Active peptides from the carboxyl-terminal globular domain of laminin α2 and Drosophila α chains

Motoyoshi Nomizu, Sang Yong Song, Yuichiro Kuratomi, Masahiko Tanaka, Woo Ho Kim, Hynda K. Kleinman, Yoshihiko Yamada

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Abstract

The laminin α1 chain carboxyl-terminal globular domain (G domain) contains multiple biological activities. Recently, we identified five cell binding sequences from the G domain by screening with overlapping 12-mer peptides encompassing the entire domain. The structures of these five sequences in the α1 chain are conserved in the corresponding regions of the different laminin α chains. Here we characterize the adhesion activities of the corresponding peptide segments from both the mouse laminin α2 chain and Drosophila laminin α chain using peptide-coated plastic plates and peptide-conjugated Sepharose beads. Using several cell lines, the laminin α2 chain peptides showed cell attachment and/or spreading activities with cell type specificities. Cell spreading on MG-10 was inhibited by integrin antibodies. Four of the Drosophila laminin peptides showed cell attachment activities. These results suggest that biologically active regions in the G domain are conserved in the laminin α1 and α2 chains, and that these regions in laminin play an important role in cell surface receptor interactions.

Original languageEnglish
Pages (from-to)37-42
Number of pages6
JournalFEBS Letters
Volume396
Issue number1
DOIs
StatePublished - 28 Oct 1996

Fingerprint

Laminin
Drosophila
Peptides
Cell Surface Receptors
Bioactivity
Integrins
Sepharose
Plastics
Screening
Adhesion
Cells
Cell Line
Antibodies

Keywords

  • Basement membrane
  • Cell attachment
  • Integrin
  • Laminin
  • Synthetic peptide

Cite this

Nomizu, Motoyoshi ; Song, Sang Yong ; Kuratomi, Yuichiro ; Tanaka, Masahiko ; Kim, Woo Ho ; Kleinman, Hynda K. ; Yamada, Yoshihiko. / Active peptides from the carboxyl-terminal globular domain of laminin α2 and Drosophila α chains. In: FEBS Letters. 1996 ; Vol. 396, No. 1. pp. 37-42.
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abstract = "The laminin α1 chain carboxyl-terminal globular domain (G domain) contains multiple biological activities. Recently, we identified five cell binding sequences from the G domain by screening with overlapping 12-mer peptides encompassing the entire domain. The structures of these five sequences in the α1 chain are conserved in the corresponding regions of the different laminin α chains. Here we characterize the adhesion activities of the corresponding peptide segments from both the mouse laminin α2 chain and Drosophila laminin α chain using peptide-coated plastic plates and peptide-conjugated Sepharose beads. Using several cell lines, the laminin α2 chain peptides showed cell attachment and/or spreading activities with cell type specificities. Cell spreading on MG-10 was inhibited by integrin antibodies. Four of the Drosophila laminin peptides showed cell attachment activities. These results suggest that biologically active regions in the G domain are conserved in the laminin α1 and α2 chains, and that these regions in laminin play an important role in cell surface receptor interactions.",
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Nomizu, M, Song, SY, Kuratomi, Y, Tanaka, M, Kim, WH, Kleinman, HK & Yamada, Y 1996, 'Active peptides from the carboxyl-terminal globular domain of laminin α2 and Drosophila α chains', FEBS Letters, vol. 396, no. 1, pp. 37-42. https://doi.org/10.1016/0014-5793(96)01060-5

Active peptides from the carboxyl-terminal globular domain of laminin α2 and Drosophila α chains. / Nomizu, Motoyoshi; Song, Sang Yong; Kuratomi, Yuichiro; Tanaka, Masahiko; Kim, Woo Ho; Kleinman, Hynda K.; Yamada, Yoshihiko.

In: FEBS Letters, Vol. 396, No. 1, 28.10.1996, p. 37-42.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Kim, Woo Ho

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AU - Yamada, Yoshihiko

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