Epimorphin was originally identified as a mesenchymal cell surface-associated protein that modulates epithelial morphogenesis in embryonic skin and lung epithelia. A previous report which utilized embryonic mouse skin, showed that epimorphin was localized non-homogeneously in a region adjacent to the epidermis and in a mesenchymal cell condensation located in front of growing hair follicles. We report herein a further detailed localization of this protein in adult mouse skin using immunoelectron microscopy. Epimorphin was found to be localized on the undersurface of basal cells, in the cytoplasm of cell processes of fibroblasts, as well as on the plasma membrane of fibroblasts, endothelial cells, pericytes, perineurium and endomysium. Our present finding indicated that epimorphin is one of the factors involved in multiple biological functions in a variety of structures derived from various origins and that it is not a specific epithelial morphogenetic factor.
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Role of syntaxin3 an apical polarity protein in poorly polarized keratinocytes: regulation of asymmetric barrier formations in the skin epidermis.
Cell Tissue Res
September 2023
Department of Biomedical Sciences, Graduate School of Science and Technology, Kwansei Gakuin University, Gakuen-Uegahara, Sanda, 669-1330, Japan.
The skin epidermis exhibits an asymmetric structure composed of multilayered keratinocytes and those in the outer layers form two-way physical barriers, cornified cell envelope (CCE), and tight junctions (TJs). While undifferentiated keratinocytes in the basal layer continuously deliver daughter cells outward, which undergo successive differentiation with losing their polarized characteristics, they retain the expression of several polarity proteins. In the present study, we revealed that the t-SNARE protein syntaxin3, a critical element for the formation of the apical compartment in simple epithelial cells, is required to confer the ability to organize the physical barriers on "poorly polarized" keratinocytes in epidermal outer layers.
View Article and Find Full Text PDFExtracellular epimorphin impairs expression and processing of profilaggrin in HaCaT keratinocytes.
Cytotechnology
April 2023
Department of Biomedical Sciences, Graduate School of Science and Technology, Kwansei Gakuin University, 1, GakuenUegahara, Sanda, 669-1330 Japan.
Unlabelled: The expression and processing of filaggrin, a filament-associated protein in the skin epidermis, is closely associated with keratinocyte cornification. The large precursor profilaggrin (Pro-FLG) is initially detected at the granular layer in keratohyalin granules, subsequently processed into 10 to 12 filaggrin monomers (mFLGs) for keratin assembly, and ultimately degraded into smaller peptides that behave as natural moisturizing factor (NMF) at the outermost epidermis. We previously reported that epimorphin (EPM) extruded upon external stimuli severely perturbs epidermal terminal differentiation.
View Article and Find Full Text PDFSulfated glycosaminoglycans and non-classically secreted proteins, basic FGF and epimorphin, coordinately regulate TGF-β-induced cell behaviors of human scar dermal fibroblasts.
J Dermatol Sci
May 2017
Department of Biomedical Chemistry, Graduate school of Science and Technology, Kwansei Gakuin University, 2-1, Gakuen, Sanda 669-1337, Japan. Electronic address:
Background: Upon skin injuries, dermal fibroblasts actively produce transforming growth factor-β (TGF-β), which leads to the formation of α-smooth muscle actin (αSMA)-positive granulation tissues. The hyperplasia or incomplete regression of these tissues subsequently causes scar formation in the skin, where sulfated glycosaminoglycans (GAGs), side chains of unique proteoglycans, are supposed to play important roles.
Objective: The aim of this study is to clarify the effects of sulfated GAGs on dermal cell behaviors triggered by the TGF-β signaling, along with its possible regulators basic fibroblast growth factor (bFGF) and cell surface epimorphin.
Epimorphin-induced differentiation of human umbilical cord mesenchymal stem cells into sweat gland cells.
Eur Rev Med Pharmacol Sci
April 2015
Department of Plastic Surgery, PLA General Hospital, Beijing, People's Republic of China.
Objectives: Mesenchymal stem cells (MSCs) have the potential for multi-directional differentiation and can be induced to differentiate into sweat gland cells under certain conditions. Epimorphin (EPM) plays an important role in the promotion of epithelial cell morphogenesis; however, its effect on sweat gland-cell differentiation of MSCs remains unknown. The purpose of this study was to investigate how EPM regulates sweat gland cell differentiation of human umbilical cord mesenchymal stem cells (hUCMSCs).
View Article and Find Full Text PDFEffluent syntaxin3 from dying cells affords protection against apoptosis in epidermal keratinocytes.
Exp Dermatol
December 2013
Department of Bioscience, Kwansei Gakuin University, Sanda, Japan.
Ultra-violet B (UVB)-induced oxidative stress crucially perturbs the epidermal homeostasis, and the skin is endowed with protective mechanisms to take action against such damage. Here, we show the possible involvement of t-SNARE protein syntaxin3, a membrane fusion mediator of cytoplasmic vesicles, and which is released from dying keratinocytes, to play a role in this response. UVB irradiation, which generates reactive oxidative stress in cells, was shown to lead to the keratinocyte cell death accompanied by a release of cytoplasmic syntaxin3.
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