The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
Regulation of Cell Migration by the Calcium-dependent Protease Calpain
Open accessAbstract
Integrin receptors play an important role during cell migration by mediating linkages and transmitting forces between the extracellular matrix and the actin cytoskeleton. The mechanisms by which these linkages are regulated and released during migration are not well understood. We show here that cell-permeable inhibitors of the calcium-dependent protease calpain inhibit both beta1 and beta3 integrin-mediated cell migration. Calpain inhibition specifically stabilizes peripheral focal adhesions, increases adhesiveness, and decreases the rate of cell detachment. Furthermore, these inhibitors alter the fate of integrin receptors at the rear of the cell during migration. A Chinese hamster ovary cell line expressing low levels of calpain I also shows reduced migration rates with similar morphological changes, further implicating calpain in this process. Taken together, the data suggest that calpain inhibition modulates cell migration by stabilizing cytoskeletal linkages and decreasing the rate of retraction of the cell's rear. Inhibiting calpain-mediated proteolysis may therefore be a potential therapeutic approach to control pathological cell migration such as tumor metastasis.
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“TBS, in addition to its actions on kinases, causes the breakdown of actin crosslinking proteins in the subsynaptic cytoskeleton; the relevant proteases also cleave transmembrane adhesion receptors that play a critical role in LTP-related actin polymerization (40–42).”
From Synaptic evidence for the efficacy of spaced learning (2012) · cites this paper as [42]
In the citing paper
“TBS, in addition to its actions on kinases, causes the breakdown of actin crosslinking proteins in the subsynaptic cytoskeleton; the relevant proteases also cleave transmembrane adhesion receptors that play a critical role in LTP-related actin polymerization (40–42).”
From Synaptic evidence for the efficacy of spaced learning (2012) · cites this paper as [42]
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Metadata
- Authors
- Huttenlocher, A., Palecek, S. P., Lu, Q., Zhang, W., Mellgren, R. L., Lauffenburger, D. A., Ginsberg, M. H., & Horwitz, A. F.
- Affiliations
- Massachusetts Institute of Technology (US)
- University of Toledo Medical Center (US)
- Scripps Research Institute (US)
- University of Illinois Urbana-Champaign (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-12
- Volume
- 272
- Issue
- 52
- Pages
- 32719-32722
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2099253537
- Cited by
- 390
- References
- 22
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 4 · 2023: 4 · 2022: 5 · 2021: 7 · 2020: 5 · 2019: 3 · 2018: 9 · 2017: 7 · 2016: 5 · 2015: 9 · 2014: 7 · 2013: 20 · 2012: 19
- FWCI
- 5.94
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Calpain Protease Function and Regulation
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- calpain, cell migration, beta1 integrin, CD61, focal adhesions, integrin-mediated adhesion, cell retraction, actin cytoskeleton, extracellular matrix, calpain inhibitors, calpain-1, metastasis, cell detachment
- MeSH terms
- Animals, Calpain, Cell Movement, Cricetinae, Platelet Membrane Glycoproteins, Antigens, CD, CHO Cells, Integrin beta1, Integrin beta3
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