A family of immunoglobulin-related cell adhesion molecules that are involved in NERVOUS SYSTEM patterning.
A group of inherited and sporadic disorders which share progressive ataxia in combination with atrophy of the CEREBELLUM; PONS; and inferior olivary nuclei. Additional clinical features may include MUSCLE RIGIDITY; NYSTAGMUS, PATHOLOGIC; RETINAL DEGENERATION; MUSCLE SPASTICITY; DEMENTIA; URINARY INCONTINENCE; and OPHTHALMOPLEGIA. The familial form has an earlier onset (second decade) and may feature spinal cord atrophy. The sporadic form tends to present in the fifth or sixth decade, and is considered a clinical subtype of MULTIPLE SYSTEM ATROPHY. (From Adams et al., Principles of Neurology, 6th ed, p1085)
Incoordination of voluntary movements that occur as a manifestation of CEREBELLAR DISEASES. Characteristic features include a tendency for limb movements to overshoot or undershoot a target (dysmetria), a tremor that occurs during attempted movements (intention TREMOR), impaired force and rhythm of diadochokinesis (rapidly alternating movements), and GAIT ATAXIA. (From Adams et al., Principles of Neurology, 6th ed, p90)
A heterogenous group of degenerative syndromes marked by progressive cerebellar dysfunction either in isolation or combined with other neurologic manifestations. Sporadic and inherited subtypes occur. Inheritance patterns include autosomal dominant, autosomal recessive, and X-linked.
A sporadic neurodegenerative disease with onset in middle-age characterized clinically by Parkinsonian features (e.g., MUSCLE RIGIDITY; HYPOKINESIA; stooped posture) and HYPOTENSION. This condition is considered a clinical variant of MULTIPLE SYSTEM ATROPHY. Pathologic features include a prominent loss of neurons in the zona compacta of the SUBSTANTIA NIGRA and PUTAMEN. (From Adams et al., Principles of Neurology, 6th ed, p1075-6)
Disorders of speech articulation caused by imperfect coordination of pharynx, larynx, tongue, or face muscles. This may result from CRANIAL NERVE DISEASES; NEUROMUSCULAR DISEASES; CEREBELLAR DISEASES; BASAL GANGLIA DISEASES; BRAIN STEM diseases; or diseases of the corticobulbar tracts (see PYRAMIDAL TRACTS). The cortical language centers are intact in this condition. (From Adams et al., Principles of Neurology, 6th ed, p489)
Diseases of the BASAL GANGLIA including the PUTAMEN; GLOBUS PALLIDUS; claustrum; AMYGDALA; and CAUDATE NUCLEUS. DYSKINESIAS (most notably involuntary movements and alterations of the rate of movement) represent the primary clinical manifestations of these disorders. Common etiologies include CEREBROVASCULAR DISORDERS; NEURODEGENERATIVE DISEASES; and CRANIOCEREBRAL TRAUMA.
A syndrome complex composed of three conditions which represent clinical variants of the same disease process: STRIATONIGRAL DEGENERATION; SHY-DRAGER SYNDROME; and the sporadic form of OLIVOPONTOCEREBELLAR ATROPHIES. Clinical features include autonomic, cerebellar, and basal ganglia dysfunction. Pathologic examination reveals atrophy of the basal ganglia, cerebellum, pons, and medulla, with prominent loss of autonomic neurons in the brain stem and spinal cord. (From Adams et al., Principles of Neurology, 6th ed, p1076; Baillieres Clin Neurol 1997 Apr;6(1):187-204; Med Clin North Am 1999 Mar;83(2):381-92)

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)

Contactins are a family of glycosylphosphatidylinositol (GPI)-anchored neuronal cell adhesion molecules that play important roles in the nervous system. They are involved in the formation and maintenance of neural connections, including axon guidance, fasciculation, and synaptogenesis. Contactins have immunoglobulin-like domains and fibronectin type III repeats, which mediate their homophilic or heterophilic interactions with other molecules on the cell surface. There are six known members of the contactin family: contactin-1 (also known as F3), contactin-2 (TAG-1), contactin-3 (BIG-1), contactin-4 (BIG-2), contactin-5, and contactin-6. Mutations in some contactin genes have been associated with neurological disorders such as X-linked mental retardation and epilepsy.

