| 1. |
- Riise, Gerdt C., 1956, et al.
(författare)
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Circulating cell adhesion molecules in bronchial lavage and serum in COPD patients with chronic bronchitis
- 1994
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Ingår i: Eur Respir J. - 0903-1936. ; 7:9, s. 1673-1677
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Tidskriftsartikel (refereegranskat)abstract
- The initial phase of inflammation in bronchial asthma appears to be triggered by the expression of leucocyte-endothelial adhesion molecules on endothelial cell surfaces. Cell adhesion molecules (CAMs) cause adhesion of leucocytes to the endothelium prior to their subsequent extravasation into inflamed tissue. We wanted to determine whether circulating intercellular adhesion molecule-1 (cICAM-1) and circulating E-selectin (cE-selectin) could be detected in bronchial lavage fluid and serum in patients with stable chronic obstructive pulmonary disease (COPD) and chronic bronchitis. Bronchoscopy and small volume bronchial lavage was performed in 19 patients with COPD and chronic bronchitis and in 13 control subjects. We found increased mean levels of cICAM-1 both in serum (481 micrograms.l-1) and in bronchial lavage (24 micrograms.l-1) in the COPD patients as compared to the controls (321 micrograms.l-1 in serum, 15 micrograms.l-1 in lavage). We also found higher mean levels of cE-selectin in serum from the COPD patients (86 micrograms.l-1) compared to controls (50 micrograms.l-1). The serum levels of cE-selectin correlated significantly with lung function measured as forced expiratory volume in one second (FEV1) in percentage of predicted. Patients with significant intrabronchial bacterial colonization had increased levels of serum cE-selectin. Our results indicate that cCAMs may reflect an upregulation of CAMs on endothelial and epithelial airway cells in COPD.
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| 2. |
- Fransson, Lars-Åke, et al.
(författare)
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Oligosaccharide mapping of proteoglycan-bound and xyloside-initiated dermatan sulfate from fibroblasts
- 1991
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Ingår i: Glycoconjugate Journal. - 1573-4986. ; 8:2, s. 108-115
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Tidskriftsartikel (refereegranskat)abstract
- The copolymeric structure of dermatan sulfate chains synthesized by skin fibroblasts has been examined. Chains initiated onto exogeneous p-nitrophenyl-beta-D-xylopyranoside or attached to protein in a large proteoglycan, PG-L, and two small proteoglycans, PG-S1 and PG-S2, have been compared by using high resolution electrophoresis and gel chromatography of oligosaccharides generated by specific enzymatic or chemical degradations. The results confirm that chains attached to PG-L are glucuronate-rich, whereas novel findings indicate that chains attached to either of the two PG-S variants yield closely similar oligosaccharide maps, have approximately equal glucuronate and iduronate content and contain over 90% 4-sulfated disaccharide repeating units. Dermatan sulfate chains built onto xyloside at concentrations of 50 microM and below have a copolymeric structure similar to that of chains from the two PG-S variants. These findings indicate that the polymer-modifying machinery can generate chains with extended iduronate-containing repeats also when the xylose primer is not linked to core protein.
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| 3. |
- Schmidtchen, Artur, et al.
(författare)
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A fibroblast heparan sulphate proteoglycan with a 70 kDa core protein is linked to membrane phosphatidylinositol
- 1990
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Ingår i: Glycoconjugate Journal. - 1573-4986. ; 7:6, s. 563-572
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Tidskriftsartikel (refereegranskat)abstract
- Here we present evidence that a fibroblast heparan sulphate proteoglycan of approx. 300 kDa and with a core protein of apparent molecular mass 70 kDa is covalently linked to the plasma membrane via a linkage structure involving phosphatidylinositol. Phosphatidylinositol-specific phospholipase C releases such a heparan sulphate proteoglycan only from cells labelled with [35S]sulphate in the absence of serum. Cell cultures labelled with [3H]myo-inositol in the absence or presence of serum produce a radiolabelled heparan sulphate proteoglycan which was purified by gel-permeation chromatography and ion-exchange chromatography on MonoQ. Digestion with heparan sulphate lyase and analysis by gel-permeation chromatography and sodium dodecylsulphate-polyacrylamide gel-electrophoresis revealed that the 3H-label is associated with a core protein of apparent mass 70 kDa.
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| 4. |
- Flinck, A, et al.
(författare)
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Oral findings in a group of newborn Swedish children.
