Analysis of receptor binding by the channel-forming toxin aerolysin using surface plasmon resonance. (1/114)
Aerolysin is a channel-forming bacterial toxin that binds to glycosylphosphatidylinositol (GPI) anchors on host cell-surface structures. The nature of the receptors and the location of the receptor-binding sites on the toxin molecule were investigated using surface plasmon resonance. Aerolysin bound to the GPI-anchored proteins Thy-1, variant surface glycoprotein, and contactin with similar rate constants and affinities. Enzymatic removal of N-linked sugars from Thy-1 did not affect toxin binding, indicating that these sugars are not involved in the high affinity interaction with aerolysin. Aerolysin is a bilobal protein, and both lobes were shown to be required for optimal binding. The large lobe by itself bound Thy-1 with an affinity that was at least 10-fold weaker than that of the whole toxin, whereas the small lobe bound the GPI-anchored protein at least 1000-fold more weakly than the intact toxin. Mutation analyses provided further evidence that both lobes were involved in GPI anchor binding, with certain single amino acid substitutions in either domain leading to reductions in affinity of as much as 100-fold. A variant with single amino acid substitutions in both lobes of the protein was completely unable to bind the receptor. The membrane protein glycophorin, which is heavily glycosylated but not GPI-anchored, bound weakly to immobilized proaerolysin, suggesting that interactions with cell-surface carbohydrate structures other than GPI anchors may partially mediate toxin binding to host cells. (+info)Functional interactions of the immunoglobulin superfamily member F11 are differentially regulated by the extracellular matrix proteins tenascin-R and tenascin-C. (2/114)
The axon-associated protein F11 is a GPI-anchored member of the immunoglobulin superfamily that promotes axon outgrowth and that shows a complex binding pattern toward multiple cell surface and extracellular matrix proteins including tenascin-R and tenascin-C. In this study, we demonstrate that tenascin-R and tenascin-C differentially modulate cell adhesion and neurite outgrowth of tectal cells on F11. While soluble tenascin-R increases the number of attached cells and the percentage of cells with neurites on immobilized F11, tenascin-C stimulates cell attachment to a similar extent but decreases neurite outgrowth. The cellular receptor interacting with F11 has been previously identified as NrCAM; however, in the presence of tenascin-R or tenascin-C cell attachment and neurite extension are independent of NrCAM. Antibody perturbation experiments indicate that beta(1) integrins instead of NrCAM function as receptor for neurite outgrowth of tectal cells on an F11.TN-R complex. Cellular binding assays support the possibility that the interaction of F11 to NrCAM is blocked in the presence of tenascin-R and tenascin-C. Furthermore, a sandwich binding assay demonstrates that tenascin-R and tenascin-C are able to form larger molecular complexes and to link F11 polypeptides by forming a molecular bridge. These results suggest that the molecular interactions of F11 might be regulated by the presence of tenascin-R and tenascin-C. (+info)NrCAM, cerebellar granule cell receptor for the neuronal adhesion molecule F3, displays an actin-dependent mobility in growth cones. (3/114)
The neuronal adhesion glycoprotein F3 is a multifunctional molecule of the immunoglobulin superfamily that displays heterophilic binding activities. In the present study, NrCAM was identified as the functional receptor mediating the inhibitory effect of F3 on axonal elongation from cerebellar granule cells. F3Fc-conjugated microspheres binding to neuronal growth cones resulted from heterophilic interaction with NrCAM but not with L1. Time-lapse video-microscopy indicated that F3Fc beads bind at the leading edge and move retrogradely to reach the base of the growth cone within a lapse of 30-60 seconds. Such velocity (5.7 microm/minute) is consistent with a coupling between F3 receptors and the retrograde flow of actin filaments. When actin filaments were disrupted by cytochalasin B, the F3Fc beads remained immobile at the leading edge. The retrograde mobility appeared to be dependent on NrCAM clustering since it was induced upon binding with cross-linked but not dimeric F3Fc chimera. These data indicate that F3 may control growth cone motility by modulating the linkage of its receptor, NrCAM, to the cytoskeleton. They provide further insights into the mechanisms by which GPI-anchored adhesion molecules may exert an inhibitory effect on axonal elongation. (+info)Pathological missense mutations of neural cell adhesion molecule L1 affect homophilic and heterophilic binding activities. (4/114)
