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          Institute: MPI für Biochemie     Collection: Emeriti Groups     Display Documents



ID: 39207.0, MPI für Biochemie / Emeriti Groups
Recombinant human laminin-10 (alpha 5,beta 1,gamma 1) - Production, purification, and migration-promoting activity on vascular endothelial cells
Authors:Doi, M.; Thyboll, J.; Kortesmaa, J.; Jansson, K.; Iivanainen, A.; Parvardeh, M.; Timpl, R.; Hedin, U.; Swedenborg, J.; Tryggvason, K.
Language:English
Date of Publication (YYYY-MM-DD):2002-04-12
Title of Journal:Journal of Biological Chemistry
Journal Abbrev.:J. Biol. Chem.
Volume:277
Issue / Number:15
Start Page:12741
End Page:12748
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:The laminin (LN) family of large heterotrimeric extracellular matrix glycoproteins has multiple functions: LNs take part in the regulation of processes such as cell migration, differentiation, and proliferation, in addition to contributing to the structure of basement membranes. LN-10, composed of alpha5, beta1, and gamma1 chains, is widely distributed in most basement membranes of both epithelia and endothelia. We determined the complete human cDNA sequence for the LN a5 chain and produced recombinant human LN-10 (rLN-10) in HEK293 cells by triple transfection of full-length cDNAs encoding the human LN alpha5, beta1, and gamma1 chains. The rLN-10 was purified using affinity chromatography and had an apparent molecular mass of -800 kDa in SDS-PAGE and a native domain structure in rotary shadowing electron microscopy. By using function- blocking monoclonal antibodies, integrin asp, was found to be a major mediator of adhesion of HT-1080 and human saphenous vein endothelial cells. Human saphenous vein endothelial cells adhered more strongly to rLN-10 than to LN-1 and LN-8 and showed better migration on rLN-10, compared with several other matrices. Considering the cell adhesive and migration-promoting properties of rLN-10 on endothelial cells, this molecule could be useful in improving the biocompatibility and endothelialization of vascular grafts.
Comment of the Author/Creator:Date: 2002, APR 12
External Publication Status:published
Document Type:Article
Communicated by:N.N.
Affiliations:MPI für Biochemie/Emeriti Groups/Protein Chemistry (R. Timpl)
External Affiliations:Karolinska Inst, Div Matrix Biol, Dept Med Biochem & Biophys,; Scheeles Vag 2,B1,4th Floor, S-17177 Stockholm, Sweden; Karolinska Inst, Div Matrix Biol, Dept Med Biochem & Biophys, S-17177 Stockholm, Sweden; Biostratum AB, S-17177 Stockholm, Sweden; Karolinska Hosp, Dept Surg Sci, Div Vasc Surg, S-17176 Stockholm, Sweden
Identifiers:ISI:000175036300033 [ID No:1]
ISSN:0021-9258 [ID No:2]
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