Evidence map›Paper›PMID 23558678›Full record

ArticleThe Journal of biological chemistry2013

Annexin A2 regulates β1 integrin internalization and intestinal epithelial cell migration.

Carl R Rankin, Roland S Hilgarth, Giovanna Leoni, Mike Kwon, Kyle A Den Beste, Charles A Parkos, Asma Nusrat

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

37 citing papers in PubMed.

  1. Review
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  12. Article
  13. Annexin A2 in Fibrinolysis, Inflammation and Fibrosis.International journal of molecular sciences · 2021
    Review
  14. Review
  15. Article
  16. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Carl R RankinDepartment of Pathology and Laboratory Medicine, Epithelial Pathobiology and Mucosal Inflammation Research Unit, Emory University, Atlanta, Georgia 30306, USA.
Roland S Hilgarth
Giovanna Leoni
Mike Kwon
Kyle A Den Beste
Charles A Parkos
Asma Nusrat

Funding

Regulation of intestinal epithelial barrier function by intercellular junction proteins in health and diseaseR01DK059888 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ASMA NUSRAT · 2001 to 2026
$10.5M
Intestinal Mucosal Wound Resealing in IBDR01DK055679 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ASMA NUSRAT · 2004 to 2026
$8.1M
Intestinal Inflammation: Signaling proteins and the rate of PMN transmigrationR01DK079392 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PARKOS, CHARLES A · 2007 to 2025
$7.2M
Neutrophil Interactions with Intestinal Epithelial CellsR01DK072564 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PARKOS, CHARLES A · 2005 to 2020
$6.5M
Structure-Function Studies on Intestinal Epithelial JAMR01DK061379 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PARKOS, CHARLES A · 2002 to 2021
$6.3M
Emory Epithelial Pathobiology Research Development CenterR24DK064399 · NIDDK · EMORY UNIVERSITY · PI PARKOS, CHARLES A · 2003 to 2012
$5.3M
NIDDK NIH HHS DK059888NIDDK NIH HHS R01 DK055679NIDDK NIH HHS R01 DK059888NIDDK NIH HHS R01 DK061379NIDDK NIH HHS R01 DK072564NIDDK NIH HHS R01 DK079392NIDDK NIH HHS R24 DK064399
6 · The paper itself

Abstract

The gastrointestinal epithelium functions as an important barrier that separates luminal contents from the underlying tissue compartment and is vital in maintaining mucosal homeostasis. Mucosal wounds in inflammatory disorders compromise the critical epithelial barrier. In response to injury, intestinal epithelial cells (IECs) rapidly migrate to reseal wounds. We have previously observed that a membrane-associated, actin binding protein, annexin A2 (AnxA2), is up-regulated in migrating IECs and plays an important role in promoting wound closure. To identify the mechanisms by which AnxA2 promotes IEC movement and wound closure, we used a loss of function approach. AnxA2-specific shRNA was utilized to generate IECs with stable down-regulation of AnxA2. Loss of AnxA2 inhibited IEC migration while promoting enhanced cell-matrix adhesion. These functional effects were associated with increased levels of β1 integrin protein, which is reported to play an important role in mediating the cell-matrix adhesive properties of epithelial cells. Because cell migration requires dynamic turnover of integrin-based adhesions, we tested whether AnxA2 modulates internalization of cell surface β1 integrin required for forward cell movement. Indeed, pulse-chase biotinylation experiments in IECs lacking AnxA2 demonstrated a significant increase in cell surface β1 integrin that was accompanied by decreased β1 integrin internalization and degradation. These findings support an important role of AnxA2 in controlling dynamics of β1 integrin at the cell surface that in turn is required for the active turnover of cell-matrix associations, cell migration, and wound closure.

Indexed as

Annexin A2Caco-2 CellsCell AdhesionCell MovementEpithelial CellsExtracellular MatrixHumansIntegrin beta1Intestinal MucosaProtein TransportProteolysisWound HealingAnnexin A2ANXA2 protein, humanIntegrin beta1Annexin 2Annexin A2Cell MigrationEndocytosisIntegrinIntestinal EpitheliumWound Healingβ1 Integrin

Identifiers

PMID23558678
PMCPMC3663542

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.