Decorin (DCN), a class I member of the small leucine-rich proteoglycan (SLRP) family, is composed of a protein core of approximately 40kDa [1, 2] substituted with a single glycosaminoglycan (GAG) chain of chondroiton/dermatan sulfate on the N-terminal site . DCN has been reported to interact with collagen [4,5] via its core protein, influence collagen fibrillogenesis , and inhibit the growth rates of various cell types when added exogenously to cell cultures [5,6]. There has recently been growing interest and studies in DCN related research using the knockout (KO) mice model which provides an excellent example of inherited disorders that stem from deficiencies in decorin expression . Skin and tendon tissues from DCN KO mice have been characterized as being extremely fragile with significantly reduced strength and stiffness [8, 9]. The DCN KO tissues also show potential functional biglycan compensation  and at the microscopic level collagen fibrils with highly irregular diameters, abnormal lateral fusion, and loose packing  in contrast to wild type (WT) mice. Despite the intensive investigation of the DCN KO mice, the complexity of the animal model makes it difficult to assess the actual influence of decorin. In an attempt to take a more simplistic approach 2D cell phenotypic characterization studies were performed in addition to studying cell growth, contraction, and matrix organization in 3-D models to show the very distinct biochemical responses to type I collagen when compared to WT control cells.
Decorin Deficient Cells Demonstrate Increased Proliferation and Altered Phenotypic Properties
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Peterson, SB, Ferdous, Z, Höök, M, & Grande-Allen, KJ. "Decorin Deficient Cells Demonstrate Increased Proliferation and Altered Phenotypic Properties." Proceedings of the ASME 2007 Summer Bioengineering Conference. ASME 2007 Summer Bioengineering Conference. Keystone, Colorado, USA. June 20–24, 2007. pp. 985-986. ASME. https://doi.org/10.1115/SBC2007-176043
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