ArticleThe Journal of biological chemistry2010
Self-association of calcium-binding protein S100A4 and metastasis.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 39 citations in OpenAlex.
- Preclinical evaluation of anEJNMMI radiopharmacy and chemistry · 2024Article
- Targeted Destruction of S100A4 Inhibits Metastasis of Triple Negative Breast Cancer Cells.Biomolecules · 2023Article
- The Role of the C-Terminal Lysine of S100P in S100P-Induced Cell Migration and Metastasis.Biomolecules · 2021Article
- Article
- The solution structure of human calcium-bound S100A4 mutated at four cysteine loci.Journal of biomolecular NMR · 2015Article
- Functional expression, characterization and application of the human S100A4 protein.Molecular medicine reports · 2015Article
- Increased expression levels of S100A4 associated with hypoxia-induced invasion and metastasis in esophageal squamous cell cancer.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014Article
- Joining S100 proteins and migration: for better or for worse, in sickness and in health.Cellular and molecular life sciences : CMLS · 2014Review
- Functionally active rat S100A4 from a polymerase chain reaction-synthesized gene expressed in soluble form inOncology letters · 2014Article
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- Article
- Single molecule fluorescence detection and tracking in mammalian cells: the state-of-the-art and future perspectives.International journal of molecular sciences · 2012Review
- S100P dissociates myosin IIA filaments and focal adhesion sites to reduce cell adhesion and enhance cell migration.The Journal of biological chemistry · 2012Article
- Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling.Structure (London, England : 1993) · 2012Article
- Two functional S100A4 monomers are necessary for regulating nonmuscle myosin-IIA and HCT116 cell invasion.Biochemistry · 2011Article
- Stable knockdown of S100A4 suppresses cell migration and metastasis of osteosarcoma.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2011Article
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- The role of the basal stem cell of the human breast in normal development and cancer.Advances in experimental medicine and biology · 2011Review
- Modulation of quaternary structure of S100 proteins by calcium ions.Biophysical chemistry · 2010Article
- S100A4 downregulates filopodia formation through increased dynamic instability.Cell adhesion & migrationArticle
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
Abstract
Elevated levels of the calcium-binding protein S100A4 promote metastasis and in carcinoma cells are associated with reduced survival of cancer patients. S100A4 interacts with target proteins that affect a number of activities associated with metastatic cells. However, it is not known how many of these interactions are required for S100A4-promoted metastasis, thus hampering the design of specific inhibitors of S100A4-induced metastasis. Intracellular S100A4 exists as a homodimer through previously identified, well conserved, predominantly hydrophobic key contacts between the subunits. Here it is shown that mutating just one key residue, phenylalanine 72, to alanine is sufficient to reduce the metastasis-promoting activity of S100A4 to 50% that of the wild type protein, and just 2 or 3 specific mutations reduces the metastasis-promoting activity of S100A4 to less than 20% that of the wild type protein. These mutations inhibit the self-association of S100A4 in vivo and reduce markedly the affinity of S100A4 for at least two of its protein targets, a recombinant fragment of non-muscle myosin heavy chain isoform A, and p53. Inhibition of the self-association of S100 proteins might be a novel means of inhibiting their metastasis-promoting activities.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.