Mutations in the gene for neural cell adhesion molecule L1 (L1CAM) result in a debilitating X-linked congenital disorder of brain development. At the neuronal cell surface L1 may interact with a variety of different molecules including itself and two other CAMs of the immunoglobulin superfamily, axonin-1 and F11. However, whether all of these interactions are relevant to normal or abnormal development has not been determined. Over one-third of patient mutations are single amino acid changes distributed across 10 extracellular L1 domains. We have studied the effects of 12 missense mutations on binding to L1, axonin-1 and F11 and shown for the first time that whereas many mutations affect all three interactions, others affect homophilic or heterophilic binding alone. Patient pathology is therefore due to different types of L1 malfunction. The nature and functional consequence of mutation is also reflected in the severity of the resultant phenotype with structural mutations likely to affect more than one binding activity and result in early mortality. Moreover, the data indicate that several extracellular domains of L1 are required for homophilic and heterophilic interactions. (+info)Compartmentation of Fyn kinase with glycosylphosphatidylinositol-anchored molecules in oligodendrocytes facilitates kinase activation during myelination. (5/114)
In many cell types, glycosylphosphatidylinositol (GPI)-anchored proteins are sequestered in detergent-resistant membrane rafts. These are plasma membrane microdomains enriched in glycosphingolipids and cholesterol and are suggested to be platforms for cell signaling. Concomitant with the synthesis of myelin glycosphingolipids, maturing oligodendrocytes progressively associate GPI-anchored proteins, including the adhesion molecules NCAM 120 and F3, in rafts. Here we show that these microdomains include Fyn and Lyn kinases. Both kinases are maximally active in myelin prepared from young animals, correlating with early stages of myelination. In the rafts, Fyn kinase is tightly associated with NCAM 120 and F3. In contrast, in oligodendrocyte progenitor cells lacking rafts or in raft-free membrane domains of more mature cells, F3 does not associate with Fyn. The addition of anti-F3 antibodies to oligodendrocytes results in stimulation of Fyn kinase specifically in rafts. Compartmentation of oligodendrocyte GPI-anchored proteins in rafts is thus a prerequisite for association with Fyn, permitting kinase activation. Interaction of oligodendrocyte F3 with axonal ligands such as L1 and ensuing kinase activation may play a crucial role in initiating myelination. (+info)Amyloid precursor protein, although partially detergent-insoluble in mouse cerebral cortex, behaves as an atypical lipid raft protein. (6/114)
Lipid rafts are regions of the plasma membrane that are enriched in cholesterol, glycosphingolipids and acylated proteins, and which have been proposed as sites for the proteolytic processing of the Alzheimer's amyloid precursor protein (APP). Lipid rafts can be isolated on the basis of their insolubility in Triton X-100 at 4 degrees C, with the resulting low-density, detergent-insoluble glycolipid-enriched fraction (DIG) being isolated by flotation through a sucrose density gradient. The detergent-insolubility of APP in mouse cerebral cortex relative to a variety of DIG marker proteins (alkaline phosphatase, flotillin, F3 protein and prion protein) and non-DIG proteins (alkaline phosphodiesterase I, aminopeptidase A and clathrin) has been examined. Alkaline phosphatase, flotillin, F3 protein and the prion protein were present exclusively in the DIG region of the sucrose gradient over a range of protein/detergent ratios used to solubilize the membranes and displayed a characteristic enrichment in the low-density fraction as the protein/detergent ratio was decreased. In contrast, most of the APP, alkaline phosphodiesterase I, aminopeptidase A and clathrin was effectively solubilized at all of