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Shared and distinct structural features of interstitial proteoglycans from different bovine tissues revealed by electron microscopy

Mörgelin, Matthias LU ; Paulsson, Mats; Malmström, Anders LU and Heinegård, Dick LU (1989) In Journal of Biological Chemistry 264(20). p.12080-12090
Abstract
Large and small interstitial proteoglycans were purified from different bovine tissues, i.e. cartilage, sclera, tendon, aorta, cornea, and bone. The structure of the molecules was compared using the glycerol spraying/rotary shadowing technique for electron microscopy. Large proteoglycans from sclera and tendon have a core protein with a domain structure similar to that previously reported for cartilage proteoglycans (Paulsson, M., Morgelin, M., Wiedemann, H., Beardmore-Gray, M., Dunham, D., Hardingham, T., Heinegard, D., Timpl, R., and Engel, J. (1987) Biochem. J. 245, 763-772). It is comprised of a pair of globules at one end of the molecule, connected by a short extended segment, followed by a long extended domain which is terminated by... (More)
Large and small interstitial proteoglycans were purified from different bovine tissues, i.e. cartilage, sclera, tendon, aorta, cornea, and bone. The structure of the molecules was compared using the glycerol spraying/rotary shadowing technique for electron microscopy. Large proteoglycans from sclera and tendon have a core protein with a domain structure similar to that previously reported for cartilage proteoglycans (Paulsson, M., Morgelin, M., Wiedemann, H., Beardmore-Gray, M., Dunham, D., Hardingham, T., Heinegard, D., Timpl, R., and Engel, J. (1987) Biochem. J. 245, 763-772). It is comprised of a pair of globules at one end of the molecule, connected by a short extended segment, followed by a long extended domain which is terminated by a third globular domain. Large aorta proteoglycans show a somewhat different structure, with only one globular domain at each end of a long extended segment. Large sclera and aorta proteoglycans form aggregates with hyaluronate and cartilage link protein in a manner similar to that of large cartilage proteoglycans. The large proteoglycans show considerable tissue variability with regard to number, length, and spacing of glycosaminoglycan side chains. The small proteoglycans reveal a small globular core protein to which one or two glycosaminoglycans are attached. Although the main structural features do not differ, proteoglycans of the S1 class have an average glycosylation close to two glycosaminoglycans/molecule, while that of the S2 class is close to one. Differences in glycosaminoglycan length were observed between tissues and between the S1 and S2 class of proteoglycan derived from a single tissue. (Less)
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author
organization
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Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
264
issue
20
pages
12080 - 12090
publisher
ASBMB
external identifiers
  • pmid:2745430
  • scopus:0024351961
ISSN
1083-351X
language
English
LU publication?
yes
id
e78a0e77-df10-4e01-89a2-a13dc3627da4 (old id 1104705)
alternative location
http://www.jbc.org/cgi/reprint/264/20/12080
date added to LUP
2008-08-06 13:46:15
date last changed
2017-08-27 04:15:42
@article{e78a0e77-df10-4e01-89a2-a13dc3627da4,
  abstract     = {Large and small interstitial proteoglycans were purified from different bovine tissues, i.e. cartilage, sclera, tendon, aorta, cornea, and bone. The structure of the molecules was compared using the glycerol spraying/rotary shadowing technique for electron microscopy. Large proteoglycans from sclera and tendon have a core protein with a domain structure similar to that previously reported for cartilage proteoglycans (Paulsson, M., Morgelin, M., Wiedemann, H., Beardmore-Gray, M., Dunham, D., Hardingham, T., Heinegard, D., Timpl, R., and Engel, J. (1987) Biochem. J. 245, 763-772). It is comprised of a pair of globules at one end of the molecule, connected by a short extended segment, followed by a long extended domain which is terminated by a third globular domain. Large aorta proteoglycans show a somewhat different structure, with only one globular domain at each end of a long extended segment. Large sclera and aorta proteoglycans form aggregates with hyaluronate and cartilage link protein in a manner similar to that of large cartilage proteoglycans. The large proteoglycans show considerable tissue variability with regard to number, length, and spacing of glycosaminoglycan side chains. The small proteoglycans reveal a small globular core protein to which one or two glycosaminoglycans are attached. Although the main structural features do not differ, proteoglycans of the S1 class have an average glycosylation close to two glycosaminoglycans/molecule, while that of the S2 class is close to one. Differences in glycosaminoglycan length were observed between tissues and between the S1 and S2 class of proteoglycan derived from a single tissue.},
  author       = {Mörgelin, Matthias and Paulsson, Mats and Malmström, Anders and Heinegård, Dick},
  issn         = {1083-351X},
  language     = {eng},
  number       = {20},
  pages        = {12080--12090},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Shared and distinct structural features of interstitial proteoglycans from different bovine tissues revealed by electron microscopy},
  volume       = {264},
  year         = {1989},
}