set up asymmetric interactions, with SynCAM proteins contributing to synapse organization and function. | SynCAMs organize synapses through heterophilic adhesion.
Fogel AI, Akins MR, Krupp AJ, Stagi M, Stein V, Biederer T., Free PMC Article | 11/13/2015 |
| SynCAM proteins are encoded by a family of four conserved IGSF4 genes found solely in vertebrates; transcripts can be alternatively spliced and encode proteins with three immunoglobulin-like domains. | Bioinformatic characterization of the SynCAM family of immunoglobulin-like domain-containing adhesion molecules.
Biederer T. | 11/13/2015 |
| a brain-specific, immunoglobulin domain-containing protein that binds to intracellular PDZ-domain proteins and functions as a homophilic cell adhesion molecule at the synapse (SynCAM; Synaptic cell adhesion molecule) | SynCAM, a synaptic adhesion molecule that drives synapse assembly.
Biederer T, Sara Y, Mozhayeva M, Atasoy D, Liu X, Kavalali ET, Südhof TC. | 11/13/2015 |
| The results indicate that SynCAM 1 expression is down-regulated in the brain after experimental subarachnoid hemorrhage. | Expression of synaptic cell adhesion molecule 1 (SynCAM 1) in different brain regions in a rat subarachnoid hemorrhage model.
Wang Z, Hu T, Feng D, Chen G. | 11/13/2015 |
| The 5' upstream region of Tslc1 was methylated in three hepatocellular hepatomas in which its expression was reduced, but was unmethylated in normal liver tissue. No change in expression lever of Dal-1 found in hepatocellular hepatomas. | Expression and DNA methylation patterns of Tslc1 and Dal-1 genes in hepatocellular carcinomas induced by N-nitrosodiethylamine in rats.
Tsujiuchi T, Sugata E, Masaoka T, Onishi M, Fujii H, Shimizu K, Honoki K. | 12/5/2011 |
| These results demonstrate a key role for Necl-2 and -4 in initiating peripheral nervous system myelination and implicate the Necl proteins as mediators of axo-glial interactions along the internode. | Nectin-like proteins mediate axon Schwann cell interactions along the internode and are essential for myelination.
Maurel P, Einheber S, Galinska J, Thaker P, Lam I, Rubin MB, Scherer SS, Murakami Y, Gutmann DH, Salzer JL., Free PMC Article | 01/21/2010 |
| These results suggest that aberrant Tslc1 gene methylation may be involved in BHP-induced development of lung adenocarcinomas in rats. | Reduced expression of the Tslc1 gene and its aberrant DNA methylation in rat lung tumors.
Shimizu K, Itsuzaki Y, Onishi M, Fujii H, Honoki K, Tsujiuchi T. | 01/21/2010 |
| We propose that SgIGSF is a novel and functional biliary epithelial cell adhesion molecule that is expressed for a limited time during active bile duct/ductule formation. | SgIGSF is a novel biliary-epithelial cell adhesion molecule mediating duct/ductule development.
Ito A, Nishikawa Y, Ohnuma K, Ohnuma I, Koma Y, Sato A, Enomoto K, Tsujimura T, Yokozaki H. | 01/21/2010 |