Biologically active sequences in the mouse laminin α3 chain G domain

Biochemistry

Volumn 48, Issue 44, 2009, Pages 10522-10532

  Urushibata, Shunsuke ^a   Katagiri, Fumihiko ^a   Takaki, Shu ^a   Yamada, Yuji ^a   Fujimori, Chikara ^a   Hozumi, Kentaro ^a   Kikkawa, Yamato ^a   Kadoya, Yuichi ^b   Nomizu, Motoyoshi ^a  

^a TOKYO UNIVERSITY OF PHARMACY AND LIFE SCIENCES   (Japan)

^b KITASATO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SEQUENCES; ACTIVE SITE; BIOLOGICAL ACTIVITIES; BIOLOGICAL FUNCTIONS; CELL ATTACHMENTS; CHITOSAN MEMBRANE; FIBROSARCOMA CELLS; HT-1080; HUMAN DERMAL FIBROBLASTS; HUMAN SKIN; INTEGRINS; KERATINOCYTES; LAMININ; MOLECULAR MECHANISM; NEURITE OUTGROWTH; PC12 CELLS; PEPTIDE BEADS; RECEPTOR INTERACTION; STRESS FIBERS; SYNTHETIC PEPTIDE; VINCULIN;

ADHESION; ANTIBODIES; CELL ADHESION; CELL CULTURE; CHITIN; CHITOSAN; GEL PERMEATION CHROMATOGRAPHY; PEPTIDES; POLYSACCHARIDES; SKIN;

CELLS;

BETA1 INTEGRIN; CHITOSAN; HEPARIN; LAMININ; LAMININ ALPHA 3 CHAIN; UNCLASSIFIED DRUG; VINCULIN;

ANIMAL EXPERIMENT; ARTICLE; CANCER CELL; CELL ADHESION; FIBROBLAST; FIBROSARCOMA; KERATINOCYTE; MOUSE; NERVE FIBER GROWTH; NONHUMAN; PRIORITY JOURNAL; STRESS FIBER;

AMINO ACID SEQUENCE; ANIMALS; CELL ADHESION; CELL LINE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; HUMANS; IMMUNOHISTOCHEMISTRY; LAMININ; MICE; MOLECULAR SEQUENCE DATA; PC12 CELLS; RATS;

EID: 70449409966     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901421t     Document Type: Article

References (44)

