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Dermatopontin effect on collagen fibrillogenesis

Dermatopontin (DPT) a decorin- an associated molecule found by research to affect the skin by interacting with collagen fibrils which leads to the formation of collagen fibrillogenesis. In a study by Ushio Takeda, DPT was found to affect elasticity in the skin and collagen accumulation which have contributed to fibrillogenesis (Takeda et al, 2002). The experiment conducted involves gene editing to create chimeric mice which are then mated to produce the dermatopontin-null(DPT-null) mice. The DPT-null mice were tested for skin elasticity using the skin tensile test. The result found that the initial elastic modulus was lower in DPT-null mice which can be accounted for by a fewer amount of collagen and decreased the thickness of the dermis. The dorsal skin of the DPT-null mice was stained with Azan and was analyzed under light microscopy. Light microscopy showed the dermis has become thinner and showed the collagen accumulation has decreased as well. Deep dermis testing of female mice showed the “mean diameters of collagen fibrils” were thicker in DPT-null mice and have a “wider range distribution” than wild-type mice (Takeda et al, 2002). These results show that DPT deficiency contributes to collagen fibrillogenesis activity. Takeda based his work from MacBeath, who has done a study involving the effects of DPT on collagen fibrillogenesis. In MacBeath’s study, they have found without the presence of DPT, the “reconstituted fibrils were relatively larger and had a wider range of diameters, from 40 to over 200nm” than the fibrils found in the existence of DPT. Takeda also confirmed this through electron microscopy analysis of the deep dermis which showed a “great variety in diameter and irregular contours”. This lead Takeda to conclude that DPT reduces the size of collagen fibrils in the deep dermis. MacBeath also found that that DPT can speed up the rate of fibril formation when “the kinetics of fibril formation was monitored by turbidity at 313 nm” and when a purified DTP was added. In addition, when DTP, by itself, was added to help accelerate fibril formation, the “final turbidity became greater in proportion to DP concentration” (Wu et al, 2014). Other studies were done on the effects of DPT on collagen fibrils in the skin. A study conducted by Danielson found that decorin affects the growth of collagen fibrils and how altering decorin can affect “biological properties of collagen and disrupt the finely balanced network of molecular interactions that govern fibril assembly”. Growth was associated with fewer “fibril-associated decorin” (Danielson et al, 1997). Decorin has many different functions from regulating fibril formation to a signaling mediator (Seidler and Dreier 730). By changing the functions of decorin, Danielson also discovered that DPT can use decorin to control the process of collagen fibrillogenesis. Interactions involving DTP with LRR PGS and type V collagen have also been noted to be a possible contribution to understanding the effect of dermatopontin on collagen fibrillogenesis. However, additional research must be conducted to interpret the relationship (Takeda et al, 2002).