Role of laminin terminal globular domains in basement membrane assembly

Karen K. McKee, David Harrison, Stephanie Capizzi, Peter D. Yurchenco

Research output: Contribution to journalArticlepeer-review

135 Scopus citations


Laminins contribute to basement membrane assembly through interactions of their N- and C-terminal globular domains. To further analyze this process, recombinant laminin-111 heterotrimers with deletions and point mutations were generated by recombinant expression and evaluated for their ability to self-assemble, interact with nidogen-1 and type IV collagen, and form extracellular matrices on cultured Schwann cells by immunofluorescence and electron microscopy. Wild-type laminin and laminin without LG domains polymerized in contrast to laminins with deleted α1-, β1-, or γ1-LN domains or with duplicated β1- or α1-LN domains. Laminins with a full complement of LN and LG domains accumulated on cell surfaces substantially above those lacking either LN or LG domains and formed a lamina densa. Accumulation of type IV collagen onto the cell surface was found to require laminin with separate contributions arising from the presence of laminin LN domains, nidogen-1, and the nidogen-binding site in laminin. Collectively, the data support the hypothesis that basement membrane assembly depends on laminin self-assembly through formation of α-, β-, and γ-LN domain complexes and LG-mediated cell surface anchorage. Furthermore, type IV collagen recruitment into the laminin extracellular matrices appears to be mediated through a nidogen bridge with a lesser contribution arising from a direct interaction with laminin.

Original languageEnglish (US)
Pages (from-to)21437-21447
Number of pages11
JournalJournal of Biological Chemistry
Issue number29
StatePublished - Jul 20 2007

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Role of laminin terminal globular domains in basement membrane assembly'. Together they form a unique fingerprint.

Cite this