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Production of cartilage-typic proteoglycans in cultures of chondrocytes from elastic cartilage

Madsen, Kjell and Lohmander, Stefan LU orcid (1979) In Archives of Biochemistry and Biophysics 196(1). p.192-198
Abstract

Chondrocytes from rabbit ear cartilage were isolated and cultured as monolayers in Ham's F-12 medium. The proteoglycans synthesized by short-term cultures formed a high proportion of aggregates and contained chrondroitin-4- and -6-sulfate in a 2:1 proportion. Dermatan sulfate was not present. The average molecular weight of the chondroitin sulfate was about 20,000. Keratan sulfate with an average molecular weight of about 6000 could be isolated from the proteoglycan monomers. Rabbit ear chondrocytes in culture thus produced proteoglycans comparable to those isolated from hyaline cartilage. Culture for longer periods and plating at lower density caused a decrease in the proportion of aggregated proteoglycans. Primary cultures continued... (More)

Chondrocytes from rabbit ear cartilage were isolated and cultured as monolayers in Ham's F-12 medium. The proteoglycans synthesized by short-term cultures formed a high proportion of aggregates and contained chrondroitin-4- and -6-sulfate in a 2:1 proportion. Dermatan sulfate was not present. The average molecular weight of the chondroitin sulfate was about 20,000. Keratan sulfate with an average molecular weight of about 6000 could be isolated from the proteoglycan monomers. Rabbit ear chondrocytes in culture thus produced proteoglycans comparable to those isolated from hyaline cartilage. Culture for longer periods and plating at lower density caused a decrease in the proportion of aggregated proteoglycans. Primary cultures continued to synthesize aggregated proteoglycans for at least 2 weeks, while subdivision of the cultures caused a shift toward the production of small-sized "ubiquitous proteoglycans." The synthesis of proteoglycan aggregates could, however, be partly restored by transfer of the monolayer cells to a suspension culture.

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publication status
published
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in
Archives of Biochemistry and Biophysics
volume
196
issue
1
pages
7 pages
publisher
Academic Press
external identifiers
  • pmid:507804
  • scopus:0018733371
ISSN
0003-9861
DOI
10.1016/0003-9861(79)90566-6
language
English
LU publication?
yes
id
b32ba94c-bfbb-4b58-8ff8-7101a8722ce1
date added to LUP
2016-05-04 12:49:08
date last changed
2024-01-04 02:40:17
@article{b32ba94c-bfbb-4b58-8ff8-7101a8722ce1,
  abstract     = {{<p>Chondrocytes from rabbit ear cartilage were isolated and cultured as monolayers in Ham's F-12 medium. The proteoglycans synthesized by short-term cultures formed a high proportion of aggregates and contained chrondroitin-4- and -6-sulfate in a 2:1 proportion. Dermatan sulfate was not present. The average molecular weight of the chondroitin sulfate was about 20,000. Keratan sulfate with an average molecular weight of about 6000 could be isolated from the proteoglycan monomers. Rabbit ear chondrocytes in culture thus produced proteoglycans comparable to those isolated from hyaline cartilage. Culture for longer periods and plating at lower density caused a decrease in the proportion of aggregated proteoglycans. Primary cultures continued to synthesize aggregated proteoglycans for at least 2 weeks, while subdivision of the cultures caused a shift toward the production of small-sized "ubiquitous proteoglycans." The synthesis of proteoglycan aggregates could, however, be partly restored by transfer of the monolayer cells to a suspension culture.</p>}},
  author       = {{Madsen, Kjell and Lohmander, Stefan}},
  issn         = {{0003-9861}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{192--198}},
  publisher    = {{Academic Press}},
  series       = {{Archives of Biochemistry and Biophysics}},
  title        = {{Production of cartilage-typic proteoglycans in cultures of chondrocytes from elastic cartilage}},
  url          = {{http://dx.doi.org/10.1016/0003-9861(79)90566-6}},
  doi          = {{10.1016/0003-9861(79)90566-6}},
  volume       = {{196}},
  year         = {{1979}},
}