Volume 272, Number 51, Issue of December 19, 1997 pp. 32198-32205

Identification of Cell Binding Sequences in Mouse Laminin 1 Chain by Systematic Peptide Screening

(Received for publication, August 15, 1997, and in revised form, October 2, 1997)

Motoyoshi Nomizu , Yuichiro Kuratomi , Sang-Yong Song , M. Lourdes Ponce , Matthew P. Hoffman , Sharon K. Powell , Kengo Miyoshi ^§ , Akira Otaka ^§ , Hynda K. Kleinman and Yoshihiko Yamada

From the  Craniofacial Developmental Biology and Regeneration Branch, NIDR, National Institutes of Health, Bethesda, Maryland 20892 and the ^§ Faculty of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606, Japan

Laminin-1, a major component of basement membranes, consists of three different chains designated 1, 1, and 1 and has diverse biological functions. We have identified cell binding sites on the mouse laminin 1 chain, using systematic screening of 165 overlapping synthetic peptides covering the entire chain. We identified 12 cell binding sequences using HT-1080 human fibrosarcoma and B16-F10 mouse melanoma cells in two independent assays employing peptide-conjugated Sepharose beads and peptide-coated dishes. Four peptides (C-16, C-28, C-64, and C-68) located on the globular domains of the 1 chain were the most active and showed dose-dependent cell attachment. Cell attachment to C-68 was inhibited by EDTA and by anti-₂₁ integrin antibodies. Cell attachment to C-16 and C-64 was partially inhibited by EDTA but was not inhibited by anti-integrin antibodies. EDTA and anti-integrin antibodies did not affect cell attachment to C-28. The four peptides were tested in adhesion and differentiation assays with endothelial, neuronal, and human salivary gland cells. C-16 was the most active for all of the cells, whereas the other three peptides showed cell type specificity in their activities. The active core sequences of C-16, C-28, C-64, and C-68 are YVRL, IRVTLN, TTVKYIFR, and SIKIRGTY, respectively. These sequences are highly conserved among the different species and in the laminin 2 chain. These results suggest that the specific sequences on the laminin 1 chain are biologically active and interact with distinct cell surface receptors.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				V. M. Freitas, V. F. Vilas-Boas, D. C. Pimenta, V. Loureiro, M. A. Juliano, M. R. Carvalho, J. J.V. Pinheiro, A. C.M. Camargo, A. S. Moriscot, M. P. Hoffman, et al. SIKVAV, a Laminin {alpha}1-Derived Peptide, Interacts with Integrins and Increases Protease Activity of a Human Salivary Gland Adenoid Cystic Carcinoma Cell Line through the ERK 1/2 Signaling Pathway Am. J. Pathol., July 1, 2007; 171(1): 124 - 138. [Abstract] [Full Text] [PDF]

				S. Hibino, M. Shibuya, M. P. Hoffman, J. A. Engbring, R. Hossain, M. Mochizuki, S. Kudoh, M. Nomizu, and H. K. Kleinman Laminin {alpha}5 Chain Metastasis- and Angiogenesis-Inhibiting Peptide Blocks Fibroblast Growth Factor 2 Activity by Binding to the Heparan Sulfate Chains of CD44 Cancer Res., November 15, 2005; 65(22): 10494 - 10501. [Abstract] [Full Text] [PDF]

				V. Vittal, A. Rose, K. E. Gregory, M. J. Kelley, and T. S. Acott Changes in Gene Expression by Trabecular Meshwork Cells in Response to Mechanical Stretching Invest. Ophthalmol. Vis. Sci., August 1, 2005; 46(8): 2857 - 2868. [Abstract] [Full Text] [PDF]

				S. Hibino, M. Shibuya, J. A. Engbring, M. Mochizuki, M. Nomizu, and H. K. Kleinman Identification of an Active Site on the Laminin {alpha}5 Chain Globular Domain That Binds to CD44 and Inhibits Malignancy Cancer Res., July 15, 2004; 64(14): 4810 - 4816. [Abstract] [Full Text] [PDF]

				N. Suzuki, H. Nakatsuka, M. Mochizuki, N. Nishi, Y. Kadoya, A. Utani, S. Oishi, N. Fujii, H. K. Kleinman, and M. Nomizu Biological Activities of Homologous Loop Regions in the Laminin {alpha} Chain G Domains J. Biol. Chem., November 14, 2003; 278(46): 45697 - 45705. [Abstract] [Full Text] [PDF]

				F. Z. Cui, W. M. Tian, Y. W. Fan, S. P. Hou, Q. Y. Xu, and I.-S. Lee Cerebrum Repair with PHPMA Hydrogel Immobilized with Neurite-Promoting Peptides in Traumatic Brain Injury of Adult Rat Model Journal of Bioactive and Compatible Polymers, November 1, 2003; 18(6): 413 - 432. [Abstract] [PDF]

