Evidence map›Paper›PMID 24755217›Full record

ArticleThe Journal of biological chemistry2014

The novel α4B murine α4 integrin protein splicing variant inhibits α4 protein-dependent cell adhesion.

Hitomi Kouro, Shigeyuki Kon, Naoki Matsumoto, Tomoe Miyashita, Ayaka Kakuchi, Dai Ashitomi, Kodai Saitoh, Takuya Nakatsuru, Sumihito Togi, Ryuta Muromoto and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.7field-weighted citation impact, top 31% of its field
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

1 citing paper in PubMed, 6 citations in OpenAlex.

  1. Alternative RNA structure-coupled gene regulations in tumorigenesis.International journal of molecular sciences · 2014
    Review
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

11 authors at 1 institution in 1 country.

Hitomi KouroFrom the Department of Immunology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-Ku, Sapporo, 060-0812, Japan.
Shigeyuki KonFrom the Department of Immunology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-Ku, Sapporo, 060-0812, Japan kon@pharm.hokudai.ac.jp.
Naoki MatsumotoFrom the Department of Immunology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-Ku, Sapporo, 060-0812, Japan.
Tomoe MiyashitaFrom the Department of Immunology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-Ku, Sapporo, 060-0812, Japan.
Ayaka KakuchiFrom the Department of Immunology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-Ku, Sapporo, 060-0812, Japan.
Dai AshitomiFrom the Department of Immunology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-Ku, Sapporo, 060-0812, Japan.
Kodai SaitohFrom the Department of Immunology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-Ku, Sapporo, 060-0812, Japan.
Takuya NakatsuruFrom the Department of Immunology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-Ku, Sapporo, 060-0812, Japan.
Sumihito TogiFrom the Department of Immunology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-Ku, Sapporo, 060-0812, Japan.
Ryuta MuromotoFrom the Department of Immunology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-Ku, Sapporo, 060-0812, Japan.
Tadashi MatsudaFrom the Department of Immunology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12 Nishi-6, Kita-Ku, Sapporo, 060-0812, Japan tmatsuda@pharm.hokudai.ac.jp.
Hokkaido University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Integrins affect the motility of multiple cell types to control cell survival, growth, or differentiation, which are mediated by cell-cell and cell-extracellular matrix interactions. We reported previously that the α9 integrin splicing variant, SFα9, promotes WT α9 integrin-dependent adhesion. In this study, we introduced a new murine α4 integrin splicing variant, α4B, which has a novel short cytoplasmic tail. In inflamed tissues, the expression of α4B, as well as WT α4 integrin, was up-regulated. Cells expressing α4B specifically bound to VCAM-1 but not other α4 integrin ligands, such as fibronectin CS1 or osteopontin. The binding of cells expressing WT α4 integrin to α4 integrin ligands is inhibited by coexpression of α4B. Knockdown of α4B in metastatic melanoma cell lines results in a significant increase in lung metastasis. Expression levels of WT α4 integrin are unaltered by α4B, with α4B acting as a regulatory subunit for WT α4 integrin by a dominant-negative effect or inhibiting α4 integrin activation.

Indexed as

Cell AdhesionProtein SplicingAlternative SplicingAmino Acid SequenceAnimalsBase SequenceCytoplasmDNA PrimersFibronectinsIntegrin alpha4MiceNIH 3T3 CellsOsteopontinRNA, MessengerVascular Cell Adhesion Molecule-1DNA PrimersFibronectinsIntegrin alpha4OsteopontinRNA, MessengerVascular Cell Adhesion Molecule-1Alternative SplicingCell AdhesionExtracellular MatrixIntegrinsTumor Metastases

Identifiers

PMID24755217
PMCPMC4047406
OpenAlexW2092636778

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.