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Microneedling
Published in Rubina Alves, Ramon Grimalt, Techniques in the Evaluation and Management of Hair Diseases, 2021
Rachita S. Dhurat, Sanober Burzin Daruwalla
The proliferative phase begins after the primary inflammatory responses to the injury. The main and leading events that happen during this phase include re-epithelialization, angiogenesis, and fibroplasia. Epidermal restoration begins with keratinocyte migration and proliferation stimulated by TGF-α, followed by neo-epithelium differentiation and basement membrane restoration. As a ligand for EGF family receptors, heparin-binding EGF-like growth factor modulates keratinocyte migration and skin wound healing [10]. Angiogenesis is primarily promoted by macrophage-released cytokines, such as TGF-β, FGF, and vascular EGF (VEGF). These factors modulate endothelial cell proliferation and promote angiogenesis [11].
The Role of Growth Factor Signaling in the Development and Treatment of Necrotizing Enterocolitis
Published in David J. Hackam, Necrotizing Enterocolitis, 2021
Rita D. Shelby, Terrence M. Rager, Barrett P. Cromeens, Gail E. Besner
Heparin-binding EGF-like growth factor (HB-EGF) is a glycoprotein first identified in the conditioned medium of cultured human macrophages (44) and a member of the EGF family (45). The HB-EGF gene is an immediate early gene induced by hypoxic and oxidative stress in response to tissue damage and resultant wound healing and tissue regeneration (46–51). It has potent mitogenic, chemoattractant, and migration-inducing effects that are mediated through activation of ErbB-1 and ErbB-4 receptors (52, 53). In addition, HB-EGF binds strongly to heparin (44). HB-EGF is found in both AF and BM, ensuring continuous exposure of fetal and newborn intestine to endogenous levels of the growth factor (54). Endogenous HB-EGF is expressed in many cell types, including intestinal epithelial cells (55, 56).
Mechanism of Action of Topical Retinoids
Published in Ayse Serap Karadag, Berna Aksoy, Lawrence Charles Parish, Retinoids in Dermatology, 2019
Sümeyre Seda Ertekin, Mehmet Salih Gurel
All-trans-retinoic acid is a naturally occurring first-generation retinoid which is normally present in the skin. The synthetic form of topical ATRA (tretinoin) has been approved by the FDA for the treatment of acne and photoaging (1). It has also been used off-label for several dermatologic conditions like pigmentary disorders, wound healing, Darier disease, verrucae plana, and actinic keratosis (20). It binds to all RAR isotypes, but not to RXRs. It normalizes follicular epithelial differentiation and keratinization. It increases mitotic activity of follicular epithelia and turnover rate of thin, loosely-adherent corneocytes. Shedding of those corneocytes from the follicle is the principal mechanism of its comedolytic activity. In addition, it has been shown to induce the expression of heparin-binding EGF-like growth factor (HB-EGF), which results in epidermal hyperplasia in atrophic photodamaged epidermis (21,22).
Attenuating influenza a virus infection by heparin binding EGF-like growth factor
Published in Growth Factors, 2020
K. M. Lai, B. H. Goh, W. L. Lee
Upon the binding of ligands, EGFR is activated and rapidly internalised via clathrin-coated pits followed by trafficking to early endosome of the cell. In early endosome, internalised receptors are either recycled to the cell surface or taken up into lysosome for degradation depending on the types of ligand bound (Roepstorff et al. 2008; Goh and Sorkin 2013). Ligand-induced endocytic down-regulation is an important mechanism for signal attenuation and prolonged stimulation of EGFR could lead to removal of the receptors from cell surface. Among eight ligands of EGFR that have been described, heparin-binding EGF-like growth factor (HB-EGF) could lead to a strong induction of internalisation followed by degradation of a large portion of the bound receptors (Roepstorff et al. 2009). This led us to ask: Can ligand-induced degradation of EGFR attenuate IAV entry in the host cells and subsequently diminish the infection?
Heparin-binding EGF-like growth factor attenuates lung inflammation and injury in a murine model of pulmonary emphysema
Published in Growth Factors, 2018
Yanwei Su, Heng Luo, Jixin Yang
Heparin-binding EGF-like growth factor (HB-EGF) was first described as a member of the epidermal growth factor (EGF) family in 1990 (Besner et al. 1990). It acts as a potent mitogenic and chemoattractant protein for many cell types, including pulmonary epithelial and endothelial cells (Cockayne et al. 2012; Leslie et al. 1997). Unlike EGF, which only binds to ErB-1 receptors, HB-EGF could simultaneously activate ErB-1, ErB-4, and NRDC receptors, thus showing more extensive biological effects than EGF (Yang et al. 2014). We have previously demonstrated that HB-EGF acts as an effective mitogen, a restitution-inducing reagent, a cellular trophic factor, and an anti-inflammatory agent in inflammatory diseases (Su et al. 2013; Su & Besner 2014; Yang et al. 2014). Other studies also revealed that HB-EGF is a mitogen for alveolar type II cells, which proliferate and differentiate into type I epithelial cells to restore the alveolar epithelium after lung injury (Leslie et al. 1997). Exogenous administration of HB-EGF could protect the lung from injury in animal models of intestinal Ischemia and Reperfusion and scald burn (James et al. 2010; Lutmer et al. 2013).
Differences in secretome in culture media when comparing blastocysts and arrested embryos using multiplex proximity assay
Published in Upsala Journal of Medical Sciences, 2018
Karin E. Lindgren, Fatma Gülen Yaldir, Julius Hreinsson, Jan Holte, Karin Kårehed, Inger Sundström-Poromaa, Helena Kaihola, Helena Åkerud
Finally, a number of proteins that we expected to detect were not identified. These proteins include heparin-binding EGF-like growth factor (HB-EGF), transforming growth factor alpha (TGF-alpha), tumour necrosis factor (TNF, formerly known as TNF-alpha), and C-X-C motif chemokine 13 (CXCL13) (17). The lack of detection of these proteins could have several explanations. Potentially, embryos that are arrested in development may discharge proteases that could degrade secreted proteins, making the comparison between blastocysts and arrested embryos more complicated.