the protein/detergent ratios examined. However, a minor proportion of these latter proteins was detected in DIGs at levels which remained constant irrespective of the protein/detergent ratio. When DIGs were isolated from the sucrose gradients and treated with excess Triton X-100, both the DIG marker proteins and APP, alkaline phosphodiesterase I and clathrin were predominantly resistant to detergent extraction at 37 degrees C. These results show that, although a minor proportion of APP is present in DIGs, where it is detergent-insoluble even at 37 degrees C, it behaves as an atypical lipid raft protein and raises questions as to whether lipid rafts are a site for its proteolytic processing. (+info)Protein tyrosine phosphatase alpha (PTPalpha) and contactin form a novel neuronal receptor complex linked to the intracellular tyrosine kinase fyn. (7/114)
Glycosyl phosphatidylinositol (GPI)-linked receptors and receptor protein tyrosine phosphatases (RPTPs), both play key roles in nervous system development, although the molecular mechanisms are largely unknown. Despite lacking a transmembrane domain, GPI receptors can recruit intracellular src family tyrosine kinases to receptor complexes. Few ligands for the extracellular regions of RPTPs are known, relegating most to the status of orphan receptors. We demonstrate that PTPalpha, an RPTP that dephosphorylates and activates src family kinases, forms a novel membrane-spanning complex with the neuronal GPI-anchored receptor contactin. PTPalpha and contactin associate in a lateral (cis) complex mediated through the extracellular region of PTPalpha. This complex is stable to isolation from brain lysates or transfected cells through immunoprecipitation and to antibody-induced coclustering of PTPalpha and contactin within cells. This is the first demonstration of a receptor PTP in a cis configuration with another cell surface receptor, suggesting an additional mode for regulation of a PTP. The transmembrane and catalytic nature of PTPalpha indicate that it likely forms the transducing element of the complex, and we postulate that the role of contactin is to assemble a phosphorylation-competent system at the cell surface, conferring a dynamic signal transduction capability to the recognition element. (+info)Ataxia and abnormal cerebellar microorganization in mice with ablated contactin gene expression. (8/114)
Axon guidance and target recognition depend on neuronal cell surface receptors that recognize and elicit selective growth cone responses to guidance cues in the environment. Contactin, a cell adhesion/recognition molecule of the immunoglobulin gene superfamily, regulates axon growth and fasciculation in vitro, but its role in vivo is unknown. To assess its function in the developing nervous system, we have ablated contactin gene expression in mice. Contactin-/- mutants displayed a severe ataxic phenotype consistent with defects in the cerebellum and survived only until postnatal day 18. Analysis of the contactin-/- mutant cerebellum revealed defects in granule cell axon guidance and in dendritic projections from granule and Golgi cells. These results demonstrate that contactin controls axonal and dendritic interactions of cerebellar interneurons and contributes to cerebellar microorganization. (+info)
Electron tomography of paranodal septate-like junctions and the associated axonal and glial cytoskeletons in the central...
Characterization of the 5 and promoter regions of the gene encoding the mouse neuronal cell adhesion molecule F3. - PubMed -...
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Contactin
Contactins are a subgroup of molecules belonging to the immunoglobulin superfamily that are expressed exclusively in the ... The subgroup consists of six members now referred to as contactin 1-6, but historically they had different names as shown in ... the table below: Shimoda, Yasushi; Watanabe, Kazutada (1 January 2009). "Contactins". Cell Adh Migr. 3 (1): 64-70. PMC 2675151 ...
Contactin 3
Contactin-3 is a protein that in humans is encoded by the CNTN3 gene. GRCh38: Ensembl release 89: ENSG00000113805 - Ensembl, ... "Entrez Gene: CNTN3 contactin 3 (plasmacytoma associated)". Human CNTN3 genome location and CNTN3 gene details page in the UCSC ... 2001). "Human NB-2 of the contactin subgroup molecules: chromosomal localization of the gene (CNTN5) and distinct expression ...
