rhEGF Treatment Improves EGFR Inhibitor-Induced Skin Barrier and Immune Defects.

The mechanisms of epidermal growth factor (EGF) affecting EGF receptor inhibitor (EGFRI)-related skin toxicities are as yet unknown. We investigated which mechanisms are involved in EGF's positive effects. Two types of EGFRIs, cetuximab and gefitinib, were used to treat the cells or 3d-cultured human skin tissue with recombinant human EGF (rhEGF).

Potential protective effects of rhEGF against ultraviolet A irradiation-induced damages on human fibroblasts.

Background: Ultraviolet A (UVA) rays reach the dermal skin layer and generate oxidative stress, DNA damage, and cell inflammation, which in turn lead to photo-aging and photo-carcinogenesis. While there have been many studies about the beneficial effects of topical epidermal growth factor (EGF) treatment in the healing of wounds, the effect of EGF on UVA-induced skin irritation remains unknown. To clarify the effects of EGF on UVA-induced skin damage, it was investigated whether EGF signaling can affect intracellular reactive oxygen species (ROS) and DNA damages in UVA-irradiated human dermal fibroblasts.

Epidermal Growth Factor Attenuated the Expression of Inflammatory Cytokines in Human Epidermal Keratinocyte Exposed to .

Background: While the beneficial effects of topical epidermal growth factor (EGF) on wound healing have been repeatedly reported, there are few reports about the effects of EGF on inflammatory skin diseases including acne.

Objective: To clarify the effects of EGF on acne, it was investigated whether recombinant human EGF (rhEGF) signalling can affect -induced cytokine expression in human epidermal keratinocytes.

Methods: The cultured normal human epidermal keratinocytes (NHK) were co-treated with and rhEGF, and mRNA levels of interleukin (IL)-1α, IL-8 and tumor necrosis factor (TNF)-α; toll-like receptor 2 (TLR2); and nuclear factor kappa B (NF-κB) were determined.

Osteoblastic differentiation of human bone marrow stromal cells in self-assembled BMP-2 receptor-binding peptide-amphiphiles.

Self-assembled nanostructures consisting of BMP receptor-binding peptides, termed osteopromotive domains (OPDs), and hydrophobic alkyl chains were fabricated with the aim of developing three-dimensional scaffolding materials for osteoblastic differentiation. OPD peptide was identified from BMP-2 and had an affinity for BMP receptors thereby inducing differentiation of human bone marrow stromal cells into osteoblastic cells. The peptide-hydrophobic alkyl chain amphiphiles were designed to mimic nanofibrous extracellular structures and to add osteogenic ligands to enhance osteoblastic cell function.

Effect of immobilized cell-binding peptides on chitosan membranes for osteoblastic differentiation of mesenchymal stem cells.

Two cell-binding domains from FGF-2 (fibroblast growth factor-2) were shown to increase cell attachment and osteoblastic differentiation. Two synthetic peptides derived from FGF-2, namely residues 36-41 (F36; PDGRVD) and 77-83 (F77; KEDGRLL), were prepared and their N-termini further modified for ease of surface immobilization. Chitosan membranes were used in the present study as mechanical supportive biomaterials for peptide immobilization.

Synthetic peptide-coated bone mineral for enhanced osteoblastic activation in vitro and in vivo.

A 15-mer synthetic peptide, designated P1, was derived from the bone morphogenetic protein (BMP) receptor I and BMP receptor II binding domains of BMP-2 for the purpose of enhancing bone regeneration capacity of inorganic bovine bone mineral. A second peptide, denoted P2, was designed by adding seven glutamic acid residues to the N-terminal of P1 to increase the surface coating efficiency onto bone mineral. The coating efficiency of P1 increased with the concentration of peptide.

Characterization of the surface immobilized synthetic heparin binding domain derived from human fibroblast growth factor-2 and its effect on osteoblast differentiation.

Fibroblast growth factor (FGF)-2 regulates a variety of cellular functions, such as proliferation and differentiation, by binding to cell surface FGF receptors (FGFRs) in the presence of heparin proteoglycans. FGF-2 is known as a heparin-binding growth factor, but the localization of the heparin binding site has not been fully investigated until now. We used two potential heparin binding domains of FGF-2, the residues 105-111 (F105, YKRSRYT) and 119-135 (F119, KRTGQYKLGSKTGPGQK).

Injectable gel with synthetic collagen-binding peptide for enhanced osteogenesis in vitro and in vivo.

A synthetic peptide denoted as collagen-binding motif (CBM) was identified from osteopontin (OPN), a multisubunit extracellular matrix (ECM) protein, by enzymatic digestion with chymotrypsin. The aim of this study was to examine the feasibility of identified CBM peptide as an active component of gel type scaffold material in osteogenesis. The binding of CBM peptide to collagen was specific and presented high affinity.