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Proteoglycans from the swarm rat chondrosarcoma. Structure of the aggregates extracted with associative and dissociative solvents as revealed by electron microscopy

Mörgelin, Matthias LU ; Engel, Jürgen; Heinegård, Dick LU and Paulsson, Mats (1992) In Journal of Biological Chemistry 267(20). p.14275-14284
Abstract
Proteoglycan aggregates were extracted from Swarm rat chondrosarcoma tissue in the native state and compared with proteoglycan aggregates isolated dissociatively with 4 M guanidine HCl. Purified aggregates were examined with a variety of electron microscopic techniques. In some cases they showed a structure of the central filament identical to that of the link-stabilized central filament observed in earlier experiments where the separated constituents were allowed to reconstitute (Morgelin, M., Paulsson, M., Hardingham, T. E., Heinegard, D., and Engel, J. (1988) Biochem. J. 253, 175-185). The tight packing of proteoglycan monomers along the hyaluronate with a minimum distance of 12 nm between adjacent E1 strands also could thus be... (More)
Proteoglycan aggregates were extracted from Swarm rat chondrosarcoma tissue in the native state and compared with proteoglycan aggregates isolated dissociatively with 4 M guanidine HCl. Purified aggregates were examined with a variety of electron microscopic techniques. In some cases they showed a structure of the central filament identical to that of the link-stabilized central filament observed in earlier experiments where the separated constituents were allowed to reconstitute (Morgelin, M., Paulsson, M., Hardingham, T. E., Heinegard, D., and Engel, J. (1988) Biochem. J. 253, 175-185). The tight packing of proteoglycan monomers along the hyaluronate with a minimum distance of 12 nm between adjacent E1 strands also could thus be confirmed for never dissociated aggregates. The results therefore show that the organization of proteoglycan aggregates assembled in vitro from the participating molecules is representative for conditions in situ. An additional structural type of central filament was observed in the preparations. This contained long stretches of free hyaluronate interspaced by short stretches of central filament with condensed arrays of link protein-proteoglycan. Chemical cross-linking in combination with low shear electron microscopical techniques showed that this discontinuous central filament structure is not an artifact of specimen preparation. The addition of suprastoichiometric amounts of exogenous link protein did not affect the central filament structure with the low packing density. Densely and loosely packed types of central filament were isolated in varying relative amounts with different associative and dissociative solvents. (Less)
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Contribution to journal
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published
subject
in
Journal of Biological Chemistry
volume
267
issue
20
pages
14275 - 14284
publisher
ASBMB
external identifiers
  • pmid:1629221
  • scopus:0026766682
ISSN
1083-351X
language
English
LU publication?
yes
id
3ccaa87c-1f6c-4aaf-873e-239972936bf3 (old id 1106684)
alternative location
http://www.jbc.org/cgi/reprint/267/20/14275
date added to LUP
2008-08-08 13:54:39
date last changed
2017-07-30 03:38:26
@article{3ccaa87c-1f6c-4aaf-873e-239972936bf3,
  abstract     = {Proteoglycan aggregates were extracted from Swarm rat chondrosarcoma tissue in the native state and compared with proteoglycan aggregates isolated dissociatively with 4 M guanidine HCl. Purified aggregates were examined with a variety of electron microscopic techniques. In some cases they showed a structure of the central filament identical to that of the link-stabilized central filament observed in earlier experiments where the separated constituents were allowed to reconstitute (Morgelin, M., Paulsson, M., Hardingham, T. E., Heinegard, D., and Engel, J. (1988) Biochem. J. 253, 175-185). The tight packing of proteoglycan monomers along the hyaluronate with a minimum distance of 12 nm between adjacent E1 strands also could thus be confirmed for never dissociated aggregates. The results therefore show that the organization of proteoglycan aggregates assembled in vitro from the participating molecules is representative for conditions in situ. An additional structural type of central filament was observed in the preparations. This contained long stretches of free hyaluronate interspaced by short stretches of central filament with condensed arrays of link protein-proteoglycan. Chemical cross-linking in combination with low shear electron microscopical techniques showed that this discontinuous central filament structure is not an artifact of specimen preparation. The addition of suprastoichiometric amounts of exogenous link protein did not affect the central filament structure with the low packing density. Densely and loosely packed types of central filament were isolated in varying relative amounts with different associative and dissociative solvents.},
  author       = {Mörgelin, Matthias and Engel, Jürgen and Heinegård, Dick and Paulsson, Mats},
  issn         = {1083-351X},
  language     = {eng},
  number       = {20},
  pages        = {14275--14284},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Proteoglycans from the swarm rat chondrosarcoma. Structure of the aggregates extracted with associative and dissociative solvents as revealed by electron microscopy},
  volume       = {267},
  year         = {1992},
}