HÜCRE ADEZYON MOLEKÜLÜ: NEKTİN

Öz

Adezyon molekülleri, birbirleriyle veya ekstraselüler gösteren, hücre-hücre ve hücre-ekstraselüler matriks bağlantısını sağlayan protein molekülleridir. Hücre adezyon molekülleri hücre aktivasyonu, göçü, büyümesi, farklılaşması ve ölümü gibi bir çok olayın düzenlenmesinde rol oynar. Nektin’ler Ca2+bağımsız immunoglobulin-benzeri hücre adezyon molekülüdür, nektin-1, nektin-2, nektin-3, ve nektin4 olmak üzere dört üyeden oluşan bir ailedir. Nektin’ler kaderinler’den bağımsız ya da kaderin işbirliği ile hareket ederek çeşitli hücre-hücre bağlantılarının oluşumuna katkıda bulunurlar ve homofilik ve heterofilik trans-etkileşimleri ile hücrehücre adezyonuna sebep olurlar. Nektin-1, nektin-2 ve nektin-3 fibroblastlar, epitelyal hücreler ve nöronları içeren çeşitli hücre tiplerinde eksprese edilmektedir. Nektin-4 ise başlıca plasentada eksprese edilmektedir. Bu derlemede nektin molekülünün morfolojik yapısı ve fonksiyonu anlatılmaktadır

Anahtar Kelimeler

• Bağlantı kompleksleri, hücre adezyon molekülleri, nektin

Cell Adhesion Molecule: Nectin

Öz

molecules, which interact with each other or the extracellular fluid molecules, cell-cell and cellextracellular matrix protein molecules that provide their connection. Cell adhesion molecules play a role in the regulation of many events such as cell activation, migration, proliferation, differentiation and immunoglobulin-like cell adhesion molecules which comprise a family of four members, nectin-1, nectin-2, nectin-3, and nectin-4. Nectins contribute to the formation of a variety of cell–cell junctions, acting cooperatively with or independently of cadherins and these cause cell-cell adhesionhomophilically and heterophilically trans-interact. Nectin-1, nectin-2 and nectin-3 are expressed in a variety of cells, including fibroblasts, epithelial cells and neurons. Human nectin-4 is expressed mainly in the placenta. In this review, morphologic structure and function of nectin molecule have been discussed

Anahtar Kelimeler

• Junctional complex, cell adhesion molecules, nectin

Kaynakça

1. Sakisaka T, Ikeda W, Ogita H, et al. The roles of nectins in cell adhesions: cooperation with other cell adhesion molecules and growth factor receptors. Current Opinion in Cell Biology 2007; 19: 593–602.
2. Mandai K, Nakanishi H, Satoh A, et al. Ponsin/SH3P12: An l-Afadin– and Vinculin- binding Protein Localized at Cell–Cell and Cell–Matrix Adherens Junctions. The Journal of Cell Biology 1999; 144: 1001-1017.
3. Miyoshi J, Takai Y. Nectin and Nectin-Like Molecules: Biology and Pathology. Am J Nephrol 2007; 27: 590–604.
4. Honda T, Shimizu K, Kawakatsu T, et al. Antagonistic and agonistic effects of an extracellular fragment of nectin on formation of E-cadherin-based cell-cell adhesion. Genes to Cells 2003; 8: 51–63.
5. Satoh-Horikawa K, Nakanishi H, Takahashi K, et al. Nectin-3, a New Member of Immunoglobulin-like Cell Adhesion Molecules That Shows Homophilic and Heterophilic Cell -Cell Adhesion Activities. The Journal of Biological Chemistry 2000; 275: 10291– 10299.
6. Takahashi K, Nakanishi H, Miyahara M, et al. Nectin/PRR: An Immunoglobulin-like Cell Adhesion Molecule Recruited to Cadherin- based Adherens Junctions through Interaction with Afadin, a PDZ Domain–containing Pro- tein. The Journal of Cell Biology 1999; 145: 539-549.
7. Reymond N, Fabre S, Lecocq E, et al. Nectin4/ PRR4, a New Afadin-associated Member of the Nectin Family That Trans-interacts with Nectin1/PRR1 through V Domain Interaction. The Journal of Bıologıcal Chemistry 2001; 276: 43205–43215.
8. Shimizu K, Takai Y. Roles of the Intercellular Adhesion Molecule Nectin in Intracellular Signaling. J Biochem 2003; 134: 631–636.

9. Mandai K, Nakanishi H, Satoh A, et al. Afadin: A Novel Actin Filament–binding Pro- tein with One PDZ Domain Localized at Cadherin-based Junction. The Journal of Cell Biology 1997; 139: 517–528. Adherens
10. Gumbiner BM. Cell Adhesion: The Molecular Basis Morphogenesis Cell 1996; 84: 345–357. Architecture and
11. Fukuhara A, Irie K, Nakanishi H, et al. Involvement of nectin in the localization of junctional adhesion molecule at tight junctions. Oncogene 2002; 21:7642-7655.
12. Mizoguchi A, Nakanishi H, Kimura K, et al. Nectin: an adhesion molecule involved in formation of synapses. The Journal of Cell Biology 2002; 156: 555–565.
13. Inagaki M, Irie K, Ishizaki H, et al. Role of cell adhesion molecule nectin-3 in spermatid Development. Genes to Cells 2006; 11: 1125– 1132.
14. Cheng CY, Mruk DD. Cell Junction Dynamics in the Testis: Sertoli-Germ Cell Interactions and Male Contraceptive Development. Physiol Rev 2002; 82: 825–874.
15. Ozaki-Kuroda K, Nakanishi H, Ohta H, et al. Nectin Couples Cell-Cell Adhesion and the Actin Scaffold at Heterotypic Testicular Junctions. Current Biology 2002; 12: 1145– 1150.
16. Bouchard MJ, Dong Y, Brıan M, et al. Defects in Nuclear and Cytoskeletal Morphology and Mitochondrial Localization in Spermatozoa of Mice Lacking Nectin-2, a Component of Cell- Cell Adherens Junctions. Molecular and Cellular Bıology 2000; 20: 2865–2873.
17. Mueller S, Rosenquist TA, Takai Y, et al. Loss of Nectin-2 at Sertoli-Spermatid Junctions Leads to Male Infertility and Correlates with Severe Spermatozoan Head and Midpiece Malformation, Impaired Binding to the Zona Pellucida, and Oocyte Penetration. Bıology of Reproductıon 2003; 69: 1330–1340.
18. Lopez M, Eberlé F, Mattei M G, et al. Complementary DNA characterization and chromosomal localization of a human gene related to the poliovirus receptor-encoding gene. Gene 1995; 155: 261-265.
19. Morrison ME, Racanıello VR. Molecular Cloning and Expression of a Murine Homolog of the Human Poliovirus Receptor Gene. Journal of Virology 1992; 66: 2807-2813.
20. Cocchi F, Lopez M, Menotti L et al. The V domain of herpesvirus Ig-like receptor (HIgR) contains a major functional region in herpes simplex virus-1 entry into cells and interacts physically with the viral glycoprotein D. Proc Natl Acad Sci 1998; 95: 15700-15705.
21. Cocchi F, Menotti L, Dubreuil P, et al. Cell-to -cell spread of wild-type herpes simplex virus type 1, but not of syncytial strains, is mediated by the immunoglobulin-like receptors that mediate virion entry, nectin1 (PRR1/HveC/ HIgR) and nectin2 (PRR2/HveB). J Virol 2000; 74: 3909-3917.