Olivopontocerebellar atrophies (OPCA) are a group of rare, progressive neurodegenerative disorders that primarily affect the cerebellum, olive (inferior olivary nucleus), and pons in the brainstem. The condition is characterized by degeneration and atrophy of these specific areas, leading to various neurological symptoms.

The term "olivopontocerebellar atrophies" encompasses several subtypes, including:

1. Hereditary spastic paraplegia with cerebellar ataxia (SPG/ATA) - Autosomal dominant or recessive inheritance pattern.
2. Hereditary dentatorubral-pallidoluysian atrophy (DRPLA) - Autosomal dominant inheritance pattern.
3. Idiopathic OPCA - No known genetic cause, possibly related to environmental factors or spontaneous mutations.

Symptoms of olivopontocerebellar atrophies may include:

* Progressive cerebellar ataxia (gait and limb incoordination)
* Dysarthria (slurred speech)
* Oculomotor abnormalities (nystagmus, gaze palsy)
* Spasticity (stiffness and rigidity of muscles)
* Dysphagia (difficulty swallowing)
* Tremors or dystonia (involuntary muscle contractions)

Diagnosis typically involves a combination of clinical examination, neuroimaging studies (MRI), genetic testing, and exclusion of other possible causes. Currently, there is no cure for olivopontocerebellar atrophies, but supportive care can help manage symptoms and improve quality of life.

Cerebellar ataxia is a type of ataxia, which refers to a group of disorders that cause difficulties with coordination and movement. Cerebellar ataxia specifically involves the cerebellum, which is the part of the brain responsible for maintaining balance, coordinating muscle movements, and regulating speech and eye movements.

The symptoms of cerebellar ataxia may include:

* Unsteady gait or difficulty walking
* Poor coordination of limb movements
* Tremors or shakiness, especially in the hands
* Slurred or irregular speech
* Abnormal eye movements, such as nystagmus (rapid, involuntary movement of the eyes)
* Difficulty with fine motor tasks, such as writing or buttoning a shirt

Cerebellar ataxia can be caused by a variety of underlying conditions, including:

* Genetic disorders, such as spinocerebellar ataxia or Friedreich's ataxia
* Brain injury or trauma
* Stroke or brain hemorrhage
* Infections, such as meningitis or encephalitis
* Exposure to toxins, such as alcohol or certain medications
* Tumors or other growths in the brain

Treatment for cerebellar ataxia depends on the underlying cause. In some cases, there may be no cure, and treatment is focused on managing symptoms and improving quality of life. Physical therapy, occupational therapy, and speech therapy can help improve coordination, balance, and communication skills. Medications may also be used to treat specific symptoms, such as tremors or muscle spasticity. In some cases, surgery may be recommended to remove tumors or repair damage to the brain.

Spinocerebellar degenerations (SCDs) are a group of genetic disorders that primarily affect the cerebellum, the part of the brain responsible for coordinating muscle movements, and the spinal cord. These conditions are characterized by progressive degeneration or loss of nerve cells in the cerebellum and/or spinal cord, leading to various neurological symptoms.

SCDs are often inherited in an autosomal dominant manner, meaning that only one copy of the altered gene from either parent is enough to cause the disorder. The most common type of SCD is spinocerebellar ataxia (SCA), which includes several subtypes (SCA1, SCA2, SCA3, etc.) differentiated by their genetic causes and specific clinical features.

Symptoms of spinocerebellar degenerations may include:

1. Progressive ataxia (loss of coordination and balance)
2. Dysarthria (speech difficulty)
3. Nystagmus (involuntary eye movements)
4. Oculomotor abnormalities (problems with eye movement control)
5. Tremors or other involuntary muscle movements
6. Muscle weakness and spasticity
7. Sensory disturbances, such as numbness or tingling sensations
8. Dysphagia (difficulty swallowing)
9. Cognitive impairment in some cases

The age of onset, severity, and progression of symptoms can vary significantly among different SCD subtypes and individuals. Currently, there is no cure for spinocerebellar degenerations, but various supportive treatments and therapies can help manage symptoms and improve quality of life.

Striatonigral degeneration (SND) is a type of neurodegenerative disorder that affects the basal ganglia, specifically the striatum and the substantia nigra. It is also known as "striatonigral degeneration with olivopontocerebellar atrophy" or "multiple system atrophy-parkinsonian type (MSA-P)".

