title: Structures and dynamic motion of laminin-1 as observed by atomic force microscopy.
abstract: Laminins are a family of multifunctional extracellular matrix glycoproteins that play important roles in the development and maintenance of tissue organization via their interactions with cells and other extracellular matrix proteins. To understand the structural basis of laminins' functions, we examined the motion of laminin-1 (Ln-1) in physiological buffers using atomic force microscopy. While many Ln-1 molecules assumed the expected cruciform structure, unexpected dynamic movements of the Ln-1 arms were observed in aqueous environments. These dynamic movements of the Ln-1 arms may contribute to the diversity of laminin functions.
authors.affiliation: Department of Physics, University of California, Santa Barbara 93106, USA.
authors.forename: C H
authors.initials: CH
authors.lastname: Chen
authors.forename: D O
authors.initials: DO
authors.lastname: Clegg
authors.forename: H G
authors.initials: HG
authors.lastname: Hansma
mesh_terms: D000818:Animals; D002021:Buffers; D006982:Hypertonic Solutions; D007038:Hypotonic Solutions; D007797:Laminin / Q000737:chemistry* / Q000502:physiology; D051379:Mice; D018625:Microscopy, Atomic Force / Q000379:methods; D009038:Motion; D012513:Sarcoma, Experimental
chemical_list: D002021:Buffers; D006982:Hypertonic Solutions; D007038:Hypotonic Solutions; D007797:Laminin