Contactin 1
... , also known as CNTN1, is a protein which in humans is encoded by the CNTN1 gene. The protein encoded by this gene ... "Entrez Gene: CNTN1 contactin 1". Sakurai T, Lustig M, Nativ M, Hemperly JJ, Schlessinger J, Peles E, Grumet M (Feb 1997). " ... Berglund EO, Ranscht B (Jun 1994). "Molecular cloning and in situ localization of the human contactin gene (CNTN1) on ... Berglund EO, Ranscht B (Jun 1994). "Molecular cloning and in situ localization of the human contactin gene (CNTN1) on ...
Contactin 6
... contactin 6, and contactin 4 candidate chromosome 3p26pter tumor suppressor genes in ovarian cancer". International Journal of ... Contactin 6 is a protein in humans that is encoded by the CNTN6 gene. The protein encoded by this gene is a member of the ... "Entrez Gene: Contactin 6". Manderson EN, Birch AH, Shen Z, Mes-Masson AM, Provencher D, Tonin PN (May 2009). "Molecular genetic ... Contactin-6) at the PDBe-KB. v t e (Articles with short description, Short description matches Wikidata, Genes on human ...
Contactin 2
Contactin-2 is a protein that in humans is encoded by the CNTN2 gene. The protein encoded by this gene is a member of the ... "Entrez Gene: CNTN2 contactin 2 (axonal)". Traka M, Goutebroze L, Denisenko N, Bessa M, Nifli A, Havaki S, Iwakura Y, Fukamauchi ...
Contactin 4
Contactin-4 is a protein that in humans is encoded by the CNTN4 gene. The protein encoded by this gene is a member of the ... 2006). "The contactin 4 gene locus at 3p26 is a candidate gene of SCA16". Neurology. 67 (7): 1236-41. doi:10.1212/01.wnl. ... "Entrez Gene: CNTN4 contactin 4". "Gene for brain connections linked with autism". www.newsdaily.com. Archived from the original ... 2004). "Disruption of contactin 4 (CNTN4) results in developmental delay and other features of 3p deletion syndrome". Am. J. ...
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CNTNAP2
Contactin-associated protein-like 2 is a protein that in humans is encoded by the CNTNAP2 gene. Since the most recent reference ... "Entrez Gene: CNTNAP2 contactin associated protein-like 2". Ashley, Euan A. (16 August 2016). "Towards precision medicine". ... Nakabayashi K, Scherer SW (April 2001). "The human contactin-associated protein-like 2 gene (CNTNAP2) spans over 2 Mb of DNA at ... Overview of all the structural information available in the PDB for UniProt: Q9UHC6 (Contactin-associated protein-like 2) at ...
CNTNAP4
Contactin-associated protein-like 4 is a protein that in humans is encoded by the CNTNAP4 gene. This gene product belongs to ... "Entrez Gene: CNTNAP4 contactin associated protein-like 4". Human CNTNAP4 genome location and CNTNAP4 gene details page in the ...
Node of Ranvier
... such as tenascin R and the cell-adhesion molecules neurofascin and contactin. Contactin is also present at nodes in the CNS and ... At CNS nodes, the axonal proteins also include contactin; however, Schwann cell microvilli are replaced by astrocyte perinodal ...
Sodium channel
Contactin, also known as F3 or F11, associates with beta 1 as shown via co-immunoprecipitation. Fibronectin-like (FN-like) ... Shah BS, Rush AM, Liu S, Tyrrell L, Black JA, Dib-Hajj SD, Waxman SG (August 2004). "Contactin associates with sodium channel ... "Contactin associates with Na+ channels and increases their functional expression". The Journal of Neuroscience. 21 (19): 7517- ...
NFASC
Gollan L, Salomon D, Salzer JL, Peles E (December 2003). "Caspr regulates the processing of contactin and inhibits its binding ... "Neurofascin is a glial receptor for the paranodin/Caspr-contactin axonal complex at the axoglial junction". Current Biology. 12 ...
Andrew D. Huberman
"Contactin-4 mediates axon-target specificity and functional development of the accessory optic system". Neuron. 86 (4): 985-999 ...
L1 family
... members also bind "heterophilically" to members of the contactin or CNTN1 family. L1 family members bind to many ...
