User:Dalinchan/sandbox

FUNCTIONS The extracellular matrix (ECM) is a component primarily in multicellular organisms that has a complex and dynamic meshwork of molecule which adjust the behavior of cells. Its components are wide variety of collagen types, noncollagenous, proteoglycans, glycoprotein, etc [1,2,3]. Dermatopontin is a 22-kDa protein of the extracellular matrix (ECM)’s noncollagenous components that compose of wet dermis weighted about 12mg/kg [1,4]. Up to date, dermatopontin’s homologues have been identified in five different mammals and 12 different invertebrates with multiple functions [1,2,4]. In vertebrate, the functional characterization of dermatopontin are related to ECM architecture (interaction with decorin and modification of collagen fibrillogenesis), cell behavior (cell adhesion, modification of TGF-β bioactivity, and expression in cell quiescence), pathological involvement (increased expression around myocardial infarct zone, decreased expression in leiomyoma and keloid, decreased expression in fibrosing diseases) while in invertebrate, the functional characterization of dermatopontin homologue are hemagglutination, cell-cell aggregation, and expression during parasite infection [1].

Cell Adhesion Cell adhesion is the effect of the cell behavior due to the function of the dermatopontin. Even though, cell adhesion activity of dermatopontin isn’t strong for a certain fibroblasts and neurogenic cells, but it might have various roles in wound healings because dermatonpontin has been found in a provisional matrix that interacted with fibrin and fibronectin (Fn) which has improved the cell adhesion activity of Fn [1,4,5]. A provisional matrix is forms of extravasated blood after the wounding, which compose of the wound fluid, fibrin and Fn [4]. In the provisional matrix, the Fn perform as an adhesion and migration structure to provide support all around the ECM for fibroblasts and circulation-derived cells, while in tissues, Fn perform as an activated and collected into the Fn matrix (a fibrillar structure) that discovered during both development of embryonic and wound healing [6,7]. In addition, one study has shown that dermatopontin has been found in the provisional matrix as well as in the wound fluid, and it has demonstrated that dermatopontin promoted Fn fibril formation that biologically functions in the dermal wound healing [4]. Moreover, the study has also revealed that the presence of dermatopontin has enhanced the Fn interaction with fibrin as well as the enhancement of cell adhesion, which indicated the morphological changed of the cells which has been adhered to the complex [4]. Furthermore, dermatopontin determined to be found in the interaction sites of Fn on III_13 and III_14 and cryptic site of III_1, which all involved in formation of Fn fibrils [4]. The inhibition of dermatopontin were considering to be between III_(2-3) and III_(12-14) because dermatopontin was not enhanced the interaction between III_(1-5) and III_(1-2), which could be the domains unfold as the disruption of the other interdomain interactions [8]. In this case, dermatopontin indicated as domain unfolding of a Fn molecule due to the binding site for anastellin (the only known protein that induce superfibronectin formation) on Fn is located between III_(2-3) and III_(12-14) inside the interaction site, which is the important binding site for the Fn fibril formation [4,8]. Therefore, dermatopontin is protein within the ECM that could activate Fn and induce Fn fibril formation, which could help in wound healing due to its accumulation in the wound whether from the ECM’s surrounded or from the serum [4]. References Okamoto, O. and Fujiwara, S. (2006) Dermatopontin, a novel player in the biology of the extracellular matrix. Connective Tissue Research, 47, 177-189. Kim, H. S. and Cheon, Y. (2006) Spatio-temporal expression and regulation of dermatopontin in the early pregnant mouse uterus. Mol. Cells, 22, 262-268. Naba, A., Pearce, O. M. T., Rosario, A. D., Ma, D., Ding, H., et al. (2017) Characterization of the extracellular matrix of normal and diseased tissues using proteomics. Journal of proteome research, 16, 3083-3091. Kato, A., Okamoto, O., Ishikawa, K., Sumiyoshi, H., Matsuo, N., et al. (2011) Dermatopontin interacts with fibronectin, promotes fibronectin fibril formation, and enhances cell adhesion. Journal of Biological Chemistry, 286, 14861-14869. Lewandowska, K., Choi, H.U., Rosenberg, L.C., Sasse, J., Neame, P.J., and Culp, L.A. (1991). Extracellular matrix adhesion-promoting activities of a dermatan sulfate proteoglycan-associated protein (22K) from bovine fetal skin. J. Cell Sci., 99, 657–668. Midwood K. S., Mao Y., Hsia H. C., Valenick L. V., Schwarzbauer J. E. (2006) J. Invest. Dermatol. Symp. Proc. 11, 73–78.	Muro A. F., Chauhan A. K., Gajovic S., Iaconcig A., Porro F., Stanta G., Baralle F. E. (2003) J. Cell Biol. 162, 149–160.	Ohashi T., Erickson H. P. (2005) Domain unfolding plays a role in superfibronectin formation. J. Biol. Chem. 280, 39143–39151.