Staining of proteoglycans in mouse lung alveoli. II. Characterization of the Cuprolinic Blue-positive, anionic sites

Kuppevelt, T. H. M. S. M. Van; Cremers, Frans P.M.; Domen, Jos; Kuyper, Ch.M.A.

doi:10.1007/bf01003394

Cited by 70 publications

(19 citation statements)

References 37 publications

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“…The GAGs are powerful inhibitors of proteases, including leucocyte elastase [20,22,53], and prevent leucocyte elastaseinduced emphysema in mouse and rat [23,24]. Ultrastructurally, proteoglycans are present around collagen fibrils, elastin fibres and in basement membranes [6,25,27,28]. Removal of proteoglycans associated with elastin facilitates the digestion of the latter [54][55][56].…”

Section: Lung and Urinary Gag Content After Elastase Instillationmentioning

confidence: 99%

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Digestion of proteoglycans in porcine pancreatic elastase-induced emphysema in rats

Lest

Versteeg²,

Veerkamp³

et al. 1995

Eur Respir J

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D Di ig ge es st ti io on n o of f p pr ro ot te eo og gl ly yc ca an ns s i in n p po or rc ci in ne e p pa an nc cr re ea at ti ic c e el la as st ta as se e--i in nd du uc ce ed d e em mp ph hy ys se em ma a i in n r ra at ts s Lung alveoli showed a decrease in heparan sulphate proteoglycan content (especially of its heparan sulphate chains) 3 h to 7 days after induction. Type IV collagen, laminin and fibronectin were not affected. The glycosaminoglycan content of the lung was decreased during the first 3 days after induction, while the glycosaminoglycan concentration in urine was increased during the first 4 days by an increase of heparan sulphate and dermatan sulphate. The increase in urinary glycosaminoglycan content was positively correlated with the extent of emphysema developed after 40 days.We conclude that proteoglycans are target molecules for elastase, and may be involved in the pathogenesis of emphysema.

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Section: Lung and Urinary Gag Content After Elastase Instillationmentioning

confidence: 99%

“…In addition, the close association of PGs with structural elements in the alveolar wall (e.g. basement membranes, collagen fibrils and elastin fibres) indicates a protective role [6,[25][26][27][28].…”

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confidence: 99%

Digestion of proteoglycans in porcine pancreatic elastase-induced emphysema in rats

Lest

Versteeg²,

Veerkamp³

et al. 1995

Eur Respir J

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“…Growth factors like fibroblast growth factors are retained by HS. Electron microscopical studies using cationic probes indicate that HS in the basement membranes of alveolar type I and type II cells and of alveolar endothelial cells are differentially sulfated (12,13). Sulfated proteoglycans play a central role in the modulation of the extracellular matrix of pulmonary fibroblasts, and HSPGs are involved in neutrophil trafficking to the alveolar space (14).…”

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confidence: 99%

Heterogeneity of Heparan Sulfates in Human Lung

Smits¹,

Robbesom²,

Versteeg³

et al. 2004

Am J Respir Cell Mol Biol

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Heparan sulfates (HS), a class of glycosaminoglycans, are long linear complex polysaccharides covalently attached to a protein core. The HS molecules are made up of repeating disaccharides onto which modification patterns are superimposed. This results in a large structural heterogeneity and forms the basis of specific interactions of HS toward a vast array of proteins, including growth factors and proteases. To study HS heterogeneity in the lung, we used phage display technology to select seven antibodies against human lung HS. Antibodies reacted with HS/heparin, but not with other glycosaminoglycans or polyanions. Sulfate groups were essential for antibody binding. The amino acid sequence of the antibodies was established, the complementarity determining region 3 of the heavy chain containing basic amino acids. The antibodies defined HS epitopes with a characteristic tissue distribution. Antibody EV3A1 primarily stained macrophages. Other antibodies primarily stained basement membranes, but with different preference toward type of basement membrane. Antibody EV3C3 was the only antibody which clearly reacted with bronchiolar epithelial cells. In human lung parenchyma, basic fibroblast growth factor and vascular endothelial growth factor were largely bound by HS. Some antibodies blocked a basic fibroblast growth factorbinding site of HS, and one antibody blocked a vascular endothelial growth factor-binding site of heparin. Taken together, these data suggest a specific role for HS epitopes in human lung. The antibodies obtained may be valuable tools to study HS in pulmonary diseases.Heparan sulfates (HS) are members of the glycosaminoglycan (GAG) family, consisting of repeating disaccharide units onto which modification patterns are superimposed. HS bind and modulate a myriad of molecules, including growth factors, cytokines, proteases, antiproteases, matrix molecules, and viral and bacterial proteins (1,2). This large number of interactions suggests an extensive structural variation within HS. The structural diversity of HS is brought about by specific chain modifications during the biosynthesis of HS, including deacetylation, sulfation, and epimerization. The addition of, e.g., sulfate groups leads to the generation of specific motifs that make HS highly versatile, protein-

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“…(1989) concluded that without the use of an agent to preserve the highly aqueous soluble negativelycharged glycoconjugates, more than 50% of these macromolecules are lost from the tissue during histochemical processing. However, in this study as in numerous other studies (Van Kuppevelt et al, 1984b;Haigh & Scott, 1986;V61ker et aL, 1986;Velasco & Hidalgo, 1988;Sauren et aL, 1989), chondroitinase digestions were performed on samples pre-fixed in aldehyde alone. Moreover, for control of enzymatic treatment, CB-staining was also only performed after a pre-fixation in glutaraldehyde with or without an intermediate step of sham digestion.…”

Section: Discussionmentioning

confidence: 99%

The proteoglycan skeleton of the Kurloff body as evidenced by Cuprolinic Blue staining

et al. 1994

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This study deals with the ultrastructure of the chondroitin sulphate proteoglycans of the Kurloff body, a large lysosome organelle, metachromatic towards Toluidine Blue, of a blood cell unique to the guinea pig and called the Kurloff cell. Splenic Kurloff cell from oestrogen-treated guinea pig cells were examined after staining with Cuprolinic Blue, a cationic phthalocyanine-like dye, in the presence of MgCl2 in a critical electrolyte concentration method. Better results were obtained when the fixation-staining by the glutaraldehyde Cuprinolinic Blue MgCl2 mixture was preceded by a glutaraldehyde pre-fixation. On light microscopy, Kurloff bodies generally exhibited an overall pink and glassy metachromasia, sometimes with additional darker metachromatic small dots at their peripheries. At the ultrastructural level, the metachromatic central matrix of the Kurloff body usually exhibited, as a major feature, a typical network pattern of ribbon-like or stellate electron-dense precipitates suggesting the presence of a skeleton of Cuprolinic Blue-reactive filamentous structures. Taking into account their high anionicity (as shown by the stability of the dye binding in the presence of 0.3 M MgCl2) and their susceptibility to chondroitinase ABC, these anionic structures were assumed to be related to the proteochondroitin-4-sulphate previously characterized as the only major sulphated glycoconjugate of the Kurloff cell.

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Staining of proteoglycans in mouse lung alveoli. II. Characterization of the Cuprolinic Blue-positive, anionic sites

Cited by 70 publications

References 37 publications

Digestion of proteoglycans in porcine pancreatic elastase-induced emphysema in rats

Digestion of proteoglycans in porcine pancreatic elastase-induced emphysema in rats

Heterogeneity of Heparan Sulfates in Human Lung

The proteoglycan skeleton of the Kurloff body as evidenced by Cuprolinic Blue staining

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