SND is characterized by the progressive loss of nerve cells in the striatum, which receives input from the cerebral cortex and sends output to the substantia nigra. This results in a decrease in the neurotransmitter dopamine, leading to symptoms similar to those seen in Parkinson's disease (PD), such as stiffness, slowness of movement, rigidity, and tremors.

However, unlike PD, SND is also associated with degeneration of the olivopontocerebellar system, which can lead to additional symptoms such as ataxia, dysarthria, and oculomotor abnormalities. The exact cause of striatonigral degeneration is unknown, but it is believed to involve a combination of genetic and environmental factors. Currently, there is no cure for the condition, and treatment is focused on managing the symptoms.

Dysarthria is a motor speech disorder that results from damage to the nervous system, particularly the brainstem or cerebellum. It affects the muscles used for speaking, causing slurred, slow, or difficult speech. The specific symptoms can vary depending on the underlying cause and the extent of nerve damage. Treatment typically involves speech therapy to improve communication abilities.

Basal ganglia diseases are a group of neurological disorders that affect the function of the basal ganglia, which are clusters of nerve cells located deep within the brain. The basal ganglia play a crucial role in controlling movement and coordination. When they are damaged or degenerate, it can result in various motor symptoms such as tremors, rigidity, bradykinesia (slowness of movement), and difficulty with balance and walking.

Some examples of basal ganglia diseases include:

1. Parkinson's disease - a progressive disorder that affects movement due to the death of dopamine-producing cells in the basal ganglia.
2. Huntington's disease - an inherited neurodegenerative disorder that causes uncontrolled movements, emotional problems, and cognitive decline.
3. Dystonia - a movement disorder characterized by sustained or intermittent muscle contractions that cause twisting and repetitive movements or abnormal postures.
4. Wilson's disease - a rare genetic disorder that causes excessive copper accumulation in the liver and brain, leading to neurological and psychiatric symptoms.
5. Progressive supranuclear palsy (PSP) - a rare brain disorder that affects movement, gait, and balance, as well as speech and swallowing.
6. Corticobasal degeneration (CBD) - a rare neurological disorder characterized by progressive loss of nerve cells in the cerebral cortex and basal ganglia, leading to stiffness, rigidity, and difficulty with movement and coordination.

Treatment for basal ganglia diseases varies depending on the specific diagnosis and symptoms but may include medication, surgery, physical therapy, or a combination of these approaches.

Multiple System Atrophy (MSA) is a rare, progressive neurodegenerative disorder that affects multiple systems in the body. It is characterized by a combination of symptoms including Parkinsonism (such as stiffness, slowness of movement, and tremors), cerebellar ataxia (lack of muscle coordination), autonomic dysfunction (problems with the autonomic nervous system which controls involuntary actions like heart rate, blood pressure, sweating, and digestion), and pyramidal signs (abnormalities in the corticospinal tracts that control voluntary movements).

The disorder is caused by the degeneration of nerve cells in various parts of the brain and spinal cord, leading to a loss of function in these areas. The exact cause of MSA is unknown, but it is thought to involve a combination of genetic and environmental factors. There is currently no cure for MSA, and treatment is focused on managing symptoms and improving quality of life.