- 1994
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Ingår i: International Journal of Paediatric Dentistry. - 0960-7439. ; 4:2, s. 67-73
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Tidskriftsartikel (refereegranskat)abstract
- Oral examinations were performed of 1021 newborn Swedish children, of whom 101 were re-examined after 2-3 or 4-5 months. The most common findings, registered in 74.9% of the children, were of oral mucosal cysts situated either palatally or on the alveolar ridges. The majority of the palatal cysts disappeared shortly after birth, and some alveolar cysts appeared after birth. Ankyloglossia was found in 2.5% of the children, and Fordyce spots in 1.0%. No natal teeth were found. The upper labial frenum was attached to the crest of the alveolar ridge in 76.7% of the children, palatally in 16.7% and buccally in 6.7%. The relationship of the alveolar ridges was recorded: the anterior segment of the mandibular ridge was distal to the maxillary in 99% of cases, and, posteriorly, the mandibular ridges were lingual to the maxillary in 97.6%. An open bite was found in 39.8% of the children.
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| 5. |
- Schmidtchen, Artur, et al.
(författare)
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Analysis of glycosaminoglycan chains from different proteoglycan populations in human embryonic skin fibroblasts
- 1992
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Ingår i: European Journal of Biochemistry. - : Wiley. - 0014-2956 .- 1432-1033. ; 208:2, s. 537-546
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Tidskriftsartikel (refereegranskat)abstract
- 1. The structure of chondroitin/dermatan and heparan-sulphate chains from various proteoglycan populations derived from cultured human skin fibroblasts have been examined. Confluent cell cultures were biosynthetically labelled with [3H]-glucosamine and 35SO4(2-), and proteoglycans were purified according to buoyant density, size and charge density [Schmidtchen, A., Carlstedt, I., Malmstrom, A. & Fransson, L.-A. (1990) Biochem. J. 265, 289-300]. Some proteoglycan fractions were further fractionated according to hydrophobicity on octyl-Sepharose in Triton X-100 gradients. The glycosaminoglycan chains, intact or degraded by chemical or enzymic methods were then analysed by gel chromatography on Sepharose CL-6B, Bio-Gel P-6, ion exchange HPLC and gel electrophoresis. 2. Three types of dermatan-sulphate chains were identified on the basis of disaccharide composition and chain length. They were derived from the large proteoglycan, two small proteoglycans and a cell-associated proteoglycan with core proteins of 90 kDa and 45 kDa. Intracellular, free dermatan-sulphate chains were very similar to those of the small proteoglycans. 3. Heparan-sulphate chains from different proteoglycans had, in spite of small but distinct differences in size, strikingly similar compositional features. They contained similar amounts of D-glucuronate, L-iduronate (with or without sulphate) and N-sulphate groups. They all displayed heparin-lyase-resistant domains with average molecular mass of 10-15 kDa. The heparan-sulphate chains from proteoglycans with 250-kDa and 350-kDa cores were the largest greater than 50 kDa), containing an average of four or five domains, in contrast to heparan-sulphate chains from the small heparan-sulphate proteoglycans which had average molecular mass of 45 kDa and consisted of three or four such domains. Free, cell-associated heparan-sulphate chains were heterogeneous in size (5-45 kDa). 4. These results suggest that the core protein may have important regulatory functions with regard to dermatan-sulphate synthesis. On the other hand, synthesis of heparan sulphate may be largely controlled by the cell that expresses a particular proteoglycan core protein.
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| 6. |
- Schmidtchen, Artur, et al.
