Cloning of mouse FGF10 and up-regulation of its gene expression during wound healing.

Tagashira, Shuzo; Harada, Hideyuki; Katsumata, Takashi; Itoh, Nobuyuki; Nakatsuka, Masashi

doi:10.1016/s0378-1119(97)00187-x

Cited by 64 publications

(51 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Studies of transgenic mice expressing FGF-7 and dominant negative KGF (FGF-7) receptor indicate that FGF-7 plays an important role in re-epithelialization during wound healing (22,23), although studies of FGF-7 null mutant mice indicate that FGF-7 is not required for wound healing (24). We observed that the induction of FGF-10 in the dermis during wound healing was larger than that of FGF-7 (25). Thus, FGF-10 is expected to play unique roles as a FGF-7-like mitogen in the lung, wound healing, and limb bud formation.…”

Section: Preparation Of Recombinant Human Fgf-10 Expressed In Ementioning

confidence: 69%

Structure and Expression of Human Fibroblast Growth Factor-10

Emoto¹,

Tagashira²,

Matteï³

et al. 1997

Journal of Biological Chemistry

Self Cite

113

View full text Add to dashboard Cite

We isolated the cDNA encoding a novel member of the human fibroblast growth factor (FGF) family from the lung. The cDNA encodes a protein of 208 amino acids with high sequence homology (95.6%) to rat FGF-10, indicating that the protein is human FGF-10. Human FGF-10 as well as rat FGF-10 has a hydrophobic amino terminus (ϳ40 amino acids), which may serve as a signal sequence. The apparent evolutionary relationships of human FGFs indicate that FGF-10 is closest to FGF-7. Chromosomal localization of the human FGF-10 gene was examined by in situ hybridization. The gene was found to map to the 5p12-p13 region. Human FGF-10 (amino acids 40 to 208 with a methionine residue at the amino terminus) was produced in Escherichia coli and purified from the cell lysate. Recombinant human FGF-10 (ϳ19 kDa) showed mitogenic activity for fetal rat keratinizing epidermal cells, but essentially no activity for NIH/3T3 cells, fibroblasts. The specificity of mitogenic activity of FGF-10 is similar to that of FGF-7 but distinct from that of bFGF. In structure and biological activity, FGF-10 is similar to FGF-7.

show abstract

Section: Preparation Of Recombinant Human Fgf-10 Expressed In Ementioning

confidence: 69%

Structure and Expression of Human Fibroblast Growth Factor-10

Emoto¹,

Tagashira²,

Matteï³

et al. 1997

Journal of Biological Chemistry

Self Cite

113

View full text Add to dashboard Cite

show abstract

“…In addition, the demonstration of high levels of KGF expression in chronic inflammatory diseases of the skin (57) and bowel (58) provide further evidence of its up-regulation in an inflammatory environment. Tagashira et al (59) reported a marked increase in mouse FGF-10 transcript levels following cutaneous wounding. In contrast, Beer et al (49) reported no induction under similar conditions, nor did these workers observe FGF-10 induction in fibroblasts following stimulation by proinflammatory mediators or serum growth factors.…”

Section: Discussionmentioning

confidence: 99%

Characterization of Recombinant Human Fibroblast Growth Factor (FGF)-10 Reveals Functional Similarities with Keratinocyte Growth Factor (FGF-7)

Igarashi

Finch

Aaronson

1998

Journal of Biological Chemistry

284

234

View full text Add to dashboard Cite

A newly identified member of the fibroblast growth factor (FGF) family, designated FGF-10, is expressed during development and preferentially in adult lung. The predicted FGF-10 protein is most related to keratinocyte growth factor (KGF, or FGF-7). The latter is unique among FGFs in that it binds and signals only through the FGF receptor (FGFR2b) isoform KGF receptor (KGFR) expressed specifically by epithelial cells. In order to examine the biological and biochemical properties of human FGF-10, we isolated the cDNA and expressed its encoded protein in bacteria. The recombinant protein (rFGF-10) was a potent mitogen for Balb/MK mouse epidermal keratinocytes with activity detectable at 0.1 nM and maximal at around 5 nM. Within this concentration range, FGF-10 did not stimulate DNA synthesis in NIH/3T3 mouse fibroblasts. rFGF-10 bound the KGFR with high affinity comparable to that of KGF, and did not bind detectably to either the FGFR1c (Flg) or FGFR2c (Bek) receptor isoforms. The mitogenic activity of FGF-10 could be distinguished from that of KGF by its different sensitivity to heparin and lack of neutralization by a KGF monoclonal antibody. These results indicate that FGF-10 and KGF have similar receptor binding properties and target cell specificities, but are differentially regulated by components of the extracellular matrix.

show abstract

“…These alternative pathways may involve other cytokines including members of the FGF family other than KGF. Of interest, FGF-10 was recently shown to be functionally similar to KGF despite limited amino acid sequence identity (44,45). Presumably, this can be accounted for by the finding that both FGF-10 and KGF interact with the same FGFR splice variant (46).…”

Section: Discussionmentioning

confidence: 99%