Evidence map›Paper›PMID 21518765›Full record

ArticleThe Journal of biological chemistry2011

Fibroblast growth factor-12 (FGF12) translocation into intestinal epithelial cells is dependent on a novel cell-penetrating peptide domain: involvement of internalization in the in vivo role of exogenous FGF12.

Fumiaki Nakayama, Takeshi Yasuda, Sachiko Umeda, Masahiro Asada, Toru Imamura, Viktor Meineke, Makoto Akashi

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

29 citing papers in PubMed, 77 citations in OpenAlex.

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  8. Development of a peptide drug restoring AMPK and adipose tissue functionality in cancer cachexia.Molecular therapy : the journal of the American Society of Gene Therapy · 2023
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  19. RNAi therapeutic strategies for acute respiratory distress syndrome.Translational research : the journal of laboratory and clinical medicine · 2019
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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 at 3 institutions in 2 countries.

Fumiaki NakayamaDepartment of Radiation Emergency Medicine, National Institute of Radiological Sciences, Inage-ku, Chiba 263-8555, Japan. f_naka@nirs.go.jp
Takeshi Yasuda
Sachiko Umeda
Masahiro Asada
Toru Imamura
Viktor Meineke
Makoto Akashi
National Institute of Advanced Industrial Science and Technology · JPNational Institute of Japanese Literature · JPUniversität Ulm · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The extracellular effect of fibroblast growth factor-12 (FGF12) remains unknown because FGF12 cannot activate any fibroblast growth factor receptors (FGFRs), and FGF12 is not currently thought to be released from cells. We reported previously that FGF12 plays an intracellular role in the inhibition of radiation-induced apoptosis. In this study, we demonstrated that recombinant FGF12 was able to be internalized into the cytoplasm of a rat intestinal epithelial cell line, IEC6, and this process was dependent on two novel cell-penetrating peptide (CPP) domains (CPP-M and CPP-C). In particular, CPP-C, composed of ∼10 amino acids, was identified as a specific domain of FGF12 and its subfamily in the C-terminal region (residues 140-149), although CPP-M was a common domain in the internal region of the FGF family. The absence of CPP-C from FGF12 or a mutation (E142L) in the CPP-C domain drastically reduced the internalization of FGF12 into cells. Therefore, CPP-C played an essential role in the internalization of FGF12. In addition, CPP-C was able to deliver other polypeptides into cells as a CPP because an FGF1/CPP-C chimeric protein was internalized into IEC6 cells more efficiently than wild-type FGF1. Finally, intraperitoneally added FGF12 inhibited radiation-induced apoptosis in the intestinal epithelial cells of BALB/c mice, and deletion of the CPP-C domain decreased the inhibition of the apoptosis. These findings suggest that exogenous FGF12 can play a role in tissues by translocating into cells through the plasma membrane, and the availability of this novel CPP provides a new tool for the intracellular delivery of bioactive molecules.

Indexed as

Amino Acid SequenceAnimalsApoptosisCell LineCell-Penetrating PeptidesCytoplasmExtracellular SpaceFibroblast Growth FactorsHumansIntestinal MucosaMaleMiceMolecular Sequence DataMutagenesis, Site-DirectedMutationProtein Structure, TertiaryCell-Penetrating PeptidesFGF12 protein, humanFibroblast Growth Factors

Identifiers

PMID21518765
PMCPMC3138292
OpenAlexW2079014348

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.