Expression and chain assembly of human laminin-332 in an insect cell-free translation system

Hoang Phuong Phan, Toru Ezure, Masaaki Ito, Tatsuhiko Kadowaki, Yasuo Kitagawa, Tomoaki Niimi*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


Laminins are a family of large heterotrimeric glycoproteins comprising α, β, and γ chains. To determine the molecular mechanisms underlying chain assembly in vitro, we expressed human laminin-332 subunits in an insect cell-free translation system. We successfully produced the β3-γ2 heterodimer and the α3-β3-γ2 heterotrimer of the laminin coiled-coil (LCC) domain following co-translation of each chain. The α3-β3 and the α3-γ2 heterodimer were not detected, suggesting that the α3 chain can assemble with only β3-γ2 heterodimer to form a heterotrimer via disulfide bonds. These results are consistent with those of a previous report indicating that laminin chain assembly proceeds through the β-γ heterodimer to the α-β-γ heterotrimer in vivo. We suggest that the cell-free translation system is a valid system with which to study the mechanisms underlying laminin chain assembly.

Original languageEnglish
Pages (from-to)1847-1852
Number of pages6
JournalBioscience, Biotechnology and Biochemistry
Issue number7
Publication statusPublished - 2008
Externally publishedYes


  • Basement membrane
  • Coiled-coil
  • Disulfide bond
  • Laminin-5


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