Disulfide-bonding between Drosophila laminin β and γ chains is essential for α chain to form αβγ trimer

Chino Kumagai, Tatsuhiko Kadowaki, Yasuo Kitagawa*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

32 Citations (Scopus)


Assembly of Drosophila laminin α, β and γ chains was analyzed by immunoprecipitation of the lysate from metabolically radiolabeled Kc 167 cells with chain-specific antibodies followed by two dimensional electrophoresis in which nonreducing and reducing SDS gel electrophoresis are combined. Precipitation of monomeric β (or γ) with anti-γ (or -β) antibody revealed that β and γ form stable dimer before they are disulfide-bonded to each other. In contrast, α associates with neither monomeric β, monomeric γ nor βγ dimer without disulfide-bonding but only with disulfide-bonded βγ dimer to form αβγ trimers. These results thus demonstrated that the interchain disulfide-boding between β and γ is essential for α to form αβγ trimer. We also found that the αβγ trimer can be secreted with α chain either disulfide-bonded or not bonded to the disulfide-bonded βγ dimer.

Original languageEnglish
Pages (from-to)211-216
Number of pages6
JournalFEBS Letters
Issue number1
Publication statusPublished - 21 Jul 1997
Externally publishedYes


  • Basement membrane
  • Disulfide-bonding
  • Drosophila
  • Laminin


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