The role of decorin in collagen fibrillogenesis and skin homeostasis.
Decorin, a prototype member of the growing family of the small leucine-rich proteoglycans (SLRP's), plays significant roles in tissue development and assembly, as well as playing both direct and indirect signaling roles. This review will concentrate on decorin's function in collagen fibrillogenesis as determined through the study of mice with a disrupted decorin gene. The fragile skin and abnormal tendon phenotypes initially observed were found to be due to fundamental alterations in collagen fibers, highlighting the crucial role of proteoglycans in general and SLRP's in particular in collagen fibrillogenesis. The altered fibril formation within tissues in turn leads to observable and quantifiable changes at the organismal level. Research into certain fibrotic processes with concomitant upregulation or reduction of decorin makes interesting comparisons with the collagen malformations seen in Dcn(-/-) mice. Overall, decorin is shown to be a vital player in maintaining skin and tendon integrity at the molecular level, among other functions.
Reed
Charles C
CC
Department of Pathology, Anatomy and Cell Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA.
Iozzo
Renato V
RV
D000818:Animals; D003094:Collagen / Q000096:biosynthesis* / Q000737:chemistry; D058575:Decorin; D016326:Extracellular Matrix Proteins; D006706:Homeostasis; D051379:Mice; D018345:Mice, Knockout; D015394:Molecular Structure; D010641:Phenotype; D011509:Proteoglycans / Q000737:chemistry / Q000172:deficiency / Q000235:genetics / Q000502:physiology*; D012879:Skin Physiological Phenomena; D013710:Tendons / Q000002:abnormalities
C546879:Dcn protein, mouse; D058575:Decorin; D016326:Extracellular Matrix Proteins; D011509:Proteoglycans; D003094:Collagen