The cartilage proteoglycan aggregate: assembly through combined protein-carbohydrate and protein-protein interactions
(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:
https://lup.lub.lu.se/record/1108345
- author
- Mörgelin, Matthias LU ; Heinegård, Dick LU ; Engel, Jürgen and Paulsson, Mats
- organization
- publishing date
- 1994
- 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
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Division of Infection Medicine (BMC) (013024020), Connective Tissue Biology (013230151)
- id
- 81cbc945-352d-46ae-ac66-3db9325fee8a (old id 1108345)
- date added to LUP
- 2016-04-01 16:21:45
- date last changed
- 2021-06-06 05:07:30
@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}}, keywords = {{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}}, doi = {{10.1016/0301-4622(94)85024-0}}, volume = {{50}}, year = {{1994}}, }