				M. L. Ponce, S. Hibino, A. M. Lebioda, M. Mochizuki, M. Nomizu, and H. K. Kleinman Identification of a Potent Peptide Antagonist to an Active Laminin-1 Sequence That Blocks Angiogenesis and Tumor Growth Cancer Res., August 15, 2003; 63(16): 5060 - 5064. [Abstract] [Full Text] [PDF]

				I. Okazaki, N. Suzuki, N. Nishi, A. Utani, H. Matsuura, H. Shinkai, H. Yamashita, Y. Kitagawa, and M. Nomizu Identification of Biologically Active Sequences in the Laminin alpha 4 Chain G Domain J. Biol. Chem., September 27, 2002; 277(40): 37070 - 37078. [Abstract] [Full Text] [PDF]

				M. L. PONCE, M. NOMIZU, and H. K. KLEINMAN An angiogenic laminin site and its antagonist bind through the {alpha}v{beta}3 and {alpha}5{beta}1 integrins FASEB J, June 1, 2001; 15(8): 1389 - 1397. [Abstract] [Full Text] [PDF]

				I. B. DeRoock, M. E. Pennington, T. C. Sroka, K. S. Lam, G. T. Bowden, E. L. Bair, and A. E. Cress Synthetic Peptides Inhibit Adhesion of Human Tumor Cells to Extracellular Matrix Proteins Cancer Res., April 1, 2001; 61(8): 3308 - 3313. [Abstract] [Full Text]

				F Decline and P Rousselle Keratinocyte migration requires alpha2beta1 integrin-mediated interaction with the laminin 5 gamma2 chain J. Cell Sci., January 2, 2001; 114(4): 811 - 823. [Abstract] [PDF]

				V Orian-Rousseau, D Aberdam, P Rousselle, A Messent, J Gavrilovic, G Meneguzzi, M Kedinger, and P Simon-Assmann Human colonic cancer cells synthesize and adhere to laminin-5. Their adhesion to laminin-5 involves multiple receptors among which is integrin alpha2beta1 J. Cell Sci., June 8, 2000; 111(14): 1993 - 2004. [Abstract] [PDF]

				M. L. Ponce, M. Nomizu, M. C. Delgado, Y. Kuratomi, M. P. Hoffman, S. Powell, Y. Yamada, H. K. Kleinman, and K. M. Malinda Identification of Endothelial Cell Binding Sites on the Laminin {gamma}1 Chain Circ. Res., April 2, 1999; 84(6): 688 - 694. [Abstract] [Full Text] [PDF]

				K. M. Malinda, M. Nomizu, M. Chung, M. Delgado, Y. Kuratomi, Y. Yamada, H. K. Kleinman, and M. L. Ponce Identification of laminin {alpha}1 and ß1 chain peptides active for endothelial cell adhesion, tube formation, and aortic sprouting FASEB J, January 1, 1999; 13(1): 53 - 62. [Abstract] [Full Text]

				M. Nomizu, Y. Kuratomi, K. M. Malinda, S.-Y. Song, K. Miyoshi, A. Otaka, S. K. Powell, M. P. Hoffman, H. K. Kleinman, and Y. Yamada Cell Binding Sequences in Mouse Laminin alpha 1 Chain J. Biol. Chem., December 4, 1998; 273(49): 32491 - 32499. [Abstract] [Full Text] [PDF]

				M. P. Hoffman, M. Nomizu, E. Roque, S. Lee, D. W. Jung, Y. Yamada, and H. K. Kleinman Laminin-1 and Laminin-2 G-domain Synthetic Peptides Bind Syndecan-1 and Are Involved in Acinar Formation of a Human Submandibular Gland Cell Line J. Biol. Chem., October 30, 1998; 273(44): 28633 - 28641. [Abstract] [Full Text] [PDF]

				M. P. Hoffman, J. A. Engbring, P. K. Nielsen, J. Vargas, Z. Steinberg, A. J. Karmand, M. Nomizu, Y. Yamada, and H. K. Kleinman Cell Type-specific Differences in Glycosaminoglycans Modulate the Biological Activity of a Heparin-binding Peptide (RKRLQVQLSIRT) from the G Domain of the Laminin alpha 1 Chain J. Biol. Chem., June 15, 2001; 276(25): 22077 - 22085. [Abstract] [Full Text] [PDF]

				M. Nomizu, G. Pietrzynski, T. Kato, P. Lachance, R. Menard, and E. Ziomek Substrate Specificity of the Streptococcal Cysteine Protease J. Biol. Chem., November 21, 2001; 276(48): 44551 - 44556. [Abstract] [Full Text] [PDF]