ArticleClinical & experimental metastasis2015
Amino-terminal fragments of laminin γ2 chain stimulate migration of metastatic breast cancer cells by interacting with CD44.
Article in Clinical & experimental metastasis, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Single-cell and spatial transcriptomics reveal TNC-positive cancer-associated fibroblasts that mediate immunosuppression and promote tumor progression in basal cell carcinoma.Journal of translational medicine · 2025Article
- Article
- Extracellular matrix marker LAMC2 targets ZEB1 to promote TNBC malignancy via up-regulating CD44/STAT3 signaling pathway.Molecular medicine (Cambridge, Mass.) · 2024Article
- Understanding the role of integrins in breast cancer invasion, metastasis, angiogenesis, and drug resistance.Oncogene · 2021Review
- Laminin‑332 mediates proliferation, apoptosis, invasion, migration and epithelial‑to‑mesenchymal transition in pancreatic ductal adenocarcinoma.Molecular medicine reports · 2021Article
- Transcriptomic response of breast cancer cells to anacardic acid.Scientific reports · 2018Article
- Transcriptomic Study Reveals Recovery of Impaired Astrocytes Contribute to Neuroprotective Effects of Danhong Injection Against Cerebral Ischemia/Reperfusion-Induced Injury.Frontiers in pharmacology · 2018Article
- Highly sensitive detection of invasive lung cancer cells by novel antibody against amino-terminal domain of laminin γ2 chain.Cancer science · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Laminin γ2 (Lmγ2) chain, a subunit of the basement membrane protein laminin-332, is regarded as a typical cancer invasion marker. The overexpression of Lmγ2 chain by invasive cancer cells correlates with poor prognosis of cancer patients, and its forced expression in human cancer cells promotes their invasive growth in a nude mouse model. However, its actual roles in cancer progression, as well as the mechanism of its proinvasive effect, remain unclear. CD44 is known to be an important cancer stem cell marker and support cancer progression and stem cell functions. Here we demonstrate that amino-terminal fragments of Lmγ2 interact with CD44 on the membrane of breast cancer cells. Lmγ2 highly bound to the metastatic cell line MDA-MB-231 but poorly to the benign cell line MCF-7. The membrane receptor for Lmγ2 on MDA-MB-231 cells was identified to be the standard form of CD44 (CD44s) by co-immunoprecipitation, affinity chromatography and direct protein interaction assay. Lmγ2 interacted with CD44s through EGF-like repeat 2/3 in the Lmγ2 amino-terminus. Amino-terminal fragments of Lmγ2 induced the phosphorylation of CD44 cytoplasmic domain and stimulated migration of the cancer cells in a CD44-dependent manner. This migration was blocked by inhibitors of TGF-β receptor I (TGF-βRI) kinase. These results suggest that two important tumor markers, Lmγ2 and CD44, cooperate for cancer progression and possibly for cancer stem cell functions. TGF-βRI may be involved in the Lmγ2/CD44 interaction.
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