Adhesion properties and retinofugal expression of chicken protocadherin-19.
Protocadherin-19 has been implicated in some neurological diseases, but even the basic properties of this protocadherin have not yet been characterized well. Hence, various basic properties of chicken protocadherin-19 were examined to elucidate its biological role. The protocadherin-19 expressed in L cells was localized at the intercellular contact sites and showed Ca(2+)-dependent homophilic cell aggregation activity that was relatively weak but showed stringent specificity. The results of a pull-down assay using fusion proteins of the cytoplasmic domain and glutathione S-transferase yielded specifically bound proteins. In the bound fractions, liquid chromatography-mass spectrometry identified Nck-associated protein 1 and cytoplasmic FMP1 interacting protein 2, which have been reported to bind to glutathione S-transferase fused with the cytoplasmic domain of OL-protocadherin, suggesting that these proteins generally have affinity for delta protocadherins. Protocadherin-19 was mainly expressed in the central nervous system. In the chicken retina, protocadherin-19 was expressed as early as embryonic day 5 and was localized in the ganglion cell layer, inner plexiform layer, and optic nerve layer. Chicken protocadherin-19 was co-localized with syntaxin 1 in inner plexiform layer and was also expressed in the optic nerve and in specific layers of optic tectum. These results suggest that protocadherin-19 plays a role as an adhesion protein in optic nerve fiber bundling, optic nerve targeting, and/or synapse formation.
Tai
Kiyoto
K
Department of Bioscience, School of Science and Technology, Kwansei Gakuin University, Nanobiology Center, 2-1 Gakuen, Sanda-shi, Hyogo-ken 669-1337, Japan.
Kubota
Masaki
M
Shiono
Kohei
K
Tokutsu
Hitoshi
H
Suzuki
Shintaro T
ST
D000595:Amino Acid Sequence; D000818:Animals; D000831:Animals, Newborn; D015820:Cadherins / Q000235:genetics* / Q000378:metabolism*; D002448:Cell Adhesion / Q000235:genetics / Q000502:physiology*; D002449:Cell Aggregation / Q000235:genetics; D002460:Cell Line; D002642:Chick Embryo; D002853:Chromatography, Liquid / Q000379:methods; D003001:Cloning, Molecular / Q000379:methods; D003593:Cytoplasm / Q000378:metabolism; D018507:Gene Expression Regulation, Developmental / Q000235:genetics / Q000502:physiology; D005982:Glutathione Transferase / Q000378:metabolism; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods; D051379:Mice; D008969:Molecular Sequence Data; D009154:Mutation / Q000502:physiology; D009419:Nerve Tissue Proteins / Q000378:metabolism; D009900:Optic Nerve / Q000196:embryology / Q000254:growth & development / Q000378:metabolism*; D012160:Retina / Q000378:metabolism*; D013477:Superior Colliculi / Q000196:embryology / Q000254:growth & development / Q000378:metabolism*; D014162:Transfection / Q000379:methods; D014795:Visual Pathways / Q000378:metabolism
D015820:Cadherins; D009419:Nerve Tissue Proteins; D005982:Glutathione Transferase