Cited by 390Calpain Protease Function and RegulationCell Adhesion Molecules ResearchCellular Mechanics and Interactions

Regulation of Cell Migration by the Calcium-dependent Protease Calpain

Open access
Huttenlocher, Anna, Palecek, Sean P., Lu, Qin, Zhang, Wenli, Mellgren, Ronald L., Lauffenburger, Douglas A., Ginsberg, Mark H., Horwitz, Alan F.·1997·Journal of Biological Chemistry

Abstract

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.

Integrity signals

Registry

Crossref · 10.1074/jbc.272.52.32719

Cites

22 of 22 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • TBS causes the breakdown of actin crosslinking proteins in the subsynaptic cytoskeleton.

    “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]

  • The relevant proteases cleave transmembrane adhesion receptors that play a critical role in LTP-related actin polymerization.

    “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]

Cites

Flagged first, then by citations

Cited by

Sorted by citations

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
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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review