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 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 ...
... , 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, 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, Articles needing ...
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 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. ...
CONTACT - in-house magazine of OTC. Masterton, R and Prances M; Invisible Bridges, Australia and International ...
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 ...
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 ...
... 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 ...
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- ...
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 ...
... members also bind "heterophilically" to members of the contactin or CNTN1 family. L1 family members bind to many ...
"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 ...
January 2008). "Molecular cytogenetic analysis and resequencing of contactin associated protein-like 2 in autism spectrum ...
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), ...
This extracellular region is similar to the cell adhesion molecule contactin and other cell adhesion molecules. It is believed ...
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 ...
Shah BS, Rush AM, Liu S, Tyrrell L, Black JA, Dib-Hajj SD, Waxman SG (August 2004). "Contactin associates with sodium channel ...
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. ...
"Mutations in contactin-1, a neural adhesion and neuromuscular junction protein, cause a familial form of lethal congenital ...
1997). "Induction of neurite outgrowth through contactin and Nr-CAM by extracellular regions of glial receptor tyrosine ...
Schuko is an abbreviation for the German word Schutzkontakt, which means "Protective contact" - in this case "protective" ...
... contactin 1 (CNTN1), contactin associated protein 1 (CASPR1) and gliomedin. All of them nodal and paranodal proteins. Several ...
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 ...
Kamei Y, Takeda Y, Teramoto K, Tsutsumi O, Taketani Y, Watanabe K (Oct 2000). "Human NB-2 of the contactin subgroup molecules: ...
... beta1 subunit-mediated modulation of Nav1.2 currents and cell surface density is dependent on interactions with contactin and ...
... beta1 subunit-mediated modulation of Nav1.2 currents and cell surface density is dependent on interactions with contactin and ...
... contactin 1 (CNTN1), contactin associated protein 1 (CASPR1) and gliomedin. All of them nodal and paranodal proteins. Anti-TNF ...
Kamei Y, Takeda Y, Teramoto K, Tsutsumi O, Taketani Y, Watanabe K (Oct 2000). "Human NB-2 of the contactin subgroup molecules: ...
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 ...
Browse more than 400 smartphones freeware Keep Contactin downloads e-books, games, themes, video, ringtones, sport, utilities ... the Keep Contactin free for Windows Mobile Smartphone .mobi Mobile friendly download. Download Keep Contactin direct on your ... Keep Contactin. � Summary: Keep Contactin is a simple address book application. Requirements:. Windows Mobile Smartphone. � ... Keep Contactin Description. Keep Contactin is a simple address book application. It allows you to manage your contacts in the ...
Contactin-1 links autoimmune neuropathy and membranous glomerulonephritis. *Mark. Fehmi, Janev ; Davies, Alexander J. ; ... Previous case reports have suggested an association between patients with anti-contactin-1 (CNTN1)-mediated neuropathies and ... Previous case reports have suggested an association between patients with anti-contactin-1 (CNTN1)-mediated neuropathies and ... Previous case reports have suggested an association between patients with anti-contactin-1 (CNTN1)-mediated neuropathies and ...
This is not just your average massage. I have tried a variety of different massages and styles of treatment for my physical ailments in the past although Lakech wellbeing takes it to another level ! With the variety of massages they offer and the years of healing experience they have it has once and for all really put me on the road to recovery 😀 I totally recommend you try them out ...
Please enable JavaScript in your browser to complete this form ...
We are based out of Valencia, CA 91355 Email:[email protected] Customer satisfaction is very important to me and I take it very seriously. Please visit my FAQs or Shipping Policies if you have a question about the status of your order. If your question still isnt answered, please contact me using this handy
In Style Executive is a premiere chauffeur-driven luxury car and van transport service based in Wellington New Zealand. Our fleet of luxury vehicles, experienced chauffeurs and our commitment to providing ultimate customer satisfaction is second to none. ...
For feedback on the music, the website, or anything #inloveandwarband youd like, please use the form below.. ...
This field is for validation purposes and should be left unchanged ...
Lets stay get to know each other better! Check out my Instagram stories to know what Im up to! ...
Edit this text and tell your site visitors who you are. To edit, simply click directly on the text and add your own words. Use this text to go into more detail about your company. Make sure to include information about how your company came to be. ...
