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HÜCRE ADEZYON MOLEKÜLÜ: NEKTİN

Year 2012, Volume: 21 Issue: 3, 205 - 211, 01.12.2012

Abstract

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

References

  • 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.
  • 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.
  • Miyoshi J, Takai Y. Nectin and Nectin-Like Molecules: Biology and Pathology. Am J Nephrol 2007; 27: 590–604.
  • 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.
  • 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.
  • 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.
  • 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.
  • Shimizu K, Takai Y. Roles of the Intercellular Adhesion Molecule Nectin in Intracellular Signaling. J Biochem 2003; 134: 631–636.
  • 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
  • Gumbiner BM. Cell Adhesion: The Molecular Basis Morphogenesis Cell 1996; 84: 345–357. Architecture and
  • 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.
  • 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.
  • 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.
  • Cheng CY, Mruk DD. Cell Junction Dynamics in the Testis: Sertoli-Germ Cell Interactions and Male Contraceptive Development. Physiol Rev 2002; 82: 825–874.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.

Cell Adhesion Molecule: Nectin

Year 2012, Volume: 21 Issue: 3, 205 - 211, 01.12.2012

Abstract

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

References

  • 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.
  • 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.
  • Miyoshi J, Takai Y. Nectin and Nectin-Like Molecules: Biology and Pathology. Am J Nephrol 2007; 27: 590–604.
  • 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.
  • 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.
  • 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.
  • 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.
  • Shimizu K, Takai Y. Roles of the Intercellular Adhesion Molecule Nectin in Intracellular Signaling. J Biochem 2003; 134: 631–636.
  • 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
  • Gumbiner BM. Cell Adhesion: The Molecular Basis Morphogenesis Cell 1996; 84: 345–357. Architecture and
  • 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.
  • 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.
  • 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.
  • Cheng CY, Mruk DD. Cell Junction Dynamics in the Testis: Sertoli-Germ Cell Interactions and Male Contraceptive Development. Physiol Rev 2002; 82: 825–874.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
There are 21 citations in total.

Details

Other ID JA47JH69NK
Journal Section Research Article
Authors

Derya Akkuş This is me

Mehmet Fatih Sönmez This is me

Publication Date December 1, 2012
Submission Date December 1, 2012
Published in Issue Year 2012 Volume: 21 Issue: 3

Cite

APA Akkuş, D., & Sönmez, M. F. (2012). HÜCRE ADEZYON MOLEKÜLÜ: NEKTİN. Sağlık Bilimleri Dergisi, 21(3), 205-211.
AMA Akkuş D, Sönmez MF. HÜCRE ADEZYON MOLEKÜLÜ: NEKTİN. JHS. December 2012;21(3):205-211.
Chicago Akkuş, Derya, and Mehmet Fatih Sönmez. “HÜCRE ADEZYON MOLEKÜLÜ: NEKTİN”. Sağlık Bilimleri Dergisi 21, no. 3 (December 2012): 205-11.
EndNote Akkuş D, Sönmez MF (December 1, 2012) HÜCRE ADEZYON MOLEKÜLÜ: NEKTİN. Sağlık Bilimleri Dergisi 21 3 205–211.
IEEE D. Akkuş and M. F. Sönmez, “HÜCRE ADEZYON MOLEKÜLÜ: NEKTİN”, JHS, vol. 21, no. 3, pp. 205–211, 2012.
ISNAD Akkuş, Derya - Sönmez, Mehmet Fatih. “HÜCRE ADEZYON MOLEKÜLÜ: NEKTİN”. Sağlık Bilimleri Dergisi 21/3 (December 2012), 205-211.
JAMA Akkuş D, Sönmez MF. HÜCRE ADEZYON MOLEKÜLÜ: NEKTİN. JHS. 2012;21:205–211.
MLA Akkuş, Derya and Mehmet Fatih Sönmez. “HÜCRE ADEZYON MOLEKÜLÜ: NEKTİN”. Sağlık Bilimleri Dergisi, vol. 21, no. 3, 2012, pp. 205-11.
Vancouver Akkuş D, Sönmez MF. HÜCRE ADEZYON MOLEKÜLÜ: NEKTİN. JHS. 2012;21(3):205-11.