1. Colognato, H., and Yurchenco, P. D. (2000) Form and function: The laminin family of heterotrimers. Dev. Dyn. 218, 213-234.
2. Miner, J. H., and Yurchenco, P. D. (2004) Laminin functions in tissue morphogenesis. Annu. Rev. Cell Dev. Biol. 20, 255-284.
3. Aumailley, M., Bruckner-Tuderman, L., Carter, W. G., Deutzmann, R., Edgar, D., Ekblom, P., Engel, J., Engvall, E., Hohenester, E., Jones, J. C., Kleinman, H. K., Marinkovich, M. P., Martin, G. R., Mayer, U., Meneguzzi, G., Miner, J. H., Miyazaki, K., Patarroyo, M., Paulsson, M., Quaranta, V., Sanes, J. R., Sasaki, T., Sekiguchi, K., Sorokin, L. M., Talts, J. F., Tryggvason, K., Uitto, J., Virtanen, I., von der Mark, K., Wewer, U. M., Yamada, Y., and Yurchenco, P. D. (2005) A simplified laminin nomenclature. Matrix Biol. 24, 326-332.
4. Yan, H. H., and Cheng, C. Y. (2006) Laminin α3 forms a complex with β3 and γ3 chains that serves as the ligand for α6β1- integrin at the apical ectoplasmic specialization in adult rat testes. J. Biol. Chem. 281, 17286-17303.
5. Nomizu, M., Kim, W. H., Yamamura, K., Utani, A., Song, S. Y., Otaka, A., Roller, P. P., Kleinman, H. K., and Yamada, Y. (1995) Identification of cell binding sites in the laminin α1 chain carboxylterminal globular domain by systematic screening of synthetic peptides. J. Biol. Chem. 270, 20583-20590.
6. Nomizu, M., Kuratomi, Y., Malinda, K. M., Song, S. Y., Miyoshi, K., Otaka, A., Powell, S. K., Hoffman, M. P., Kleinman, H. K., and Yamada, Y. (1998) Cell binding sequences in mouse laminin α1 chain. J. Biol. Chem. 273, 32491-32499.
7. Nomizu, M., Kuratomi, Y., Ponce, M. L., Song, S. Y., Miyoshi, K., Otaka, A., Powell, S. K., Hoffman, M. P., Kleinman, H. K., and Yamada, Y. (2000) Cell adhesive sequences in mouse laminin β1 chain. Arch. Biochem. Biophys. 378, 311-320.
8. Nomizu, M., Kuratomi, Y., Song, S. Y., Ponce, M. L., Hoffman, M. P., Powell, S. K., Miyoshi, K., Otaka, A., Kleinman, H. K., and Yamada, Y. (1997) Identification of cell binding sequences in mouse laminin γ1 chain by systematic peptide screening. J. Biol. Chem. 272, 32198-32205.
9. Yamada, K. M. (1991) Adhesive recognition sequences. J. Biol. Chem. 266, 12809-12812.
10. Yamada, Y., and Kleinman, H. K. (1992) Functional domains of cell adhesion molecules. Curr. Opin. Cell Biol. 4, 819-823.
11. Suzuki, N., Ichikawa,N., Kasai, S., Yamada, M., Nishi, N., Morioka, H., Yamashita, H., Kitagawa, Y., Utani, A., Hoffman, M. P., and Nomizu, M. (2003) Syndecan binding sites in the laminin α1 chain G domain. Biochemistry 42, 12625-12633.
12. Suzuki, N., Yokoyama, F., and Nomizu, M. (2005) Functional sites in the laminin R chains. Connect. Tissue Res. 46, 142-152.
13. Timpl, R., Tisi, D., Talts, J. F., Andac, Z., Sasaki, T., and Hohenester, E. (2000) Structure and function of laminin LG modules. Matrix Biol. 19, 309-317.
14. Nguyen, B. P., Gil, S. G., and Carter, W. G. (2000) Deposition of laminin 5 by keratinocytes regulates integrin adhesion and signaling. J. Biol. Chem. 275, 31896-31907.
15. Sugawara, K., Tsuruta, D., Ishii, M., Jones, J. C., and Kobayashi, H. (2008) Laminin-332 and -511 in skin. Exp. Dermatol. 17, 473-480.
16. Marinkovich, M. P., Lunstrum, G. P., Keene, D. R., and Burgeson, R. E. (1992) The dermal-epidermal junction of human skin contains a novel laminin variant. J. Cell Biol. 119, 695-703.
17. Tsubota, Y., Yasuda, C., Kariya, Y., Ogawa, T., Hirosaki, T., Mizushima, H., and Miyazaki, K. (2005) Regulation of biological activity and matrix assembly of laminin-5 by COOH-terminal, LG4-5 domain of α3 chain. J. Biol. Chem. 280, 14370-14377.
