The proteoglycans aggrecan and Versican form networks with fibulin-2 through their lectin domain binding
Olin, Anders LU ; Mörgelin, Matthias LU ; Sasaki, Takako ; Timpl, Rupert ; Heinegård, Dick LU and Aspberg, Anders LU
(2001)
In Journal of Biological Chemistry
276(2).
p.1253-1261
- Abstract
- Aggrecan, versican, neurocan, and brevican are important components of the extracellular matrix in various tissues. Their amino-terminal globular domains bind to hyaluronan, but the function of their carboxyl-terminal globular domains has long remained elusive. A picture is now emerging where the C-type lectin motif of this domain mediates binding to other extracellular matrix proteins. We here demonstrate that aggrecan, versican, and brevican lectin domains bind fibulin-2, whereas neurocan does not. As expected for a C-type lectin, the interactions are calcium-dependent, with K(D) values in the nanomolar range as measured by surface plasmon resonance. Solid phase competition assays with previously identified ligands demonstrated that... (More)
- Aggrecan, versican, neurocan, and brevican are important components of the extracellular matrix in various tissues. Their amino-terminal globular domains bind to hyaluronan, but the function of their carboxyl-terminal globular domains has long remained elusive. A picture is now emerging where the C-type lectin motif of this domain mediates binding to other extracellular matrix proteins. We here demonstrate that aggrecan, versican, and brevican lectin domains bind fibulin-2, whereas neurocan does not. As expected for a C-type lectin, the interactions are calcium-dependent, with K(D) values in the nanomolar range as measured by surface plasmon resonance. Solid phase competition assays with previously identified ligands demonstrated that fibulin-2 and tenascin-R bind the same site on the proteoglycan lectin domains. Fibulin-1 has affinity for the common site on versican but may bind to a different site on the aggrecan lectin domain. By using deletion mutants, the interaction sites for aggrecan and versican lectin domains were mapped to epidermal growth factor-like repeats in domain II of fibulin-2. Affinity chromatography and solid phase assays confirmed that also native full-length aggrecan and versican bind the lectin domain ligands. Electron microscopy confirmed the mapping and demonstrated that hyaluronan-aggrecan complexes can be cross-linked by the fibulins. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1122282
- author
- Olin, Anders
LU
; Mörgelin, Matthias
LU
; Sasaki, Takako
; Timpl, Rupert
; Heinegård, Dick
LU
and Aspberg, Anders
LU
- organization
- publishing date
- 2001
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 276
- issue
- 2
- pages
- 1253 - 1261
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:11038354
- scopus:0035847046
- pmid:11038354
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M006783200
- 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: Connective Tissue Biology (013230151), Division of Infection Medicine (BMC) (013024020)
- id
- b691ac45-ce3e-4a7f-8be7-cfeb6a82b66e (old id 1122282)
- date added to LUP
- 2016-04-01 12:23:57
- date last changed
- 2022-04-21 06:54:17
@article{b691ac45-ce3e-4a7f-8be7-cfeb6a82b66e,
abstract = {{Aggrecan, versican, neurocan, and brevican are important components of the extracellular matrix in various tissues. Their amino-terminal globular domains bind to hyaluronan, but the function of their carboxyl-terminal globular domains has long remained elusive. A picture is now emerging where the C-type lectin motif of this domain mediates binding to other extracellular matrix proteins. We here demonstrate that aggrecan, versican, and brevican lectin domains bind fibulin-2, whereas neurocan does not. As expected for a C-type lectin, the interactions are calcium-dependent, with K(D) values in the nanomolar range as measured by surface plasmon resonance. Solid phase competition assays with previously identified ligands demonstrated that fibulin-2 and tenascin-R bind the same site on the proteoglycan lectin domains. Fibulin-1 has affinity for the common site on versican but may bind to a different site on the aggrecan lectin domain. By using deletion mutants, the interaction sites for aggrecan and versican lectin domains were mapped to epidermal growth factor-like repeats in domain II of fibulin-2. Affinity chromatography and solid phase assays confirmed that also native full-length aggrecan and versican bind the lectin domain ligands. Electron microscopy confirmed the mapping and demonstrated that hyaluronan-aggrecan complexes can be cross-linked by the fibulins.}},
author = {{Olin, Anders and Mörgelin, Matthias and Sasaki, Takako and Timpl, Rupert and Heinegård, Dick and Aspberg, Anders}},
issn = {{1083-351X}},
language = {{eng}},
number = {{2}},
pages = {{1253--1261}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{The proteoglycans aggrecan and Versican form networks with fibulin-2 through their lectin domain binding}},
url = {{http://dx.doi.org/10.1074/jbc.M006783200}},
doi = {{10.1074/jbc.M006783200}},
volume = {{276}},
year = {{2001}},
}