ArticleThe Journal of biological chemistry2010
Maspin (SERPINB5) is an obligate intracellular serpin.
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 23 papers.
What it found
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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
23 citing papers in PubMed, 54 citations in OpenAlex.
- Serpin peptidase inhibitor (SERPINB5) haplotypes are associated with susceptibility to hepatocellular carcinoma.Scientific reports · 2016Trial
- BioMark: biomarker analysis tool.BMC bioinformatics · 2026Article
- Maspin/SerpinB5 is a cytoskeleton-binding protein that regulates epithelial cell shape.Communications biology · 2025Article
- Inhibition of the SERPINB5/HSP90AA1 axis restrains the proliferation and invasion of rectal cancer.World journal of gastroenterology · 2025Article
- Role of class I histone deacetylases in the regulation of maspin expression in prostate cancer.Molecular carcinogenesis · 2020Article
- Maspin suppresses cell invasion and migration in gastric cancer through inhibiting EMT and angiogenesis via ITGB1/FAK pathway.Human cell · 2020Article
- Article
- Cervicovaginal microbiome dysbiosis is associated with proteome changes related to alterations of the cervicovaginal mucosal barrier.Mucosal immunology · 2016Article
- Low spinophilin expression enhances aggressive biological behavior of breast cancer.Oncotarget · 2015Article
- The aggregation-prone intracellular serpin SRP-2 fails to transit the ER in Caenorhabditis elegans.Genetics · 2015Article
- Cytoplasmic maspin expression predicts poor prognosis of patients with soft tissue sarcomas.Diagnostic pathology · 2014Article
- Proteolytic histone modification by mast cell tryptase, a serglycin proteoglycan-dependent secretory granule protease.The Journal of biological chemistry · 2014Article
- Maspin is not required for embryonic development or tumour suppression.Nature communications · 2014Article
- Glucose-regulated protein 78 mediates hormone-independent prostate cancer progression and metastasis through maspin and COX-2 expression.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014Article
- Role of maspin in cancer.Clinical and translational medicine · 2013Article
- Identification of an intrinsic determinant critical for maspin subcellular localization and function.PloS one · 2013Article
- A versatile monoclonal antibody specific to human SERPINB5.Hybridoma (2005) · 2012Article
- Maspin increases extracellular plasminogen activator activity associated with corneal fibroblasts and myofibroblasts.Experimental eye research · 2011Article
- Maspin, the molecular bridge between the plasminogen activator system and beta1 integrin that facilitates cell adhesion.The Journal of biological chemistry · 2011Article
- Identification of phosphorylation sites on extracellular corneal epithelial cell maspin.Proteomics · 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
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Maspin (SERPINB5) is a tumor suppressor lost in breast and prostate cancer whose molecular function is unknown. It is a non-inhibitory member of the clade B serpins suggested to play a role in a plethora of intracellular and extracellular settings, yet its normal cellular distribution has never been clarified. Here we investigate the distribution of maspin in non-transformed human epithelial cells. By indirect immunofluorescence, maspin has a nucleocytoplasmic distribution in breast (MCF10A) and prostate (RWPE-1) cells and, by immunoblotting and pulse-chase analyses, is neither glycosylated nor secreted. Cell surface biotinylation studies also show that maspin is not present at the cell surface. Differentiation of MCF10A cells into three-dimensional acini results in the redistribution of maspin from the nucleus to the cytoplasm but does not result in secretion. Addition of an efficient conventional signal peptide to maspin directs it into the secretory pathway and results in glycosylation but not secretion. We further show that maspin in the cytoplasm of MCF10A cells is a soluble monomeric protein that is not detectably associated with the cytoskeleton or other extractable components. Taken together, these results suggest that maspin is restricted to an intracellular, possibly nuclear, role in which it influences cell-matrix interactions indirectly. It is probably released only as a consequence of cell damage or necrosis.
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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.