(författare)
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Analysis of heparan-sulphate chains and oligosaccharides from proliferating and quiescent fibroblasts. A proposed model for endoheparanase activity
- 1994
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Ingår i: European Journal of Biochemistry. - : Wiley. - 0014-2956 .- 1432-1033. ; 223:1, s. 211-221
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Tidskriftsartikel (refereegranskat)abstract
- Human skin fibroblasts in different growth states were incubated with [3H]glucosamine and/or Na(2)35SO4 and extracted with Triton X-100 for various periods of time. Free heparan-sulphate oligosaccharides and protein-bound heparan-sulphate chains were separated by chromatography on octyl-Sepharose and analyzed. A pool of endogenously produced oligosaccharides, present in the cultured cells and isolated after brief extraction, contained fragments of uniform size (approximately 7-10 kDa corresponding to approximately 14-20 disaccharides). Analysis by heparinase I and heparinase III degradations followed by electrophoretic separation (oligosaccharide mapping) showed that the oligosaccharides were rich in glucuronic acid but had a few sulphated iduronic acid residues at the periphery of each molecule. These results indicated that endoheparanase cleavage points were located close to linkages between N-sulphated glucosamine and sulphated iduronic acid, generating fragments that comprise a major portion of the unmodified segments and a minor portion of the highly modified segments. Prolonged extraction (24-48 h) of cells with Triton X-100 at 4 degrees C in the presence of proteinase inhibitors resulted in further degradation. There was an increase in the amount of heparan-sulphate oligosaccharides and a concomitant decrease in the amount of protein-bound heparan-sulphate chains present in the same extract. The heparan-sulphate oligosaccharides obtained after prolonged extraction were more heterogeneous in size comprising, in addition to the major species of approximately 7-10 kDa, intermediate and larger fragments of approximately 17 kDa and 30-40 kDa. This observation suggests that endoheparanase acted at periodically appearing, specific regions in the intact heparan-sulphate chain. Furthermore, the enzyme and substrate should remain closely associated during cold Triton X-100 extraction. To determine if the endogenously produced heparan-sulphate oligosaccharides were derived from a particular heparan-sulphate species degraded during the growth phase, proteoglycan-derived heparan-sulphate chains obtained from proliferating or quiescent fibroblasts were also examined. These chains showed similar oligosaccharide maps, except for a small increase in the amount of glucuronic acid as cell growth was arrested. Hence, an endoheparanase with restricted specificity may generate slightly different oligosaccharides in the various growth states.
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| 7. |
- Schmidtchen, Artur, et al.
(författare)
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Hydrophobic interaction chromatography of fibroblast proteoglycans
- 1993
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Ingår i: Biomedical Chromatography. - : Wiley. - 0269-3879 .- 1099-0801. ; 7:1, s. 48-55
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Forskningsöversikt (refereegranskat)abstract
- We have investigated the hydrophobic properties of human skin fibroblast proteoglycans and related material by affinity chromatography on Octyl-Sepharose CL-4B in 4 M guanidinium hydrochloride (GdnHCl). Proteoglycans and related material could be separated into non-, medium and highly hydrophobic forms by elution with gradients of Triton X-100 in 4 M Gdn HCl. The non-hydrophobic material included endogenously produced glycosaminoglycan chains and oligosaccharides as well as an HS-proteoglycan with a 35 kDa core. The 65-70 kDa core (glypican-related) proteoglycans appeared among the highly hydrophobic ones, but variable proportions were seen both in the medium and the non-hydrophobic material. Other membrane-bound proteoglycans, like fibroglycan (45 kDa core) and the HS-proteoglycans with 90 and 130 kDa cores, as well as the CS/DS-proteoglycan with a 90 kDa core, were all of high hydrophobicity. There were also indications of a highly hydrophobic CS/DS-proteoglycan with a 45 kDa core. The extracellular proteoglycans, PG-L, PG-S1 and PG-S2, and the HS-proteoglycans with 350 and 250 kDa cores were all of medium hydrophobicity. These proteoglycans emerged in distinct positions when the column was eluted with a gradient of 3-[(3-cholamidopropyl)dimethylammonio]propanesulphonate.
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| 8. |
- Bendsöe, Niels, et al.
(författare)
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Inflammatory reactions from organic pigments in red tattoos
- 1991
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Ingår i: Acta Dermato-Venereologica. - 1651-2057. ; 71:1, s. 70-73
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Tidskriftsartikel (refereegranskat)abstract
- Two different red pigments used for tattooing were found to give rise to inflammatory reactions in the skin. No inorganic component was found in the pigments. NMR and MS analyses elucidated the molecular structures of two different organic compounds. A bright red pigment was found to be an aromatic azo-derivative, and a red-violet pigment was found to be linear quinacridone. A strong exposure to UV-light was reported in most cases prior to the onset of the inflammation.
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| 9. |
- Bergendorff, Ola, et al.
(författare)
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Airborne contact dermatitis from formaldehyde released from heated plastic polymers.
- 1994
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Ingår i: American Journal of Contact Dermatitis. - 1532-8163. ; 5:4, s. 223-225
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Tidskriftsartikel (refereegranskat)abstract
- A 55-year-old woman developed an airborne dermatitis on her face. Patch testing was performed and showed positive reactions to formaldehyde, thiuram mix, carba mix, and nickel sulphate. She operated a machine at work in which polyacetal granules were heated. The presence of formaldehyde in the pyrolysis smoke from the polymer was confirmed by chemical analysis.
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| 10. |
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