Variability in the G3 domain content of bovine aggrecan from cartilage extracts and chondrocyte cultures
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1106691
- author
- Flannery, Carl ; Stanescu, Victor ; Mörgelin, Matthias LU ; Boynton, Raymond ; Gordy, John and Sandy, John
- publishing date
- 1992
- 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
- 2016-04-01 12:11:44
- date last changed
- 2021-01-03 09:07:12
@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}},
doi = {{10.1016/0003-9861(92)90640-I}},
volume = {{297}},
year = {{1992}},
}