scholarly journals Immunocytochemical investigation on the distribution of small chondroitin sulfate-dermatan sulfate proteoglycan in the human.

1986 ◽  
Vol 34 (8) ◽  
pp. 1013-1019 ◽  
Author(s):  
B Voss ◽  
J Glössl ◽  
Z Cully ◽  
H Kresse
Keyword(s):  
Chondroitin Sulfate ◽  
Dermatan Sulfate ◽  
Core Protein ◽  
Affinity Purification ◽  
Basement Membranes ◽  
Positive Staining ◽  
Human Skin Fibroblast ◽  
Sulfate Proteoglycan ◽  
Specific Staining ◽  
Dermatan Sulfate Proteoglycan

Polyclonal antibodies against the core protein of the small chondroitin sulfate-dermatan sulfate proteoglycan from human skin fibroblast secretions were used, after affinity-purification, as a probe to study localization of crossreactive material in several human tissues by indirect immunocytochemistry. In contrast to skin, kidney, and the adventitial layer of aorta, positive staining of brain, liver, cartilage, and intimal and medial layers of aorta required pre-treatment of tissue sections with chondroitin ABC lyase. In all tissues investigated, antigenic material was present in the interstitial space. Filamentous structures were perpendicularly oriented towards basement membranes. In liver, specific staining was seen along the sinusoidal walls. Reticular fibers with or without focal condensations were seen in cerebral cortex and cerebellum. The results suggest a role of small chondroitin sulfate-dermatan sulfate proteoglycan in cell-matrix interactions.

scholarly journals Production and characterization of monoclonal antibody to dermatan sulfate proteoglycan.

1988 ◽  
Vol 36 (5) ◽  
pp. 479-485 ◽  
Author(s):  
M Sobue ◽  
N Nakashima ◽  
T Fukatsu ◽  
T Nagasaka ◽  
T Katoh ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Dermatan Sulfate ◽  
Core Protein ◽  
Immunohistochemical Localization ◽  
Positive Staining ◽  
Sulfate Proteoglycan ◽  
Atherosclerotic Lesions ◽  
Dermatan Sulfate Proteoglycan ◽  
Intact Molecule ◽  
Almost All

We purified dermatan sulfate proteoglycan (PG) from the capsule of human ovarian fibroma for use as an immunogen. A monoclonal antibody, designated 6B6, was produced which reacts to the intact molecule of dermatan sulfate PG and the chondroitinase AC-treated core molecule on Western-blotted nitrocellulose membrane. Localization of materials showing crossreactivity to this antibody was studied in human tissues by indirect immunohistochemistry. The interstitial elements of almost all tissues examined were positive for the antibody: dermis, submucosal layer of digestive tract, perichondral layer, perivascular connective tissue, perineurium, adventitia of aorta, vessel wall of vein, pleura, and fibrous capsule of kidney and liver. Positive staining was also observed in fibrous elements at post-necrotic foci of cardiac muscle and pancreas, and at atherosclerotic lesions of aorta. The distribution of the antigen, core protein of the dermatan sulfate PG, revealed with 6B6 was compared to that of the dermatan sulfate side chain, which was demonstrated with antibody 9A-2 (Couchman et al.: Nature 307:650, 1984) after treatment with chondroitin sulfate B-lyase. The distribution of both antigens, core protein, and dermatan sulfate side chains showed the same pattern, with minor exceptions. The antibody 6B6 will be a useful tool to study the immunohistochemical localization of dermatan sulfate PG.

Isolation of a chondroitin sulfate-dermatan sulfate proteoglycan from bovine aorta

1975 ◽  
Vol 171 (1) ◽  
pp. 361-369 ◽  
Author(s):  
Kenneth C. Ehrlich ◽  
Bhandaru Radhakrishnamurthy ◽  
Gerald S. Berenson
Keyword(s):  
Chondroitin Sulfate ◽  
Dermatan Sulfate ◽  
Sulfate Proteoglycan ◽  
Dermatan Sulfate Proteoglycan

scholarly journals Basement membrane chondroitin sulfate proteoglycans: localization in adult rat tissues.

