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Cited by 93Proteoglycans and glycosaminoglycans researchFibroblast Growth Factor ResearchPolymer Surface Interaction Studies

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Comparison of the Interactions of Different Growth Factors and Glycosaminoglycans

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Zhang, Fuming, Zheng, Lanhong, Cheng, Shuihong, Peng, Yanfei, Fu, Li, Zhang, Xing, Linhardt, Robert·2019·Molecules
DOI 10.3390/molecules24183360PMC PMC6767211
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Abstract

Most growth factors are naturally occurring proteins, which are signaling molecules implicated in cellular multiple functions such as proliferation, migration and differentiation under patho/physiological conditions by interacting with cell surface receptors and other ligands in the extracellular microenvironment. Many of the growth factors are heparin-binding proteins (HBPs) that have a high affinity for cell surface heparan sulfate proteoglycans (HSPG). In the present study, we report the binding kinetics and affinity of heparin interacting with different growth factors, including fibroblast growth factor (FGF) 2,7,10, hepatocyte growth factor (HGF) and transforming growth factor (TGF β-1), using a heparin chip. Surface plasmon resonance studies revealed that all the tested growth factors bind to heparin with high affinity (with KD ranging from ~0.1 to 59 nM) and all the interactions are oligosaccharide size dependent except those involving TGF β-1. These heparin-binding growth factors also interact with other glycosaminoglycans (GAGs), as well as various chemically modified heparins. Other GAGs, including heparan sulfate, chondroitin sulfates A, B, C, D, E and keratan sulfate, showed different inhibition activities for the growth factor-heparin interactions. FGF2, FGF7, FGF10 and HGF bind heparin but the 2-O-sulfo and 6-O-sulfo groups on heparin have less impact on these interactions than do the N-sulfo groups. All the three sulfo groups (N-, 2-O and 6-O) on heparin are important for TGFβ-1-heparin interaction.

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  • GAGs are important growth factor reservoirs.

    “while also being important growth factor reservoirs [160].”

    From Immune Response to Extracellular Matrix Bioscaffolds: A Comprehensive Review (2025) · cites this paper as [160]

    The Introduction (no page provided) says many growth factors interact with GAGs, and the Discussion reports their binding preferences. These passages support the idea that GAGs bind growth factors, but they do not establish that GAGs store them or act as reservoirs. (LLM, conf=0.82)

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Research works printed but not linked: 40

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Metadata

Authors
Zhang, F., Zheng, L., Cheng, S., Peng, Y., Fu, L., Zhang, X., & Linhardt, R.
Affiliations
  • Rensselaer Polytechnic Institute (US)
  • Nanjing Normal University (CN)
Corresponding author
  • Zhang, Fuming
  • Linhardt, Robert
ORCID
Venue
Molecules
Publisher
MDPI AG
Published
2019-09-16
Volume
24
Issue
18
Pages
3360
ISSN
1420-3049 (ISSN-L)
DOI
10.3390/molecules24183360
PMC
PMC6767211
OpenAlex
W2973215277
Cited by
93
References
45
Citations by year
2026: 8 · 2025: 16 · 2024: 12 · 2023: 9 · 2022: 19 · 2021: 15 · 2020: 13 · 2019: 1
FWCI
6.35
Type
journal article
Language
en
Open access
Licence
Locations
  • Molecules (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
National Institutes of Health (DK111958, CA231074, HL125371, NS088496, AG062344)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fibroblast Growth Factor Research
  • Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
Keywords
heparin-binding protein, heparan sulfate proteoglycans, glycosaminoglycans, fibroblast growth factor, hepatocyte growth factor, TGF-β1, binding affinity, binding kinetics, chondroitin sulfate, keratan sulfate
MeSH terms
Glycosaminoglycans, Heparin, Kinetics, Oligosaccharides, Protein Binding, Molecular Structure, Surface Plasmon Resonance, Intercellular Signaling Peptides and Proteins

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