Cell Adhesive Sequences in Mouse Laminin β1 Chain

Nomizu, Motoyoshi; Kuratomi, Yuichiro; Ponce, M. Lourdes; Song, Sang‐Yong; Miyoshi, Kengo; Otaka, Akira; Powell, Stephen Joseph; Hoffman, Matthew P.; Kleinman, Hynda K.; Yamada, Yoshihiko

doi:10.1006/abbi.2000.1828

Cited by 79 publications

(66 citation statements)

References 49 publications

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“…22,23,26,43,44,46 -52 Several active sequences on laminin-111 have been identified using proteolytic fragments, recombinant proteins, and systematic peptide screening. [53][54][55] The YIGSR sequence located on the ␤1 chain promotes cell adhesion and migration and inhibits angiogenesis and metastasis. 45,48,56 The PDGSR and F-9 (RYVVLPR) sequences located on the ␤1 chain also promote cell adhesion.…”

Section: Discussionmentioning

confidence: 99%

SIKVAV, a Laminin α1-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

Freitas

Vilas-Boas

Pimenta

et al. 2007

The American Journal of Pathology

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Adenoid cystic carcinoma is a frequently occurring malignant salivary gland neoplasm. We studied the induction of protease activity by the laminin-derived peptide, SIKVAV, in cells (CAC2) derived from this neoplasm. Laminin ␣1 and matrix metalloproteinases (MMPs) 2 and 9 were immunolocalized in adenoid cystic carcinoma cells in vivo and in vitro. CAC2 cells cultured on SIKVAV showed a dose-dependent increase of MMP9 as detected by zymography and colocalization of ␣3 and ␣6 integrins. Small interfering RNA (siRNA) knockdown of integrin expression in CAC2 cells resulted in decreased adhesion to the peptide. SIKVAV affinity chromatography and immunoblot analysis showed that ␣3, ␣6, and ␤1 integrins were eluted from the SIKVAV column, which was confirmed by mass spectrometry and a solid-phase binding assay. Small interfering RNA experiments also showed that these integrins, through extracellular signal-regulated kinase (ERK) 1/2 signaling, regulate MMP secretion induced by SIKVAV in CAC2 cells. We propose that SIKVAV increases protease activity of a human salivary gland adenoid cystic carcinoma cell line through ␣3␤1 and ␣6␤1 integrins and the ERK 1/2 signaling pathway.

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Section: Discussionmentioning

confidence: 99%

SIKVAV, a Laminin α1-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

Freitas

Vilas-Boas

Pimenta

et al. 2007

The American Journal of Pathology

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“…Many laboratories are now beginning to identify additional active sites on the homologous laminin chains (10,11). Most of the active peptides are localized in the globular domains (G-domains) and play a critical role in binding to cell surface receptors in a peptide-and cell typespecific manner (12)(13)(14)(15)(16). Several receptors for these active sequences have been identified.…”

Section: Introductionmentioning

confidence: 99%

Identification of an Active Site on the Laminin α5 Chain Globular Domain That Binds to CD44 and Inhibits Malignancy

et al. 2004

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The laminin ␣5 chain is a component of laminin-10 (␣5␤1␥1) and -11 (␣5␤2␥1). In this study, we have screened 113 overlapping synthetic peptides from the laminin ␣5 globular domain (G-domain) for cell attachment activity with B16-F10 cells using peptide-coated dishes. Eleven attachment-active peptides were identified. In vivo experimental B16-F10 pulmonary metastasis and primary tumor growth assays found that 4 of the 11 peptides inhibited tumor metastasis and growth and increased apoptosis. These four peptides also blocked tumor cell migration, invasion, and angiogenesis. Two of the peptides were highly homologous and showed significant similarity to sequences in collagens. We sought to identify the B16-F10 cell surface receptors for each of the four active peptides using peptide affinity chromatography. Only one peptide recognized a cell surface protein. Peptide A5G27 (RLVSYNGIIFFLK, residues 2892-2904) bound a diffuse M r ϳ120,000 -180,000 band that eluted with 2 M NaCl. Glycosidase digestion of the 2 M eluate yielded protein bands of M r 90,000 and 60,000 that reacted in Western blot analysis with antibodies to CD44. Immunoprecipitation of the A5G27-bound membrane proteins with various cell surface proteoglycan antibodies confirmed CD44 as the surface receptor for A5G27. Finally, attachment assays to A5G27 in the presence of soluble glycosaminoglycans (GAGs) identified the GAGs of CD44 as the binding sites for A5G27. Our results suggest that A5G27 binds to the CD44 receptor of B16-F10 melanoma cells via the GAGs on CD44 and, thus, inhibits tumor cell migration, invasion, and angiogenesis in a dominant-negative manner.

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“…[26][27][28][29] The IKVAV sequence within the LCC domain of the 1 chain has been well studied for its roles in cell attachment, migration, and neurite outgrowth.…”

Section: Discussionmentioning

confidence: 99%

Expression and Chain Assembly of Human Laminin-332 in an Insect Cell-Free Translation System

Phan

Ezure

Ito

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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Cell Adhesive Sequences in Mouse Laminin β1 Chain

Cited by 79 publications

References 49 publications

SIKVAV, a Laminin α1-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

SIKVAV, a Laminin α1-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

Identification of an Active Site on the Laminin α5 Chain Globular Domain That Binds to CD44 and Inhibits Malignancy

Expression and Chain Assembly of Human Laminin-332 in an Insect Cell-Free Translation System

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