CASPR
"Entrez Gene: Contactin associated protein 1". "OMIM Entry- * 602346 - CONTACTIN-ASSOCIATED PROTEIN 1; CNTNAP1". omim.org. ... "Contactin-Associated Protein (Caspr) and Contactin Form a Complex That Is Targeted to the Paranodal Junctions during ... CASPR also known as Contactin associated protein 1, Paranodin and CASPR1 is a protein that in humans is encoded by the CNTNAP1 ... The gene product was initially identified as a 190-kD protein associated with the contactin-PTPRZ1 complex. The 1,384-amino ...
Heritability of autism
January 2008). "Molecular cytogenetic analysis and resequencing of contactin associated protein-like 2 in autism spectrum ...
Anti-VGKC-complex encephalitis
5 had antibodies against Contactin-2 and 18 (19%) had antibodies with unknown specificity. Of the patients with Contactin-2 ... 2010). "Antibodies to Kv1 potassium channel-complex proteins leucine-rich, glioma inactivated 1 protein and contactin- ... 19 had antibodies reacting with Contactin-associated protein 2 (CASPR 2), ...
Generalized epilepsy with febrile seizures plus
This extracellular region is similar to the cell adhesion molecule contactin and other cell adhesion molecules. It is believed ...
Sulfatide
In order to form a paranodal junction, Caspr and contactin form a complex with neurofascin 155. It has been shown that ... neurofascin 155 protein clusters then bring Caspr and contactin into the membrane to form the complex, which allows the ...
SCN3A
Shah BS, Rush AM, Liu S, Tyrrell L, Black JA, Dib-Hajj SD, Waxman SG (August 2004). "Contactin associates with sodium channel ...
Septate junction
Faivre-Sarrailh C, Banerjee S, Li J, Hortsch M, Laval M, Bhat MA (October 2004). "Drosophila contactin, a homolog of vertebrate ... contactin, is required for septate junction organization and paracellular barrier function". Development. 131 (20): 4931-42. ...
Compton-North congenital myopathy
"Mutations in contactin-1, a neural adhesion and neuromuscular junction protein, cause a familial form of lethal congenital ...
NRCAM
1997). "Induction of neurite outgrowth through contactin and Nr-CAM by extracellular regions of glial receptor tyrosine ...
CEE 7 standard AC plugs and sockets
Schuko is an abbreviation for the German word Schutzkontakt, which means "Protective contact" - in this case "protective" ...
Inflammatory demyelinating diseases of the central nervous system
... contactin 1 (CNTN1), contactin associated protein 1 (CASPR1) and gliomedin. All of them nodal and paranodal proteins. Several ...
Chronic inflammatory demyelinating polyneuropathy
Autoantibodies to components of the Ranvier nodes, specially autoantibodies the Contactin-associated protein 1 (CASPR), cause a ... contactin-1 and caspr-1. These cases are special not only because of their pathology, but also because they are non-responsive ...
ARFGEF1
Kamei Y, Takeda Y, Teramoto K, Tsutsumi O, Taketani Y, Watanabe K (Oct 2000). "Human NB-2 of the contactin subgroup molecules: ...
SCN1B
... beta1 subunit-mediated modulation of Nav1.2 currents and cell surface density is dependent on interactions with contactin and ...
SCN2A
... beta1 subunit-mediated modulation of Nav1.2 currents and cell surface density is dependent on interactions with contactin and ...
Multiple sclerosis research
... contactin 1 (CNTN1), contactin associated protein 1 (CASPR1) and gliomedin. All of them nodal and paranodal proteins. Anti-TNF ...
Antibodies to neurofascin, contactin-1, and contactin-associated protein 1 in CIDP: Clinical relevance of IgG isotype
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Antibodies to neurofascin, contactin-1, and contactin-associated protein 1 in CIDP | Neurology Neuroimmunology &...
