Advanced

The cartilage proteoglycan aggregate: assembly through combined protein-carbohydrate and protein-protein interactions

Mörgelin, Matthias LU ; Heinegård, Dick LU ; Engel, Jürgen and Paulsson, Mats (1994) In Biophysical Chemistry 50(1-2). p.113-128
Abstract
In vitro reassembled aggregates of cartilage proteoglycan (aggrecan) were studied by glycerol spraying/rotary shadowing electron microscopy and compared to the corresponding native (i.e. never dissociated) structures. In both cases a tightly packed central filament structure was observed consisting of the hyaluronate binding region (HABR) of the proteoglycan, link protein (LP) and hyaluronate (HA). This differs from earlier results where a discontinuous central filament structure was seen after spreading proteoglycan aggregates at a water/air interphase. Binding of isolated HABR to HA is random but upon addition of link protein a clustering of the HA-binding proteins is observed, indicating a cooperativity. In a fully saturated aggregate... (More)
In vitro reassembled aggregates of cartilage proteoglycan (aggrecan) were studied by glycerol spraying/rotary shadowing electron microscopy and compared to the corresponding native (i.e. never dissociated) structures. In both cases a tightly packed central filament structure was observed consisting of the hyaluronate binding region (HABR) of the proteoglycan, link protein (LP) and hyaluronate (HA). This differs from earlier results where a discontinuous central filament structure was seen after spreading proteoglycan aggregates at a water/air interphase. Binding of isolated HABR to HA is random but upon addition of link protein a clustering of the HA-binding proteins is observed, indicating a cooperativity. In a fully saturated aggregate the HA is covered by a continuous protein shell consisting of HABR and LP. When added in amounts below saturation HABR and LP bind to the HA in clusters which are interrupted by free strands of HA. The proteoglycan aggregate is thus an example for a structure where a polysaccharide forms a template for a supramolecular assembly largely stabilized by protein-protein interactions. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Aggrecan, Hyaluronate, Link protein, Electron microscopy, Cartilage, Swarm rat chondrosarcoma
in
Biophysical Chemistry
volume
50
issue
1-2
pages
113 - 128
publisher
Elsevier
external identifiers
  • pmid:8011926
  • scopus:0028314130
ISSN
1873-4200
DOI
10.1016/0301-4622(94)85024-0
language
English
LU publication?
yes
id
81cbc945-352d-46ae-ac66-3db9325fee8a (old id 1108345)
date added to LUP
2008-07-23 17:30:19
date last changed
2017-07-30 04:36:19
@article{81cbc945-352d-46ae-ac66-3db9325fee8a,
  abstract     = {In vitro reassembled aggregates of cartilage proteoglycan (aggrecan) were studied by glycerol spraying/rotary shadowing electron microscopy and compared to the corresponding native (i.e. never dissociated) structures. In both cases a tightly packed central filament structure was observed consisting of the hyaluronate binding region (HABR) of the proteoglycan, link protein (LP) and hyaluronate (HA). This differs from earlier results where a discontinuous central filament structure was seen after spreading proteoglycan aggregates at a water/air interphase. Binding of isolated HABR to HA is random but upon addition of link protein a clustering of the HA-binding proteins is observed, indicating a cooperativity. In a fully saturated aggregate the HA is covered by a continuous protein shell consisting of HABR and LP. When added in amounts below saturation HABR and LP bind to the HA in clusters which are interrupted by free strands of HA. The proteoglycan aggregate is thus an example for a structure where a polysaccharide forms a template for a supramolecular assembly largely stabilized by protein-protein interactions.},
  author       = {Mörgelin, Matthias and Heinegård, Dick and Engel, Jürgen and Paulsson, Mats},
  issn         = {1873-4200},
  keyword      = {Aggrecan,Hyaluronate,Link protein,Electron microscopy,Cartilage,Swarm rat chondrosarcoma},
  language     = {eng},
  number       = {1-2},
  pages        = {113--128},
  publisher    = {Elsevier},
  series       = {Biophysical Chemistry},
  title        = {The cartilage proteoglycan aggregate: assembly through combined protein-carbohydrate and protein-protein interactions},
  url          = {http://dx.doi.org/10.1016/0301-4622(94)85024-0},
  volume       = {50},
  year         = {1994},
}