Contact Firstlight Home Care Franklin for affordable Senior Home Care and Elderly Care Services.
Questions? Comments? Encouragement? Contact us here! Shoot us a note, email or call, and well be happy to serve you however we can.
AFM Force Spectroscopy and Steered Molecular Dynamics Simulation of Protein Contactin 4. J. Strzelecki; K. Mikulska; M. Lekka; ... Nanomechanics of multidomain neuronal cell adhesion protein contactin revealed by single molecule AFM and SMD. K. Mikulska- ...
Contactin-4. MRI-proven cerebellar atrophy without brainstem involvement; onset at 20-66 years; pure cerebellar ataxia, some ... Contactin-4. MRI-proven cerebellar atrophy without brainstem involvement; onset at 20-66 years; pure cerebellar ataxia, some ...
For immunofluorescence staining, we used rabbit anti-Ankyrin G (AnkG, InsightBio, Wembley, UK) or rabbit anti-Contactin ... Node of Ranvier: ankG, ankyrin G; Caspr, contactin associated protein; MBP, myelin basic protein; MOG, myelin oligodendrocyte ... and contactin associated protein (Caspr) (Figure 5B). MBP adheres adjacent cytoplasmic faces of myelin together, neurofilament ...
contactin 2. involved_in. IEA. Ensembl. GO_REF:0000107. NCBI chr38:1,570,598...1,600,524 Ensembl chr38:1,576,898...1,596,621 ...
Phoenix Contactin modulaariset suorakulmaliittimet YouTube Modulaariset suorakulmaliittimet tuovat joustavuutta vaikeissa ...
The crystal structure of the ligand binding module of axonin-1/TAG-1 suggests a zipper mechanism for neural cell adhesion ...
Anti-contactin associated protein-like 2 (CASPR-2); Anti-gamma aminobutyric acid (GABA); Anti-glutamic acid decarboxylase 65 ( ...
Take a look at Gripples building suspension system design and installation service to find out how we can help simplify your next project.
Footballs future is hazy, but footballs present can be made safer, right now, with a simple change in approach. Thats the school of thought one man brought…
Cross-Talk between F3/Contactin and Notch at Axoglial Interface: A Role in Oligodendrocyte Development Dev Neurosci (March,2006 ...
Autoantibodies against contactin-associated protein 2 (Caspr2) not only induce limbic autoimmune encephalitis but are also ...
Hello, thank you for contactin… (Click here to read the rest of the answer) ...
Triple-lip contactin; D:7.7550 in; expansion type:Non-Expansion Bearin; ...
identified common variants that contribute to autism in contactin-associated protein-like 2 (CNTNAP2), a member of the neurexin ...
Solution structures of the fn3 domain of human contactin 1. 2ee3. Solution structures of the fn3 domain of human collagen alpha ... Crystal structure of an internal FN3 domain from human Contactin-5 [PSI-NYSGRC-005804]. ...
  • Antibodies against other protein in the voltage-gated potassium channel/LGI1 complex, such as Caspr2 (contactin- associated protein 2) and contactin-2, have been shown to also cause Autoimmune LE. (scirp.org)
  • Laboratory testing should include tests for antibodies to contactin-associated protein-like 2 (Caspr2), the striational voltage-gated calcium channel, gliadin, glutamic acid decarboxylase (GAD), muscle acetylcholine receptor (AChR), and the voltage-gated potassium channel. (msdmanuals.com)
  • Previous case reports have suggested an association between patients with anti-contactin-1 (CNTN1)-mediated neuropathies and MGN. (lu.se)
  • We identify Contactin-1 (Cntn1) as an AIS cell surface protein. (bvsalud.org)
  • The gene, CNTNAP2 (contactin-associated protein-like 2) is active in the developing fetus. (nih.gov)
  • 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)
  • 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)
  • 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)
  • 16. Contactin-1/F3 Regulates Neuronal Migration and Morphogenesis Through Modulating RhoA Activity. (nih.gov)
  • Contactin-associated protein-2 antibodies in non-paraneoplastic cerebellar ataxia. (ox.ac.uk)
  • One strong-binding serum was selected for immunoprecipitation and mass spectrometry, which resulted in the identification of contactin-associated protein 2 (CASPR2) as a major antigen. (ox.ac.uk)
  • 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)
  • 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)
  • Leucine-Rich Glioma-Inactivated 1 versus Contactin-Associated Protein-like 2 Antibody Neuropathic Pain: Clinical and Biological Comparisons. (ox.ac.uk)
  • Description: A sandwich quantitative ELISA assay kit for detection of Mouse Contactin 1 (CNTN1) in samples from tissue homogenates, cell lysates or other biological fluids. (glideruniversity.org)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Contactin 1 (CNTN1) in tissue homogenates, cell lysates and other biological fluids. (glideruniversity.org)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Mouse Contactin 1 (CNTN1) in samples from tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (glideruniversity.org)
  • 10. A spontaneous mutation in contactin 1 in the mouse. (nih.gov)
  • In those mice with mutated Contactin-4, the direction-selective RGCs in the eye didn't talk to the brain correctly. (nih.gov)
  • 6. Contactin 1 as a potential biomarker promotes cell proliferation and invasion in thyroid cancer. (nih.gov)