Evidence map›Paper›PMID 27965915›Full record

ArticleBioResearch open access2016

Mixed Fibronectin-Derived Peptides Conjugated to a Chitosan Matrix Effectively Promotes Biological Activities through Integrins, α4β1, α5β1, αvβ3, and Syndecan.

Kentaro Hozumi, Kyotaro Nakamura, Haruna Hori, Mari Miyagi, Rika Nagao, Keiko Takasaki, Fumihiko Katagiri, Yamato Kikkawa, Motoyoshi Nomizu

Open access · diamondAbstract read
In one paragraph

Article in BioResearch open access, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. 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

9 authors at 1 institution in 1 country.

Kentaro HozumiLaboratory of Clinical Biochemistry, Department of Pharmacy, Tokyo University of Pharmacy and Life Sciences , Hachioji, Tokyo, Japan .
Kyotaro NakamuraLaboratory of Clinical Biochemistry, Department of Pharmacy, Tokyo University of Pharmacy and Life Sciences , Hachioji, Tokyo, Japan .
Haruna HoriLaboratory of Clinical Biochemistry, Department of Pharmacy, Tokyo University of Pharmacy and Life Sciences , Hachioji, Tokyo, Japan .
Mari MiyagiLaboratory of Clinical Biochemistry, Department of Pharmacy, Tokyo University of Pharmacy and Life Sciences , Hachioji, Tokyo, Japan .
Rika NagaoLaboratory of Clinical Biochemistry, Department of Pharmacy, Tokyo University of Pharmacy and Life Sciences , Hachioji, Tokyo, Japan .
Keiko TakasakiLaboratory of Clinical Biochemistry, Department of Pharmacy, Tokyo University of Pharmacy and Life Sciences , Hachioji, Tokyo, Japan .
Fumihiko KatagiriLaboratory of Clinical Biochemistry, Department of Pharmacy, Tokyo University of Pharmacy and Life Sciences , Hachioji, Tokyo, Japan .
Yamato KikkawaLaboratory of Clinical Biochemistry, Department of Pharmacy, Tokyo University of Pharmacy and Life Sciences , Hachioji, Tokyo, Japan .
Motoyoshi NomizuLaboratory of Clinical Biochemistry, Department of Pharmacy, Tokyo University of Pharmacy and Life Sciences , Hachioji, Tokyo, Japan .
Tokyo University of Pharmacy and Life Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mimicking the biological function of the extracellular matrix is an approach to developing cell adhesive biomaterials. The RGD peptide, derived from fibronectin (Fn), mainly binds to integrin αvβ3 and has been widely used as a cell adhesive peptide on various biomaterials. However, cell adhesion to Fn is thought to be mediated by several integrin subtypes and syndecans. In this study, we synthesized an RGD-containing peptide (FIB1) and four integrin α4β1-binding-related motif-containing peptides (LDV, IDAPS, KLDAPT, and PRARI) and constructed peptide-chitosan matrices. The FIB1-chitosan matrix promoted human dermal fibroblast (HDF) attachment, and the C-terminal elongated PRARI (ePRARI-C)-conjugated chitosan matrix significantly promoted HDF attachment through integrin α4β1 and syndecan binding. Next, we constructed a mixed ePRARI-C- and FIB1-chitosan matrix to develop a Fn mimetic biomaterial. The mixed ePRARI-C/FIB1-chitosan matrix promoted significantly better cell attachment and neurite outgrowth compared to those of either ePRARI-C- or FIB1-chitosan matrices. HDF adhesion to the ePRARI-C/FIB1-chitosan matrix was mediated by integrin, α4β1, α5β1, and αvβ3, similar to HDF adhesion to Fn. These data suggest that an ePRARI-C/FIB1-chitosan matrix can be used as a tool to analyze the multiple functions of Fn and can serve as a Fn-mimetic biomaterial.

Indexed as

artificial extracellular matrixcell adhesive peptidechitosanfibronectinintegrin

Identifiers

PMID27965915
PMCPMC5144869
OpenAlexW2559741424

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.