Generation of a Monoclonal Antibody Against Avian Small Dermatan Sulfate Proteoglycan: Immunolocalization and Tissue Distribution of PG-II (Decorin) in Embryonic Tissues

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.

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Inhibition of EGF receptor phosphorylation and PI-3 kinase activity negatively regulates endocytosis of the dermatan sulfate proteoglycan decorin in human fibroblasts

Experimental and Clinical Endocrinology & Diabetes ◽

10.1055/s-2006-933019 ◽

2006 ◽

Vol 114 (S 1) ◽

Author(s):

M Götte ◽

DD Sofeu Feugaing ◽

L Kiesel

Keyword(s):

Kinase Activity ◽

Egf Receptor ◽

Dermatan Sulfate ◽

Human Fibroblasts ◽

Sulfate Proteoglycan ◽

Receptor Phosphorylation ◽

Dermatan Sulfate Proteoglycan

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A temporal and ultrastructural relationship between heparan sulfate proteoglycans and AA amyloid in experimental amyloidosis.

Journal of Histochemistry & Cytochemistry ◽

10.1177/39.10.1940305 ◽

1991 ◽

Vol 39 (10) ◽

pp. 1321-1330 ◽

Cited By ~ 69

Author(s):

A D Snow ◽

R Bramson ◽

H Mar ◽

T N Wight ◽

R Kisilevsky

Keyword(s):

Heparan Sulfate ◽

Amyloid Fibrils ◽

Dermatan Sulfate ◽

Polyclonal Antibodies ◽

Amyloid Deposition ◽

Sulfate Proteoglycan ◽

Aa Amyloidosis ◽

Experimental Amyloidosis ◽

Protein Core ◽

Dermatan Sulfate Proteoglycan

Previous histochemical studies have suggested a close temporal relationship between the deposition of highly sulfated glycosaminoglycans (GAGs) and amyloid during experimental AA amyloidosis. In the present investigation, we extended these initial observations by using specific immunocytochemical probes to analyze the temporal and ultrastructural relationship between heparan sulfate proteoglycan (HSPG) accumulation and amyloid deposition in a mouse model of AA amyloidosis. Antibodies against the basement membrane-derived HSPG (either protein core or GAG chains) demonstrated a virtually concurrent deposition of HSPGs and amyloid in specific tissue sites regardless of the organ involved (spleen or liver) or the induction protocol used (amyloid enhancing factor + silver nitrate, or daily azocasein injections). Polyclonal antibodies to AA amyloid protein and amyloid P component also demonstrated co-localization to sites of HSPG deposition in amyloid sites, whereas no positive immunostaining was observed in these locales with a polyclonal antibody to the protein core of a dermatan sulfate proteoglycan (known as "decorin"). Immunogold labeling of HSPGs (either protein core or GAG chains) in amyloidotic mouse spleen or liver revealed specific localization of HSPGs to amyloid fibrils. In the liver, heparan sulfate GAGs were also immunolocalized to the lysosomal compartment of hepatocytes and/or Kupffer cells adjacent to sites of amyloid deposition, suggesting that these cells are involved in HSPG production and/or degradation. The close temporal and ultrastructural relationship between HSPGs and AA amyloid further implies an important role for HSPGs during the initial stages of AA amyloidosis.

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