18. Kariya, Y., Tsubota, Y., Hirosaki, T., Mizushima, H., Puzon-McLaughlin, W., Takada, Y., and Miyazaki, K. (2003) Differential regulation of cellular adhesion and migration by recombinant laminin-5 forms with partial deletion or mutation within the G3 domain of α3 chain. J. Cell. Biochem. 88, 506-520.
19. Mizushima, H., Takamura, H., Miyagi, Y., Kikkawa, Y., Yamanaka, N., Yasumitsu, H., Misugi, K., and Miyazaki, K. (1997) Identification of integrin-dependent and -independent cell adhesion domains in COOH-terminal globular region of laminin-5 α3 chain. Cell Growth Differ. 8, 979-987.
20. Shang, M., Koshikawa, N., Schenk, S., and Quaranta, V. (2001) The LG3 module of laminin-5 harbors a binding site for integrin α3β1 that promotes cell adhesion, spreading, and migration. J. Biol. Chem. 276, 33045-33053.
21. Ryan, M. C., Lee, K., Miyashita, Y., and Carter, W. G. (1999) Targeted disruption of the LAMA3 gene in mice reveals abnormalities in survival and late stage differentiation of epithelial cells. J. Cell Biol. 145, 1309-1323. (Pubitemid 29293640)
22. Utani, A., Nomizu, M., Matsuura, H., Kato, K., Kobayashi, T., Takeda, U., Aota, S., Nielsen, P. K., and Shinkai, H. (2001) A unique sequence of the laminin α3 G domain binds to heparin and promotes cell adhesion through syndecan-2 and -4. J. Biol. Chem. 276, 28779-28788.
23. Kato, K., Utani, A., Suzuki, N., Mochizuki, M., Yamada, M., Nishi, N., Matsuura, H., Shinkai, H., and Nomizu, M. (2002) Identification of neurite outgrowth promoting sites on the laminin α3 chain G domain. Biochemistry 41, 10747-10753. (Pubitemid 34971050)
24. Araki, E., Momota, Y., Togo, T., Tanioka, M., Hozumi, K., Nomizu, M., Miyachi, Y., and Utani, A. (2009) Clustering of syndecan-4 and integrin β1 by laminin α3 chain-derived peptide promotes keratinocyte migration. Mol. Biol. Cell 20, 3012-3024.
25. Utani, A., Momota, Y., Endo, H., Kasuya, Y., Beck, K., Suzuki, N., Nomizu, M., and Shinkai, H. (2003) Laminin α3 LG4 module induces matrix metalloproteinase-1 through mitogen-activated protein kinase signaling. J. Biol. Chem. 278, 34483-34490.
26. Hohenester, E., Tisi, D., Talts, J. F., and Timpl, R. (1999) The crystal structure of a laminin G-like module reveals the molecular basis of α-dystroglycan binding to laminins, perlecan, and agrin. Mol. Cell 4, 783-792.
27. Suzuki, N., Nakatsuka, H., Mochizuki, M., Nishi, N., Kadoya, Y., Utani, A., Oishi, S., Fujii, N., Kleinman, H. K., and Nomizu, M. (2003) Biological activities of homologous loop regions in the laminin R chain G domains. J. Biol. Chem. 278, 45697-45705.
28. Kato-Takagaki, K., Suzuki, N., Yokoyama, F., Takaki, S., Umezawa, K., Higo, J., Mochizuki, M., Kikkawa, Y., Oishi, S., Utani, A., and Nomizu, M. (2007) Cyclic peptide analysis of the biologically active loop region in the laminin α3 chain LG4 module demonstrates the importance of peptide conformation on biological activity. Biochemistry 46, 1952-1960.
29. Galliano, M. F., Aberdam, D., Aguzzi, A., Ortonne, J. P., and Meneguzzi, G. (1995) Cloning and complete primary structure of the mouse laminin δ3 chain. Distinct expression pattern of the laminin α3A and α3B chain isoforms. J. Biol. Chem. 270, 21820-21826.
30. Mochizuki, M., Kadoya, Y., Wakabayashi, Y., Kato, K., Okazaki, I., Yamada, M., Sato, T., Sakairi, N., Nishi, N., and Nomizu, M. (2003) Laminin-1 peptide-conjugated chitosan membranes as a novel approach for cell engineering. FASEB J. 17, 875-877.
