ArticleThe Journal of biological chemistry2011
Basement membrane deposition of nidogen 1 but not nidogen 2 requires the nidogen binding module of the laminin gamma1 chain.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- POGLUT2/3 mediated EGF O-glucosylation promotes separation of digits 2 and 3 by influencing fibrillin network reorganization, signaling, and cell dynamics.Developmental biology · 2025Article
- Visualization of basement membranes by a nidogen-based fluorescent reporter in mice.Matrix biology plus · 2023Article
- Interaction of non‑parenchymal hepatocytes in the process of hepatic fibrosis (Review).Molecular medicine reports · 2021Review
- Basement Membrane Changes in Ischemic Stroke.Stroke · 2020Review
- Laminin: loss-of-function studies.Cellular and molecular life sciences : CMLS · 2017Review
- Transcriptomics of post-stroke angiogenesis in the aged brain.Frontiers in aging neuroscience · 2014Article
- Skin basement membrane: the foundation of epidermal integrity--BM functions and diverse roles of bridging molecules nidogen and perlecan.BioMed research international · 2013Review
- Absence of the basement membrane component nidogen 2, but not of nidogen 1, results in increased lung metastasis in mice.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2012Article
- Laminin-411 is a vascular ligand for MCAM and facilitates TH17 cell entry into the CNS.PloS one · 2012Article
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
Abstract
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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