Decorin interacts with fibrillar collagen of embryonic and adult human skin

Abstract

Biglycan (PG-I, BGN) and decorin (PG-II, DCN) are small proteoglycans that have been isolated in cartilage, skin, and bone. Although the function of biglycan is unknown, there is biochemical evidence that deeorin interacts with fibrillar collagens (type I, type II). The purpose of this study was to perform immunofluorescence and immunoelectron microscopy and immunoblotting of human embryonic and adult skin with antibodies directed against biglycan and decorin. These antibodies were developed against synthetic peptides of the core proteins of biglycan (amino acid sequence 11-24) and decorin (amino acid sequence 5-17). Immunofluorescence microscopy showed that decorin stained embryonic and adult collagen fib&. Biglycan did not stain collagen, but it appeared to stain the pericellular matrix of embryonic mesenchymal cells. Immunoelectron microscopy revealed labeling of all collagen fibrils with decorin antibodies regardless of their diameter, often at 60-nm perk&city. Positive stains suggest that most of the labeling was in the gap of the D-period (d and e bands) and also in one of the steps (c band). Decorin was identified by immunoblotting in fetal and adult skin. Also, significant amounts of core protein was identified lacking the dermatan sulfate chain. This study suggests that the core protein of decorin interacts with collagen fibrils although its specific function remains unknown. 0 1991 Academic Press, 1~.

FOXD1 promotes nephron progenitor differentiation by repressing decorin in the embryonic kidney

“…S2). DCN associates with collagen I and is predicted to bind collagen IV, modulating their conformation (Fleischmajer et al, 1991;Parkin et al, 2011;Schönherr et al, 1995). We next investigated whether collagens also mislocalize in Foxd1 −/− kidneys.…”

Lysophosphatidylcholine Regulates Synthesis of Biglycan and the Proteoglycan Form of Macrophage Colony Stimulating Factor

“…Hydrodynamic size and glycosaminoglycan chain length were evaluated by analytical Sepharose CL-2B and CL-6B, respectively. 14 Core proteins of chondroitin ABC lyase (CABC lyase)-digested samples were identified by Western analysis using antisera specific for human biglycan (1:1000) 22 or human osteosarcoma PG-100/PG-MCSF (1:1000). 23 Total RNA was isolated using the RNAqueous system (Ambion) for Northern analysis.…”

Morphological assessment of bone mineralization in tibial metaphyses of ascorbic acid-deficient ODS rats

“…Many researchers investigated whether very small crystals nucleate in these hole zones (13,16,21,37). There exists an assumption that the "hole zone" is normally occupied by small proteoglycans such as decorin and biglycan (10,13), which may inhibit the nucleation of mineral crystals in a normal state. It has been shown that decorindeficient tendons develop abnormal, irregularly contoured collagen fibrils, indicating that small leucine-rich proteoglycans such as biglycan, decorin, fibromodulin, and lumican, as well as glycoproteins are involved in collagen fibril strucutral maturation and tissue function (8,39).…”

“…Despite a marked reduction in bone formation, ascorbic acid deprivation seemed to have no deleterious effect on mineralization: while reduced in number, normal matrix vesicles and mineralized nodules could be seen in aadef bones. Theoretically, the "hole zone" in collagen fibrils should be occupied by small proteoglycans such as decorin and biglycan (10,13), and the release of these proteoglycans may trigger crystal nucleation in collagen. In aa-def bones, the presence of very fine fibrillar and amorphous materials indicated alterations of the ultrastructural geometry of collagen fibrils, implying the absence or disruption of the hole zones.…”