Disease relevance of CNTN1

• Contactin/F11 mRNA is detected in bipolar cells or their precursors from E8-9, and later in horizontal and ganglion neurons [1].

High impact information on CNTN1

• Using an in vivo approach, we demonstrate an involvement of the two immunoglobulin superfamily cell adhesion molecules axonin-1/TAG-1 and F11/F3/contactin in subpopulation-specific sensory axon guidance [2].
• The possible identity of F11 with the chick neural glycoprotein contactin is discussed [3].
• Neural cell recognition molecule F11: homology with fibronectin type III and immunoglobulin type C domains [3].
• The primary amino acid sequence of contactin, a neuronal cell surface glycoprotein of 130 kD that is isolated in association with components of the cytoskeleton (Ranscht, B., D. J. Moss, and C. Thomas. 1984. J. Cell Biol. 99:1803-1813), was deduced from the nucleotide sequence of cDNA clones and is reported here [4].
• Unlike contactin, it is not restricted to nervous tissue and is quite abundant in gizzard, where there are two antigenically related proteins of 100K and 90K (K = 10(3) Mr) [5].

Biological context of CNTN1

• Antibody-mediated cross-linking of contactin/F11 on embryonic chick neuronal cells leads to an increase of the Fyn-activity coprecipitated with contactin/F11, and elevates phosphorylation of an additional 75/80 K component within the contactin/F11-immune-complex [6].
• To examine the structure and tissue distribution of Xenopus contactin, a cDNA clone was isolated based on the amino acid sequences conserved among chicken and mammalian contactin proteins [7].

Anatomical context of CNTN1

• The neural cell recognition molecule F11 is expressed on Müller cells and Schwann cells in vitro [8].
• The onset of both tenascin-C and contactin/F11 expression coincides with the appearance of ganglion cell dendrides and neurites from bipolar and amacrine cells in the inner layer (IPL) at E8, and the extension of bipolar and horizontal cell processes in the outer plexiform layer (OPL) at E9 [1].
• The neural immunoglobulin-like cell adhesion molecule contactin/F11 and the extracellular matrix glycoprotein tenascin-C are prominent molecules in the developing nervous system which interact in in vitro assays (Zisch et al., J. Cell Biol. 119, 203-213) [1].
• On brain tissue sections, strong contactin immunoreactivities were detected on nerve fibers of a subset of cerebral and cerebellar neurons [7].

Associations of CNTN1 with chemical compounds

• Analysis of detergent-resistant immune-complexes reveals that the glypiated neuronal cell adhesion molecule contactin/F11 specifically complexes with the cytoplasmic, nonreceptor type src-family tyrosine kinase Fyn [6].
• Purification, crystallization and preliminary crystallographic studies of a two fibronectin type-III domain segment from chicken tenascin encompassing the heparin- and contactin-binding regions [9].

Physical interactions of CNTN1

• The glypiated neuronal cell adhesion molecule contactin/F11 complexes with src-family protein tyrosine kinase Fyn [6].

Other interactions of CNTN1

• The contactin-related protein FAR-2 defines purkinje cell clusters and labels subpopulations of climbing fibers in the developing cerebellum [10].

Analytical, diagnostic and therapeutic context of CNTN1

• In situ hybridization reveals that tenascin-C and contactin/F11 mRNAs are synthesized by different neuronal types [1].
• In a first step, we have examined the distribution of tenascin isoforms and contactin/F11 during retinal development by means of immunohistochemistry and in situ hybridization with tenascin isoform-specific probes [11].

References