Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and versican
Aspberg, Anders LU
; Adam, S
; Kostka, G
; Timpl, R
and Heinegård, Dick
LU
(1999)
In Journal of Biological Chemistry
274(29).
p.20444-20449
- Abstract
- The aggregating proteoglycans (aggrecan, versican, neurocan, and brevican) are important components of many extracellular matrices. Their N-terminal globular domain binds to hyaluronan, but the function of their C-terminal region containing a C-type lectin domain is less clear. We now report that a 90-kDa protein copurifies with recombinant lectin domains from aggrecan and versican, but not from the brain-specific neurocan and brevican. Amino acid sequencing of tryptic peptides from this protein identified it as fibulin-1. This extracellular matrix glycoprotein is strongly expressed in tissues where versican is expressed (blood vessels, skin, and developing heart), and also expressed in developing cartilage and bone. It is thus likely to... (More)
- The aggregating proteoglycans (aggrecan, versican, neurocan, and brevican) are important components of many extracellular matrices. Their N-terminal globular domain binds to hyaluronan, but the function of their C-terminal region containing a C-type lectin domain is less clear. We now report that a 90-kDa protein copurifies with recombinant lectin domains from aggrecan and versican, but not from the brain-specific neurocan and brevican. Amino acid sequencing of tryptic peptides from this protein identified it as fibulin-1. This extracellular matrix glycoprotein is strongly expressed in tissues where versican is expressed (blood vessels, skin, and developing heart), and also expressed in developing cartilage and bone. It is thus likely to interact with these proteoglycans in vivo. Surface plasmon resonance measurements confirmed that aggrecan and versican lectin domains bind fibulin-1, whereas brevican and neurocan do not. As expected for a C-type lectin, the interactions with fibulin-1 are Ca2+-dependent, with KD values in the low nanomolar range. Using various deletion mutants, the binding site for aggrecan and versican lectin domains was mapped to the epidermal growth factor-like repeats in domain II of fibulin-1. No difference in affinity was found for deglycosylated fibulin-1, indicating that the proteoglycan C-type lectin domains bind to the protein part of fibulin-1. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1116007
- author
- Aspberg, Anders
LU
; Adam, S
; Kostka, G
; Timpl, R
and Heinegård, Dick
LU
- organization
- publishing date
- 1999
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 274
- issue
- 29
- pages
- 20444 - 20449
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:10400671
- scopus:0033575208
- ISSN
- 1083-351X
- 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)
- id
- 2aed5618-24b6-4871-84f3-7343efdf1219 (old id 1116007)
- alternative location
- http://www.jbc.org/cgi/content/full/274/29/20444
- date added to LUP
- 2016-04-01 11:36:50
- date last changed
- 2022-02-03 02:01:16
@article{2aed5618-24b6-4871-84f3-7343efdf1219,
abstract = {{The aggregating proteoglycans (aggrecan, versican, neurocan, and brevican) are important components of many extracellular matrices. Their N-terminal globular domain binds to hyaluronan, but the function of their C-terminal region containing a C-type lectin domain is less clear. We now report that a 90-kDa protein copurifies with recombinant lectin domains from aggrecan and versican, but not from the brain-specific neurocan and brevican. Amino acid sequencing of tryptic peptides from this protein identified it as fibulin-1. This extracellular matrix glycoprotein is strongly expressed in tissues where versican is expressed (blood vessels, skin, and developing heart), and also expressed in developing cartilage and bone. It is thus likely to interact with these proteoglycans in vivo. Surface plasmon resonance measurements confirmed that aggrecan and versican lectin domains bind fibulin-1, whereas brevican and neurocan do not. As expected for a C-type lectin, the interactions with fibulin-1 are Ca2+-dependent, with KD values in the low nanomolar range. Using various deletion mutants, the binding site for aggrecan and versican lectin domains was mapped to the epidermal growth factor-like repeats in domain II of fibulin-1. No difference in affinity was found for deglycosylated fibulin-1, indicating that the proteoglycan C-type lectin domains bind to the protein part of fibulin-1.}},
author = {{Aspberg, Anders and Adam, S and Kostka, G and Timpl, R and Heinegård, Dick}},
issn = {{1083-351X}},
language = {{eng}},
number = {{29}},
pages = {{20444--20449}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and versican}},
url = {{http://www.jbc.org/cgi/content/full/274/29/20444}},
volume = {{274}},
year = {{1999}},
}