Glycosaminoglycan affinity of the complete fibroblast growth factor family

Asada, Masahiro; Shinomiya, Michiyo; Suzuki, Masashi; Honda, Emi; Sugimoto, Rika; Ikekita, Masahiko; Imamura, Toru

doi:10.1016/j.bbagen.2008.09.001

Cited by 104 publications

(98 citation statements)

References 48 publications

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“…35,36) Our results show that CS induces MAPK pathways that may be casually linked to injury and proliferation of specific cell types. In previous reports, GAGs containing CS interact with the FGF family 37) and controlled the release of FGF. 38) CS interacts with dermal fibroblasts and has a potential role in wound healing, such as cell adhesion, proliferation and matrix deposition.…”

Section: Discussionmentioning

confidence: 99%

Isolation and Characterization of Chondroitin Sulfates from Sturgeon (<i>Acipenser sinensis</i>) and Their Effects on Growth of Fibroblasts

Park

Kim

2010

Biological & Pharmaceutical Bulletin

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Chondroitin sulfate (CS) is a glycosaminoglycan that composed of hexosamine (D-galactosamine) and hexuronic acid (D-glucuronic acid) unit arranged in an alternating unbranched sequence. CS is an essential component of the extracellular matrix (ECM) of connective tissue. It is mainly covalently attached to core proteins in the form of proteoglycans so that it exhibits specific interactions with proteins for cell growth, differentiation, division and migration. In this study, CSs were purified from the cartilage and backbone of sturgeon (Acipenser sinensis). To characterize their biochemical properties, we performed disaccharide compositional analysis after chondroitinase ABC digestion, high performance size exclusion chromatography (HPSEC) and 1 H-NMR spectroscopy. We also investigated the effects of CSs on fibroblast proliferation and adhesion to determine whether wound healing was accelerated in vitro and proliferation of different mitogen-activated protein kinases (MAPK) signaling pathways was facilitated. The CS purified from sturgeon cartilage was primarily composed of 4-sulfated CS (88.8%) and sturgeon backbone CS contains more than 60% 6-sulfated CS. The average molecular weights of CSs obtained from sturgeon cartilage and backbone were found to be 8 and 43 kDa, respectively. Our results showed that both CSs are able to increase cell adhesion, induce proliferation and migration on fibroblasts and may accelerate wound healing by inducing MAPK signaling pathways.

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Section: Discussionmentioning

confidence: 99%

Isolation and Characterization of Chondroitin Sulfates from Sturgeon (<i>Acipenser sinensis</i>) and Their Effects on Growth of Fibroblasts

Park

Kim

2010

Biological & Pharmaceutical Bulletin

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“…Recombinant human FGF12B without any tags was purchased from R&D Systems (Minneapolis, MN). Recombinant human FGF12A linked to a 3xFLAG-His 6 tag was produced using the same procedure as described previously (32). Recombinant human FGF1 without any tags was produced as described previously (9).…”

Section: Methodsmentioning

confidence: 99%

“…Human recombinant FGF12 was labeled with Alexa Fluor 568. FGF12B (R&D) had no tags, whereas FGF12A was linked to a 3xFLAG-His 6 tag as described previously (32). A rat intestinal epithelial cell line, IEC6, was cultured in complete medium with Alexa Fluor 568-labeled FGF12 A, IEC6 cells were incubated with FGF12B at a dose of 10, 100, or 1000 ng/ml for 24 h. They were harvested in trypsin-EDTA, washed twice with phosphate-buffered saline (PBS) containing 0.2% bovine serum albumin (BSA), and subjected to FACS Calibur flow cytometry to estimate fluorescence intensity.…”

Section: Externally Added Fgf12 Inhibits Radiation-induced Apoptosis mentioning

confidence: 99%

Fibroblast Growth Factor-12 (FGF12) Translocation into Intestinal Epithelial Cells Is Dependent on a Novel Cell-penetrating Peptide Domain

Nakayama¹,

Yasuda²,

Umeda³

et al. 2011

Journal of Biological Chemistry

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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 ϳ10 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.

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“…The conserved core region is flanked by divergent N and C termini, which play a critical role in conferring distinct biological activity on FGFs (3,8). All FGFs interact with pericellular heparan sulfate (HS) glycosaminoglycans, albeit with different affinities (30). The HS-binding site of FGFs is comprised of the ␤1-␤2 loop and the region between ␤10 and ␤12 strands (3).…”

Section: (Fgf23)mentioning

confidence: 99%

Conversion of a Paracrine Fibroblast Growth Factor into an Endocrine Fibroblast Growth Factor

Goetz

Ohnishi

Kir

et al. 2012

Journal of Biological Chemistry

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Glycosaminoglycan affinity of the complete fibroblast growth factor family

Cited by 104 publications

References 48 publications

Isolation and Characterization of Chondroitin Sulfates from Sturgeon (<i>Acipenser sinensis</i>) and Their Effects on Growth of Fibroblasts

Isolation and Characterization of Chondroitin Sulfates from Sturgeon (<i>Acipenser sinensis</i>) and Their Effects on Growth of Fibroblasts

Fibroblast Growth Factor-12 (FGF12) Translocation into Intestinal Epithelial Cells Is Dependent on a Novel Cell-penetrating Peptide Domain

Conversion of a Paracrine Fibroblast Growth Factor into an Endocrine Fibroblast Growth Factor

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