Evidence map›Paper›PMID 26731578›Full record

ArticleBiomaterials2016

Fibroblast growth factor 2 dimer with superagonist in vitro activity improves granulation tissue formation during wound healing.

Caitlin G Decker, Yu Wang, Samantha J Paluck, Lu Shen, Joseph A Loo, Alex J Levine, Lloyd S Miller, Heather D Maynard

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

Article in Biomaterials, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
5.1field-weighted citation impact, top 5% 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

27 citing papers in PubMed, 78 citations in OpenAlex.

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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

8 authors at 4 institutions in 1 country.

Caitlin G DeckerDepartment of Chemistry and Biochemistry and California NanoSystems Institute, University of California, Los Angeles, 607 Charles E. Young Drive South, Los Angeles, CA 90095-1569, United States.
Yu WangDepartment of Dermatology, Johns Hopkins University School of Medicine, 1550 Orleans St., Baltimore, MD 21231, United States.
Samantha J PaluckDepartment of Chemistry and Biochemistry and California NanoSystems Institute, University of California, Los Angeles, 607 Charles E. Young Drive South, Los Angeles, CA 90095-1569, United States.
Lu ShenDepartment of Chemistry and Biochemistry and California NanoSystems Institute, University of California, Los Angeles, 607 Charles E. Young Drive South, Los Angeles, CA 90095-1569, United States.
Joseph A LooDepartment of Chemistry and Biochemistry and California NanoSystems Institute, University of California, Los Angeles, 607 Charles E. Young Drive South, Los Angeles, CA 90095-1569, United States; Department of Biological Chemistry, David Geffen School of Medicine, and UCLA/DOE Institute of Genomics and Proteomics, University of California, Los Angeles, CA 90095, United States.
Alex J LevineDepartment of Chemistry and Biochemistry and California NanoSystems Institute, University of California, Los Angeles, 607 Charles E. Young Drive South, Los Angeles, CA 90095-1569, United States; Department of Physics and Astronomy, University of California, Los Angeles, CA 90095-1569, United States; Department of Biomathematics, University of California, Los Angeles, CA 90095-1569, United States.
Lloyd S MillerDepartment of Dermatology, Johns Hopkins University School of Medicine, 1550 Orleans St., Baltimore, MD 21231, United States.
Heather D MaynardDepartment of Chemistry and Biochemistry and California NanoSystems Institute, University of California, Los Angeles, 607 Charles E. Young Drive South, Los Angeles, CA 90095-1569, United States. Electronic address: maynard@chem.ucla.edu.
University of California, Los Angeles · USCalifornia NanoSystems Institute · USJohns Hopkins Medicine · USJohns Hopkins University · US

Funding

CHEMISTRY BIOLOGY INTERFACE TRAINING PROGRAMT32GM008496 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MAYNARD, HEATHER D · 1993 to 2019
$6.3M
UV Laser for Photodissociation-Mass Spectrometry of Proteins and Protein ComplexesR01GM103479 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LOO, JOSEPH A · 2012 to 2021
$3.2M
Stable and Active bFGF-Polymer Conjugates for Wound HealingR01EB013674 · NIBIB · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MAYNARD, HEATHER D · 2012 to 2015
$1.3M
STAT3 and IL-17-Th17 in skin immunity to MRSAR56AR065804 · NIAMS · JOHNS HOPKINS UNIVERSITY · PI MILLER, LLOYD S · 2014 to 2014
$356k
NIAMS NIH HHS R56AR065804NIBIB NIH HHS R01 EB013674NIBIB NIH HHS R01EB013674NIGMS NIH HHS R01 GM103479NIGMS NIH HHS R01GM103479NIGMS NIH HHS T32 GM 008496NIGMS NIH HHS T32 GM008496
6 · The paper itself

Abstract

Site-specific chemical dimerization of fibroblast growth factor 2 (FGF2) with the optimal linker length resulted in a FGF2 homodimer with improved granulation tissue formation and blood vessel formation at exceptionally low concentrations. Homodimers of FGF2 were synthesized through site-specific linkages to both ends of different molecular weight poly(ethylene glycols) (PEGs). The optimal linker length was determined by screening dimer-induced metabolic activity of human dermal fibroblasts and found to be that closest to the inter-cysteine distance, 70 Å, corresponding to 2 kDa PEG. A straightforward analysis of the kinetics of second ligand binding as a function of tether length showed that, as the polymerization index (the number of monomer repeat units in the polymer, N) of the tether decreases, the mean time for second ligand capture decreases as ∼N(3/2), leading to an enhancement of the number of doubly bound ligands in steady-state for a given (tethered) ligand concentration. FGF2-PEG2k-FGF2 induced greater fibroblast metabolic activity than FGF2 alone, all other dimers, and all monoconjugates, at each concentration tested, with the greatest difference observed at low (0.1 ng/mL) concentration. FGF2-PEG2k-FGF2 further exhibited superior activity compared to FGF2 for both metabolic activity and migration in human umbilical vein endothelial cells, as well as improved angiogenesis in a coculture model in vitro. Efficacy in an in vivo wound healing model was assessed in diabetic mice. FGF2-PEG2k-FGF2 increased granulation tissue and blood vessel density in the wound bed compared to FGF2. The results suggest that this rationally designed construct may be useful for improving the fibroblast matrix formation and angiogenesis in chronic wound healing.

Indexed as

Protein MultimerizationAnimalsBlood VesselsBlotting, WesternCell MovementCross-Linking ReagentsDermisDiabetes Mellitus, ExperimentalFibroblast Growth Factor 2FibroblastsGranulation TissueHuman Umbilical Vein Endothelial CellsMaleMiceNeovascularization, PhysiologicPolyethylene GlycolsCross-Linking ReagentsFibroblast Growth Factor 2Polyethylene GlycolsAngiogenesisDiabetic woundsDimerizationGrowth factorPEGylationWound healing

Identifiers

PMID26731578
PMCPMC4715972
OpenAlexW2218702703

What OpenQuestion holds

Textmetadata
LicenceTDM
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.