31. Mochizuki, M., Yamagata, N., Philp, D., Hozumi, K., Watanabe, T., Kikkawa, Y., Kadoya, Y., Kleinman, H. K., and Nomizu, M. (2007) Integrin-dependent cell behavior on ECM peptide-conjugated chitosan membranes. Biopolymers 88, 122-130. (Pubitemid 46657978)
32. Greene, L. A., and Tischler, A. S. (1976) Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor. Proc. Natl. Acad. Sci. U.S.A. 73, 2424-2428.
33. Richard, B. L., Nomizu, M., Yamada, Y., and Kleinman, H. K. (1996) Identification of synthetic peptides derived from laminin α1 and α2 chains with cell type specificity for neurite outgrowth. Exp. Cell Res. 228, 98-105.
34. Hoffman, M. P., Engbring, J. A., Nielsen, P. K., Vargas, J., Steinberg, Z., Karmand, A. J., Nomizu, M., Yamada, Y., and Kleinman, H. K. (2001) Cell type-specific differences in glycosaminoglycans modulate the biological activity of a heparin-binding peptide (RKRLQVQLSIRT) from the G domain of the laminin α1 chain. J. Biol. Chem. 276, 22077-22085.
35. Miner, J. H., Patton, B. L., Lentz, S. I., Gilbert, D. J., Snider,W. D., Jenkins, N. A., Copeland, N. G., and Sanes, J. R. (1997) The laminin R chains: Expression, developmental transitions, and chromosomal locations of α1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel α3 isoform. J. Cell Biol. 137, 685-701.
36. Kim, J. M., Park, W. H., and Min, B. M. (2005) The PPFLMLLKGSTR motif in globular domain 3 of the human laminin-5 α3 chain is crucial for integrin α3β1 binding and cell adhesion. Exp. Cell Res. 304, 317-327.
37. Okamoto, O., Bachy, S., Odenthal, U., Bernaud, J., Rigal, D., Lortat-Jacob, H., Smyth, N., and Rousselle, P. (2003) Normal human keratinocytes bind to the α3LG4/5 domain of unprocessed laminin-5 through the receptor syndecan-1. J. Biol. Chem. 278, 44168-44177.
38. Hozumi, K., Suzuki, N., Uchiyama, Y., Katagiri, F., Kikkawa, Y., and Nomizu, M. (2009) Chain-specific heparin-binding sequences in the laminin R chain LG45 modules. Biochemistry 48, 5375-5381.
39. Tashiro, K., Sephel, G. C., Weeks, B., Sasaki, M., Martin, G. R., Kleinman, H. K., and Yamada, Y. (1989) A synthetic peptide containing the IKVAV sequence from theAchain of laminin mediates cell attachment, migration, and neurite outgrowth. J. Biol. Chem. 264, 16174-16182.
40. Kasai, S., Urushibata, S., Hozumi, K., Yokoyama, F., Ichikawa, N., Kadoya, Y., Nishi, N., Watanabe, N., Yamada, Y., and Nomizu, M. (2007) Identification ofmultiple amyloidogenic sequences in laminin-1. Biochemistry 46, 3966-3974.
41. Hozumi, K., Suzuki, N., Nielsen, P. K., Nomizu, M., and Yamada, Y. (2006) Laminin α1 chain LG4 module promotes cell attachment through syndecans and cell spreading through integrin α2β1. J. Biol. Chem. 281, 32929-32940.
42. Carafoli, F., Clout, N. J., and Hohenester, E. (2009) Crystal structure of the LG1-3 region of the laminin α2 chain. J. Biol. Chem. 284, 22786-22792.
43. Okazaki, I., Suzuki, N., Nishi, N., Utani, A., Matsuura, H., Shinkai, H., Yamashita, H., Kitagawa, Y., and Nomizu, M. (2002) Identification of biologically active sequences in the laminin α4 chain G domain. J. Biol. Chem. 277, 37070-37078.
44. Grose, R., Hutter, C., Bloch, W., Thorey, I., Watt, F. M., Fassler, R., Brakebusch, C., and Werner, S. (2002) A crucial role of β1 integrins for keratinocyte migration in vitro and during cutaneous wound repair. Development 129, 2303-2315. (Pubitemid 34874240)