1990 ◽  
Vol 38 (10) ◽  
pp. 1479-1486 ◽  
Author(s):  
K J McCarthy ◽  
J R Couchman
Keyword(s):  
Chondroitin Sulfate ◽  
Dermatan Sulfate ◽  
Core Protein ◽  
Rat Kidney ◽  
Basement Membranes ◽  
Rat Tissues ◽  
Adult Rat ◽  
Unique Distribution ◽  
Reichert's Membrane

Heparan sulfate proteoglycans have been described as the major proteoglycan component of basement membranes. However, previous investigators have also provided evidence for the presence of chondroitin sulfate glycosaminoglycan in these structures. Recently we described the production and characterization of core protein-specific monoclonal antibodies (MAb) against a chondroitin sulfate proteoglycan (CSPG) present in Reichert's membrane, a transient extra-embryonic structure of rodents. This CSPG was also demonstrated to be present in adult rat kidney. We report here the tissue distribution of epitopes recognized by these MAb. The ubiquitous presence of these epitopes in the basement membranes of nearly all adult rat tissues demonstrates that at least one CSPG is a constituent of most basement membranes, and by virtue of its unique distribution is distinct from other chondroitin and dermatan sulfate proteoglycans previously described.

scholarly journals Effect of beta-D-xyloside on the glomerular proteoglycans. I. Biochemical studies.

1984 ◽  
Vol 99 (2) ◽  
pp. 715-722 ◽  
Author(s):  
Y S Kanwar ◽  
V C Hascall ◽  
M L Jakubowski ◽  
J T Gibbons
Keyword(s):  
Dermatan Sulfate ◽  
De Novo ◽  
Core Protein ◽  
Total Radioactivity ◽  
Sulfate Proteoglycan ◽  
Perfusion Medium ◽  
Density Fractions ◽  
Dermatan Sulfate Proteoglycan ◽  
Cscl Density Gradient ◽  
Isolated Organ Perfusion

The effect of p-nitrophenyl-beta-D-xylopyranoside on glomerular extracellular matrices (glomerular basement membrane and mesangial matrix) proteoglycans was studied. The proteoglycans of rat kidneys were labeled with [35S]sulfate in the presence or absence of beta-xyloside (2.5 mM) by using an isolated organ perfusion system. The proteoglycans from the glomeruli and perfusion medium were isolated and characterized by Sepharose CL-6B chromatography and by their behavior in CsCl density gradients. With xyloside treatment there was a twofold decrease in 35S-labeled macromolecules in the tissues but a twofold increase in those recovered in the medium as compared with the control. The labeled proteoglycans extracted from control kidneys eluted as a single peak with Kav = 0.25 (Mr = approximately 130,000), and approximately 95% of the radioactivity was associated with heparan sulfate proteoglycan (HS-PG), the remainder with chondroitin (or dermatan) sulfate proteoglycan (CS-PG). In the xyloside-treated kidneys, the proteoglycans extracted from the tissue eluted as two peaks, Kav = 0.25 (Mr = approximately 130,000) and 0.41 (Mr = approximately 46,000), which contained approximately 40 and approximately 60% of the total radioactivity, respectively. The first peak contained mostly the HS-PG (approximately 90%) while the second peak had a mixture of HS-PG (approximately 70%) and CS-PG (approximately 30%). In controls, approximately 90% of the radioactivity, mostly HS-PG, was confined to high density fractions of a CsCl density gradient. In contrast, in xyloside experiments, both HS-PG and CS-PG were distributed in variable proportions throughout the gradient. The incorporated 35S activity in the medium of xyloside-treated kidneys was twice that of the controls and had three to four times the amount of free chondroitin (or dermatan) sulfate glycosaminoglycan chains. The data suggest that beta-xyloside inhibits the addition of de novo synthesized glycosaminoglycan chains onto the core protein of proteoglycans and at the same time stimulates the synthesis of chondroitin or dermatan sulfate chains which are mainly discharged into the perfusion medium.

