ArticleThe Journal of biological chemistry2011
Maspin, the molecular bridge between the plasminogen activator system and beta1 integrin that facilitates cell adhesion.
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 17 papers, 1 of them a synthesis that pooled it.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 1 synthesis or guideline pooled it, 34 citations in OpenAlex.
- A clinical-pathogenetic approach on associated anomalies and chromosomal defects supports novel candidate critical regions and genes for gastroschisis.Pediatric surgery international · 2018Pooled it
- Serpin B5 as a Potential Biomarker for the Diagnosis and Prognosis of Oral Squamous Cell Carcinoma.Cureus · 2026Article
- Fibrinolysis-unrelated functions of the plasminogen/plasmin system: A gateway to successful parasitism?Current research in parasitology & vector-borne diseases · 2026Review
- Early host-parasite interaction models reveal a key role for fibrinolysis in Fasciola hepatica intestinal migration.Parasites & vectors · 2025Article
- Maspin/SerpinB5 is a cytoskeleton-binding protein that regulates epithelial cell shape.Communications biology · 2025Article
- Prognostic value of Maspin protein level in patients with triple negative breast cancer.Scientific reports · 2024Article
- A meta‑ and bioinformatics analysis of maspin expression levels influencing the prognosis of patients with breast cancer.Oncology letters · 2024Article
- The roles of maspin expression in gastric cancer: a meta- and bioinformatics analysis.Oncotarget · 2017Article
- The Opportunity of Precision Medicine for Breast Cancer With Context-Sensitive Tumor Suppressor Maspin.Journal of cellular biochemistry · 2017Review
- Self-assembling peptide-based building blocks in medical applications.Advanced drug delivery reviews · 2017Review
- Methylation-induced silencing of maspin contributes to the proliferation of human glioma cells.Oncology reports · 2016Article
- Supramolecular assembly of multifunctional maspin-mimetic nanostructures as a potent peptide-based angiogenesis inhibitor.Acta biomaterialia · 2015Article
- Internalization by multiple endocytic pathways and lysosomal processing impact maspin-based therapeutics.Molecular cancer research : MCR · 2014Article
- Tumor-suppressive maspin functions as a reactive oxygen species scavenger: importance of cysteine residues.The Journal of biological chemistry · 2013Article
- Identification of an intrinsic determinant critical for maspin subcellular localization and function.PloS one · 2013Article
- Tyrosine phosphorylation plays a role in increasing maspin protein levels and its cytoplasmic accumulation.FEBS open bio · 2012Article
- Maspin reprograms the gene expression profile of prostate carcinoma cells for differentiation.Genes & cancer · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Maspin is a non-inhibitory serine protease inhibitor (serpin) that influences many cellular functions including adhesion, migration, and invasion. The underlying molecular mechanisms that facilitate these actions are still being elucidated. In this study we determined the mechanism by which maspin mediates increased MCF10A cell adhesion. Utilizing competition peptides and mutation analyses, we discovered two unique regions (amino acid residues 190-202 and 260-275) involved in facilitating the increased adhesion function of maspin. In addition, we demonstrate that the urokinase-type plasminogen activator (uPA)/uPA receptor (uPAR) complex is required for the localization and adhesion function of maspin. Finally, we showed that maspin, uPAR, and β1 integrin co-immunoprecipitate, suggesting a novel maspin-uPA-uPAR-β1 integrin mega-complex that regulates mammary epithelial cell adhesion.
Indexed as
Identifiers
What OpenQuestion holds
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.