Antibodies to neurofascin, contactin-1, and contactin-associated protein 1 in CIDP. Clinical relevance of IgG isotype. Andrea ... Antibodies to cell adhesion molecules of the paranodal complex, neurofascin-155 (Nfasc155), contactin-1 (CNTN1), and contactin- ... Antibodies to neurofascin, contactin-1, and contactin-associated protein 1 in CIDP ... ANOVA = analysis of variance; Caspr1 = contactin-associated protein 1; CNTN1 = contactin-1; GFP = green fluorescent protein; ...
Neurofascin-1551
- Methods Antibodies to neurofascin-155 (Nfasc155), neurofascin-140/186 (Nfasc140/186), contactin-1 (CNTN1), and contactin-associated protein 1 (Caspr1) were detected with ELISA and/or cell-based assay. (neurology.org)
CNTN11
- The concurrence of anti-contactin 1 (CNTN1) antibody-associated chronic inflammatory demyelinating polyneuropathy (CIDP) and membranous nephropathy (MN) has previously been reported in the literature. (frontiersin.org)
Protein2
- 1) We identified a de novo chromosome 7q inversion disrupting Autism susceptibility candidate 2 (AUTS2) and Contactin Associated Protein-Like 2 (CNTNAP2) in a child with cognitive and social delay. (hacettepe.edu.tr)
- Genotype-phenotype correlation in contactin-associated protein-like 2 (CNTNAP-2) developmental disorder. (cdc.gov)
Adhesion2
- We identified Contactin as the adhesion molecule responsible for this phenotype. (houstonmethodist.org)
- We show that Contactin expression is related to IKAP expression, suggesting that IKAP regulates Contactin levels for appropriate cell-cell adhesion that could modulate neuronal growth of PNS neurons during development. (houstonmethodist.org)
Developmental1
- This wide role in neural ontogenesis is consistent with the recognized interaction of F3/Contactin with developmental control genes belonging to the Notch pathway. (uniba.it)
Neuronal1
- F3/Contactin is differentially expressed in distinct populations of central and peripheral neurons and in some non-neuronal cells. (uniba.it)
Expression1
- Transgenic models allowed to follow F3/Contactin promoter activation in vivo and to modify F3/Contactin gene expression under a heterologous promoter, which resulted in morphological and functional phenotypes. (uniba.it)
Protein12
- Molecular cytogenetic analysis and resequencing of contactin associated protein-like 2 in autism spectrum disorders. (acibadem.edu.tr)
- Contactin-associated protein 1 (Caspr1), also known as Neurexin-4, Paranodin, and NCP1, is an approximately 190 kDa transmembrane protein that is concentrated at paranodal junctions of axons during myelination. (rndsystems.com)
- Using mouse models, Huberman led a team demonstrating that two proteins, Contactin-4 and amyloid precursor protein, act during early development to establish and reinforce the accessory optic system. (nih.gov)
- Likewise, in the absence of amyloid precursor protein, which binds to Contactin-4, normal eye and brain connections did not occur. (nih.gov)
- The gene, CNTNAP2 (contactin-associated protein-like 2) is active in the developing fetus. (nih.gov)
- 1. Contactin 1: An Important and Emerging Oncogenic Protein Promoting Cancer Progression and Metastasis. (nih.gov)
- 12. A complex between contactin-1 and the protein tyrosine phosphatase PTPRZ controls the development of oligodendrocyte precursor cells. (nih.gov)
- From NCBI Gene: The protein encoded by this gene is a member of the immunoglobulin superfamily, and contactin family, which mediate cell surface interactions during nervous system development. (nih.gov)
- Potassium channel associated protein, contactin 2, CNTN2, of 1040 aas and possibly 2 TMSs, at the N- and C-termini. (tcdb.org)
- Although genetic variations in several genes encoding for synaptic adhesion proteins have been found to be associated with autism spectrum disorders, one of the most consistently replicated genes has been CNTNAP2, encoding for contactin-associated protein-like 2 (CASPR2), a multidomain transmembrane protein of the neurexin superfamily. (nih.gov)
