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Tytuł pozycji:

Basement membrane deposition of nidogen 1 but not nidogen 2 requires the nidogen binding module of the laminin gamma1 chain.

Tytuł :
Basement membrane deposition of nidogen 1 but not nidogen 2 requires the nidogen binding module of the laminin gamma1 chain.
Autorzy :
Mokkapati S; Department of Dermatology, University Hospital of Cologne, 50937 Cologne, Germany.
Fleger-Weckmann A
Bechtel M
Koch M
Breitkreutz D
Mayer U
Smyth N
Nischt R
Pokaż więcej
Źródło :
The Journal of biological chemistry [J Biol Chem] 2011 Jan 21; Vol. 286 (3), pp. 1911-8. Date of Electronic Publication: 2010 Nov 17.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
Język :
English
Imprint Name(s) :
Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
MeSH Terms :
Basement Membrane/*metabolism
Laminin/*metabolism
Membrane Glycoproteins/*metabolism
Animals ; Calcium-Binding Proteins ; Cell Adhesion Molecules ; Gene Deletion ; Laminin/genetics ; Membrane Glycoproteins/genetics ; Mice ; Mice, Knockout
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Grant Information :
G0501515 United Kingdom Medical Research Council; BJ10R141 United Kingdom Medical Research Council
Substance Nomenclature :
0 (Calcium-Binding Proteins)
0 (Cell Adhesion Molecules)
0 (Laminin)
0 (Membrane Glycoproteins)
0 (Nid2 protein, mouse)
0 (laminin gamma 1)
0 (nidogen)
Entry Date(s) :
Date Created: 20101119 Date Completed: 20110224 Latest Revision: 20210205
Update Code :
20210210
PubMed Central ID :
PMC3023487
DOI :
10.1074/jbc.M110.149864
PMID :
21084308
Czasopismo naukowe
The nidogen-laminin interaction is proposed to play a key role in basement membrane (BM) assembly. However, though there are similarities, the phenotypes in mice lacking nidogen 1 and 2 (nidogen double null) differ to those of mice lacking the nidogen binding module (γ1III4) of the laminin γ1 chain. This indicates different cell- and tissue-specific functions for nidogens and their interaction with laminin and poses the question of whether the phenotypes in nidogen double null mice are caused by the loss of the laminin-nidogen interaction or rather by other unknown nidogen functions. To investigate this, we analyzed BMs, in particular those in the skin of mice lacking the nidogen binding module. In contrast to nidogen double null mice, all skin BMs in γ1III4-deficient mice appeared normal. Furthermore, although nidogen 1 deposition was strongly reduced, nidogen 2 appeared unchanged. Mice with additional deletion of the laminin γ3 chain, which contains a γ1-like nidogen binding module, showed a further reduction of nidogen 1 in the dermoepidermal BM; however, this again did not affect nidogen 2. This demonstrates that in vivo only nidogen 1 deposition is critically dependent on the nidogen binding modules of the laminin γ1 and γ3 chains, whereas nidogen 2 is independently recruited either by binding to an alternative site on laminin or to other BM proteins.

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