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Variability in the G3 domain content of bovine aggrecan from cartilage extracts and chondrocyte cultures

Flannery, Carl; Stanescu, Victor; Mörgelin, Matthias LU ; Boynton, Raymond; Gordy, John and Sandy, John (1992) In Archives of Biochemistry and Biophysics 297(1). p.52-60
Abstract
The content of the globular domains G1, G2 and G3 on the core protein of high-density (A1D1) aggrecan isolated from newborn and mature bovine cartilage and from cultures of bovine chondrocytes was examined. Quantitation based on the 220 nm absorbance of tryptic marker peptides from each domain isolated by reversed-phase HPLC showed that while the content of G1 and G2 was essentially the same for all samples, the content of G3 varied markedly. The molar yield of G3 and G1 marker peptides indicated that approximately 55% of the G1-bearing aggrecan from immature cartilage carried the G3 domain, while for mature cartilage this figure was markedly reduced, at about 35%. Aggrecan prepared from the cell layer matrix of calf chondrocyte cultures... (More)
The content of the globular domains G1, G2 and G3 on the core protein of high-density (A1D1) aggrecan isolated from newborn and mature bovine cartilage and from cultures of bovine chondrocytes was examined. Quantitation based on the 220 nm absorbance of tryptic marker peptides from each domain isolated by reversed-phase HPLC showed that while the content of G1 and G2 was essentially the same for all samples, the content of G3 varied markedly. The molar yield of G3 and G1 marker peptides indicated that approximately 55% of the G1-bearing aggrecan from immature cartilage carried the G3 domain, while for mature cartilage this figure was markedly reduced, at about 35%. Aggrecan prepared from the cell layer matrix of calf chondrocyte cultures had an apparent G3 content similar to newborn cartilage (55%), whereas aggrecan prepared from the medium of these cultures had a markedly higher G3 content, at about 80%. The high content of G3 in cell medium samples compared to cartilage extracts was supported by electron microscopic analysis of A1D1 preparations. The G3 content of the two subpopulations of aggrecan present in mature cartilage and separable by flat bed agarose gel electrophoresis was also determined at about 45% (Band I) and 20% (Band II) respectively. These results are discussed in terms of the likely origin of the marked variability in the G3 domain content of aggrecan. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
in
Archives of Biochemistry and Biophysics
volume
297
issue
1
pages
52 - 60
publisher
Academic Press
external identifiers
  • pmid:1637183
  • scopus:0026726696
ISSN
0003-9861
DOI
10.1016/0003-9861(92)90640-I
language
English
LU publication?
no
id
2a2134a6-0afd-490a-8128-835d32210196 (old id 1106691)
date added to LUP
2008-08-01 14:30:24
date last changed
2017-08-27 04:08:54
@article{2a2134a6-0afd-490a-8128-835d32210196,
  abstract     = {The content of the globular domains G1, G2 and G3 on the core protein of high-density (A1D1) aggrecan isolated from newborn and mature bovine cartilage and from cultures of bovine chondrocytes was examined. Quantitation based on the 220 nm absorbance of tryptic marker peptides from each domain isolated by reversed-phase HPLC showed that while the content of G1 and G2 was essentially the same for all samples, the content of G3 varied markedly. The molar yield of G3 and G1 marker peptides indicated that approximately 55% of the G1-bearing aggrecan from immature cartilage carried the G3 domain, while for mature cartilage this figure was markedly reduced, at about 35%. Aggrecan prepared from the cell layer matrix of calf chondrocyte cultures had an apparent G3 content similar to newborn cartilage (55%), whereas aggrecan prepared from the medium of these cultures had a markedly higher G3 content, at about 80%. The high content of G3 in cell medium samples compared to cartilage extracts was supported by electron microscopic analysis of A1D1 preparations. The G3 content of the two subpopulations of aggrecan present in mature cartilage and separable by flat bed agarose gel electrophoresis was also determined at about 45% (Band I) and 20% (Band II) respectively. These results are discussed in terms of the likely origin of the marked variability in the G3 domain content of aggrecan.},
  author       = {Flannery, Carl and Stanescu, Victor and Mörgelin, Matthias and Boynton, Raymond and Gordy, John and Sandy, John},
  issn         = {0003-9861},
  language     = {eng},
  number       = {1},
  pages        = {52--60},
  publisher    = {Academic Press},
  series       = {Archives of Biochemistry and Biophysics},
  title        = {Variability in the G3 domain content of bovine aggrecan from cartilage extracts and chondrocyte cultures},
  url          = {http://dx.doi.org/10.1016/0003-9861(92)90640-I},
  volume       = {297},
  year         = {1992},
}