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- Chen, Fang, et al.
(författare)
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A field study of cold effects among cold store workers in China
- 1991
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Ingår i: Arctic Medical Research. - 0782-226X. ; 50:Suppl. 6, s. 99-103
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Tidskriftsartikel (refereegranskat)abstract
- A field study was carried out among cold store workers in China. A self administrative questionnaire and health check-up were taken among 463 male workers from two different types of cold stores, all during their whole daily work. 296 men from Lower Temperature Stores (LTS), where the air temperature was between -10 to -25 degrees C, and 167 men from Ice Stores (IS), where the air temperature was between -5 and +5 degrees C participated. Another group of 152 men working in normal stores and exposed to an air temperature between 20 and 30 degrees C served as a control group. The study did not indicate any special disease attributable to the cold environment. The number of complaints of lower back pain and knee pain in the cold exposed group were significantly higher than that of the control group (in LTS: 42.3%, 46.6%; IS: 52.7%, 50.8%; control group: 9.2%, 14.5%; low back and knee pain, respectively). After 5 years of cold exposure work, the lower back and knee symptoms were very frequent. The point press pain on the knees of the cooler group (LTS) was higher than in the moderate cold group (IS). We suppose that the cold factor contributed to lower back and knee pain. 12.2% of 463 cold exposed workers had frostbite on the body extremities viz: hand, foot and ear. Self estimation of health indicated more problems among cold exposed workers (28.0%) than control group (2.7%).
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| 3. |
- Cheng, Fang, et al.
(författare)
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Patterns of uronosyl epimerization and 4-/6-O-sulphation in chondroitin/dermatan sulphate from decorin and biglycan of various bovine tissues
- 1994
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Ingår i: Glycobiology. - 1460-2423. ; 4:5, s. 685-696
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Tidskriftsartikel (refereegranskat)abstract
- Dermatan sulphate is a co-polymer of two types of disaccharide repeats: D-glucuronate-N-acetylgalactosamine and L-iduronate-N-acetylgalactosamine. The former can be O-sulphated at C-4 or C-6 of the galactosamine, whereas the latter contains almost exclusively 4-O-sulphated galactosamine. A minor proportion of the L-iduronate may be O-sulphated at C-2. Chondroitin sulphate has no L-iduronate-containing repeats. We have used our recently developed methods for sequence analysis of galactosaminoglycans to investigate the structure of dermatan/chondroitin sulphates of the proteoglycans decorin and biglycan derived from various bovine tissues, like dermis, sclera, tendon, aorta, cartilage and bone. The glycan chains, radioiodinated at the reducing end, were partially cleaved with specific enzymes (chondroitin lyases), and subjected to high-resolution polyacrylamide gel electrophoresis, blotting and autoradiography to identify fragments extending from the labelled reducing end to the point of cleavage. We used chondroitin B lyase to identify the location of L-iduronate, chondroitin AC-I lyase to locate D-glucuronate and chondroitin C lyase to cleave where D-glucuronate residues were succeeded by 6-O-sulphated N-acetylgalactosamine. We could demonstrate tissue-specific, periodic and wave-like patterns of distribution for the two epimeric uronic acids, as well as specific patterns of sulphation in dermatan sulphates derived from either decorin or biglycan. For example, some dermatan sulphates contained D-glucuronate-rich domains that were always 6-sulphated (scleral decorin), others were always 4-sulphated (decorin from bovine dermis, cartilage and bone; biglycan from aorta) or 6-sulphated near the linkage region, but 4-sulphated in more distal domains (decorin from porcine dermis and bovine tendon). Decorin from bone and articular cartilage, as well as biglycan from articular and nasal cartilage, carried largely chondroitin sulphate chains, but also some dermatan sulphate, whereas galactosaminoglycan chains derived from aggrecan of nasal cartilage were free of L-iduronate. Decorin and biglycan from the same tissue (articular cartilage or sclera) had similar glycan chains. The two side chains in a biglycan molecule are probably also similar to one another. The portion of the glycan chains nearest to the core protein was substituted with charged groups to a variable degree, which may correlate with the structural features of the main chain.
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