scholarly journals Novel Insight Into Glycosaminoglycan Biosynthesis Based on Gene Expression Profiles

2021 ◽  
Vol 9 ◽  
Author(s):  
Yi-Fan Huang ◽  
Shuji Mizumoto ◽  
Morihisa Fujita
Keyword(s):  
Gene Expression ◽  
Chondroitin Sulfate ◽  
Dermatan Sulfate ◽  
Expression Profiles ◽  
Gene Expression Profiles ◽  
Sulfate Proteoglycan ◽  
Expression Levels ◽  
Core Proteins ◽  
Dermatan Sulfate Proteoglycan ◽  
Insight Into

Glycosaminoglycans (GAGs) including chondroitin sulfate, dermatan sulfate, heparan sulfate, and keratan sulfate, except for hyaluronan that is a free polysaccharide, are covalently attached to core proteins to form proteoglycans. More than 50 gene products are involved in the biosynthesis of GAGs. We recently developed a comprehensive glycosylation mapping tool, GlycoMaple, for visualization and estimation of glycan structures based on gene expression profiles. Using this tool, the expression levels of GAG biosynthetic genes were analyzed in various human tissues as well as tumor tissues. In brain and pancreatic tumors, the pathways for biosynthesis of chondroitin and dermatan sulfate were predicted to be upregulated. In breast cancerous tissues, the pathways for biosynthesis of chondroitin and dermatan sulfate were predicted to be up- and down-regulated, respectively, which are consistent with biochemical findings published in the literature. In addition, the expression levels of the chondroitin sulfate-proteoglycan versican and the dermatan sulfate-proteoglycan decorin were up- and down-regulated, respectively. These findings may provide new insight into GAG profiles in various human diseases including cancerous tumors as well as neurodegenerative disease using GlycoMaple analysis.

scholarly journals Interaction of small dermatan sulfate proteoglycan from fibroblasts with fibronectin.

1987 ◽  
Vol 104 (6) ◽  
pp. 1683-1691 ◽  
Author(s):  
G Schmidt ◽  
H Robenek ◽  
B Harrach ◽  
J Glössl ◽  
V Nolte ◽  
...  
Keyword(s):  
Dermatan Sulfate ◽  
Core Protein ◽  
Human Fibroblasts ◽  
Enzyme Linked Immunosorbent Assay ◽  
Sulfate Proteoglycan ◽  
Heparin Binding ◽  
Dermatan Sulfate Proteoglycan ◽  
Cultured Human Fibroblasts ◽  
Heparin Binding Domain ◽  
Double Label

Immunogold labeling was used to localize the core protein of small dermatan sulfate proteoglycan (DS-PG) on the surface of cultured human fibroblasts. At 4 degrees C, DS-PG core protein was uniformly distributed over the cell surface. At 37 degrees C, gold particles either became rearranged in form of clusters or remained associated with fibrils. Double-label immunocytochemistry indicated the co-distribution of DS-PG core protein and fibronectin in the fibrils. In an enzyme-linked immunosorbent assay, binding of DS-PG from fibroblast secretions and of its core protein to fibronectin occurred at pH 7.4 and at physiological ionic strength. Larger amounts of core protein than of intact proteoglycan could be bound. Fibronectin peptides containing either the heparin-binding domain near the COOH-terminal end or the heparin-binding NH2 terminus were the only fragments interacting with DS-PG and core protein. Competition and replacement experiments with heparin and dermatan sulfate suggested the existence of adjacent binding sites for heparin and DS-PG core protein. It is hypothesized that heparan sulfate proteoglycans and DS-PG may competitively interact with fibronectin.

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