Structure and synthesis of intracellular proteoglycan in HL-60 human leukemic promyelocytes
(1990) In Journal of Biological Chemistry 265(10). p.5802-5808- Abstract
The structure, biosynthesis, and metabolism of proteoglycans in the HL-60 human promyelocytes were studied by metabolic labeling in culture with [35S]sulfate, [3H]glucosamine, [3H]serine, and [3H]leucine. These cells synthesize a single predominant species of intracellular proteoglycan with an approximate molecular weight of 100,000. The cells contain about 1 μg of proteoglycan/million cells. The proteoglycan is turned over within the cells in two apparent pools with half-lives of about 0.6 and 27 h, respectively. The fast pool represents secretion into medium in an apparently intact form, whereas the slow pool represents intracellular degradation to free chondroitin sulfate chains and smaller... (More)
The structure, biosynthesis, and metabolism of proteoglycans in the HL-60 human promyelocytes were studied by metabolic labeling in culture with [35S]sulfate, [3H]glucosamine, [3H]serine, and [3H]leucine. These cells synthesize a single predominant species of intracellular proteoglycan with an approximate molecular weight of 100,000. The cells contain about 1 μg of proteoglycan/million cells. The proteoglycan is turned over within the cells in two apparent pools with half-lives of about 0.6 and 27 h, respectively. The fast pool represents secretion into medium in an apparently intact form, whereas the slow pool represents intracellular degradation to free chondroitin sulfate chains and smaller fragments. The proteoglycan contains a protein core with an apparent Mr on gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis of about 20,000-30,000. To the core protein are attached an average of six or seven chondroitin sulfate chains, each with an Mr of about 10,000. The chondroitin sulfate chains contain ∼85% 4-sulfated and ∼15% nonsulfated disaccharides. The chondroitin sulfate attachment region of the core protein is essentially resistant to trypsin and elastase, whereas the remainder of the protein core is readily degraded by proteases. The size of the chondroitin sulfate attachment region peptide generated by trypsin was estimated to be ∼5 kDa. Based on the molecular size, distribution of amino acids, protease susceptibility, and the extent of O-glycosylation, we propose that the intracellular proteoglycan characterized in this study is the translation product of a proteoglycan gene reported to be present in these cells
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- author
- Stefan Lohmander, L. ; Arnljots, Kristina LU and Yanagishita, Masaki
- organization
- publishing date
- 1990
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- leukemic, proteoglycans
- in
- Journal of Biological Chemistry
- volume
- 265
- issue
- 10
- pages
- 7 pages
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- scopus:0025265152
- pmid:2108148
- ISSN
- 0021-9258
- language
- English
- LU publication?
- yes
- id
- 7ac8a86c-0215-4e45-b12d-7d4d5d09c4c4
- date added to LUP
- 2016-05-04 18:15:06
- date last changed
- 2024-01-04 02:47:14
@article{7ac8a86c-0215-4e45-b12d-7d4d5d09c4c4, abstract = {{<p>The structure, biosynthesis, and metabolism of proteoglycans in the HL-60 human promyelocytes were studied by metabolic labeling in culture with [<sup>35</sup>S]sulfate, [<sup>3</sup>H]glucosamine, [<sup>3</sup>H]serine, and [<sup>3</sup>H]leucine. These cells synthesize a single predominant species of intracellular proteoglycan with an approximate molecular weight of 100,000. The cells contain about 1 μg of proteoglycan/million cells. The proteoglycan is turned over within the cells in two apparent pools with half-lives of about 0.6 and 27 h, respectively. The fast pool represents secretion into medium in an apparently intact form, whereas the slow pool represents intracellular degradation to free chondroitin sulfate chains and smaller fragments. The proteoglycan contains a protein core with an apparent M<sub>r</sub> on gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis of about 20,000-30,000. To the core protein are attached an average of six or seven chondroitin sulfate chains, each with an Mr of about 10,000. The chondroitin sulfate chains contain ∼85% 4-sulfated and ∼15% nonsulfated disaccharides. The chondroitin sulfate attachment region of the core protein is essentially resistant to trypsin and elastase, whereas the remainder of the protein core is readily degraded by proteases. The size of the chondroitin sulfate attachment region peptide generated by trypsin was estimated to be ∼5 kDa. Based on the molecular size, distribution of amino acids, protease susceptibility, and the extent of O-glycosylation, we propose that the intracellular proteoglycan characterized in this study is the translation product of a proteoglycan gene reported to be present in these cells </p>}}, author = {{Stefan Lohmander, L. and Arnljots, Kristina and Yanagishita, Masaki}}, issn = {{0021-9258}}, keywords = {{leukemic; proteoglycans}}, language = {{eng}}, number = {{10}}, pages = {{5802--5808}}, publisher = {{American Society for Biochemistry and Molecular Biology}}, series = {{Journal of Biological Chemistry}}, title = {{Structure and synthesis of intracellular proteoglycan in HL-60 human leukemic promyelocytes}}, volume = {{265}}, year = {{1990}}, }