- Pre-analytical stability of serum biomarkers for neurological disease: neurofilament-light, glial fibrillary acidic protein and contactin-1. (nih.gov)
- Contactin-associated protein (Caspr) is a major component of the perinodes. (nih.gov)
Cntn11
- Levels of NfL and GFAP were quantified using an HDx analyzer and CNTN1 were quantified using the Human contactin-1 Magnetic Luminex Assay on a Bio-PlexTM 200 system. (nih.gov)
Phoenix Contactin2
- Phoenix Contactin keskeytymättömät teholähteet AC-sovelluksiin tuottavat lähdössä puhtaan sinikäyrän. (phoenixcontact.com)
- Phoenix Contactin uuden CONTACTRON pro -tuotesarjan tuotteet sallivat yksinkertaisen turvallisuusintegraation ja ovat modulaarisesti laajennettavissa. (phoenixcontact.com)
Gene4
- They found that those cells in the accessory optic system express (turn on) the Contactin-4 gene at the time that the system is developing. (nih.gov)
- Using a mouse model with a mutated Contactin-4 gene, they showed that Contactin-4's function is very specific to direction-selective RGCs. (nih.gov)
- 8. The gene encoding the mouse contactin-1 axonal glycoprotein is regulated by the collier/Olf1/EBF family early B-Cell factor 2 transcription factor. (nih.gov)
- This gene encodes a member of the contactin family of proteins, part of the immunoglobulin superfamily of cell adhesion molecules. (nih.gov)
Proteins1
- Recently, studies identified a subgroup of patients with CIDP who were positive for IgG4 autoantibodies against paranodal proteins, such as neurofascin-155 and contactin-1, who respond poorly to first-line therapies for typical CIDP, including intravenous immunoglobulin therapy. (researchprotocols.org)
Molecule1
- We first demonstrate that the Ig superfamily molecule contactin is associated in oligodendrocytes with integrins, extracellular matrix receptors that regulate target-dependent survival by amplification of growth factor signaling. (ed.ac.uk)
Knockdown2
- This amplification is inhibited by small interfering RNA-mediated knockdown of contactin in oligodendrocytes. (ed.ac.uk)
- 13. Significances of contactin-1 expression in human gastric cancer and knockdown of contactin-1 expression inhibits invasion and metastasis of MKN45 gastric cancer cells. (nih.gov)
Inhibits1
- Caspr1 interacts with Contactins and Nogo-A at the paranodal junction and inhibits the binding of Contactin to glial cell Neurofascin. (rndsystems.com)
Axonal1
- We conclude, therefore, that a novel integrin/contactin complex coordinates signals from extracellular matrix and the axonal surface to regulate both oligodendrocyte survival and myelination by controlling Fyn activity. (ed.ac.uk)
Synaptic1
- 20. F3/Contactin promotes hippocampal neurogenesis, synaptic plasticity, and memory in adult mice. (nih.gov)
Descriptor1
- Contactins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (ucdenver.edu)
Cell1
- 6. Contactin 1 as a potential biomarker promotes cell proliferation and invasion in thyroid cancer. (nih.gov)
Mouse1
- 10. A spontaneous mutation in contactin 1 in the mouse. (nih.gov)
Website1
- This graph shows the total number of publications written about "Contactins" by people in this website by year, and whether "Contactins" was a major or minor topic of these publications. (ucdenver.edu)
Complex1
- An integrin-contactin complex regulates CNS myelination by differential Fyn phosphorylation. (ed.ac.uk)
Role1
- 7. The Role of Contactin 1 in Cancers: What We Know So Far. (nih.gov)
Specific1
- Huberman and his team labeled specific target groups of neurons in the accessory optic system and then stained sections of the tissue with an antibody specific for Contactin-4. (nih.gov)
Brain1
- In those mice with mutated Contactin-4, the direction-selective RGCs in the eye didn't talk to the brain correctly. (nih.gov)
Cells1
- 5. Overexpression of Contactin 1 promotes growth, migration and invasion in Hs578T breast cancer cells. (nih.gov)
Publications1
- Below are the most recent publications written about "Contactins" by people in Profiles. (ucdenver.edu)