Versican interacts with fibrillin-1 and links extracellular microfibrils to other connective tissue networks
Isogai, Z ; Aspberg, Anders LU
; Keene, DR
; Ono, RN
; Reinhardt, DP
and Sakai, LY
(2002)
In Journal of Biological Chemistry
277(6).
p.4565-4572
- Abstract
- Fibrillin-containing microfibrils are polymeric structures that are difficult to extract from connective tissues. Proteolytic digestion of tissues has been utilized to release microfibrils for study. Few of the molecules that connect microfibrils to other elements in the matrix have been identified. In this study, electron microscopic immunolocalization of anti-versican antibodies in tissues and in extracted microfibrils demonstrated that the C-terminal region of versican is found associated with fibrillin microfibrils. Extraction of microfibrils followed by treatment of microfibrils under dissociating conditions suggested that the versican C terminus is covalently bound to microfibrils. Binding assays using recombinant fibrillin-1... (More)
- Fibrillin-containing microfibrils are polymeric structures that are difficult to extract from connective tissues. Proteolytic digestion of tissues has been utilized to release microfibrils for study. Few of the molecules that connect microfibrils to other elements in the matrix have been identified. In this study, electron microscopic immunolocalization of anti-versican antibodies in tissues and in extracted microfibrils demonstrated that the C-terminal region of versican is found associated with fibrillin microfibrils. Extraction of microfibrils followed by treatment of microfibrils under dissociating conditions suggested that the versican C terminus is covalently bound to microfibrils. Binding assays using recombinant fibrillin-1 polypeptides and recombinant lectican lectin domains indicated that the versican lectin domain binds to specific fibrillin-1 polypeptides. The versican lectin domain also bound to molecules comigrating with authentic fibrillin-1 monomers in anassay using cell culture medium. In assays using microfibrils, the versican lectin domain demonstrated preferential binding compared with other lecticans. Binding was calcium-dependent. The binding site for versican in microfibrils is most likely within a region of fibrillin-1 between calcium-binding epidermal growth factor-like domains 11 and 21. Human mutations irk this region can result in severe forms of the Marfan syndrome ("neonatal" Marfan syndrome). The connection between versican and fibrillin microfibrils may be functionally significant, particularly in cardiovascular tissues. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/343452
- author
- Isogai, Z
; Aspberg, Anders
LU
; Keene, DR
; Ono, RN
; Reinhardt, DP
and Sakai, LY
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 277
- issue
- 6
- pages
- 4565 - 4572
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- wos:000173813900101
- pmid:11726670
- scopus:0037040276
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M110583200
- 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
- e42a10ba-0aea-40cd-b4e1-b99f83e9b36c (old id 343452)
- date added to LUP
- 2016-04-01 12:12:07
- date last changed
- 2022-02-11 03:26:34
@article{e42a10ba-0aea-40cd-b4e1-b99f83e9b36c,
abstract = {{Fibrillin-containing microfibrils are polymeric structures that are difficult to extract from connective tissues. Proteolytic digestion of tissues has been utilized to release microfibrils for study. Few of the molecules that connect microfibrils to other elements in the matrix have been identified. In this study, electron microscopic immunolocalization of anti-versican antibodies in tissues and in extracted microfibrils demonstrated that the C-terminal region of versican is found associated with fibrillin microfibrils. Extraction of microfibrils followed by treatment of microfibrils under dissociating conditions suggested that the versican C terminus is covalently bound to microfibrils. Binding assays using recombinant fibrillin-1 polypeptides and recombinant lectican lectin domains indicated that the versican lectin domain binds to specific fibrillin-1 polypeptides. The versican lectin domain also bound to molecules comigrating with authentic fibrillin-1 monomers in anassay using cell culture medium. In assays using microfibrils, the versican lectin domain demonstrated preferential binding compared with other lecticans. Binding was calcium-dependent. The binding site for versican in microfibrils is most likely within a region of fibrillin-1 between calcium-binding epidermal growth factor-like domains 11 and 21. Human mutations irk this region can result in severe forms of the Marfan syndrome ("neonatal" Marfan syndrome). The connection between versican and fibrillin microfibrils may be functionally significant, particularly in cardiovascular tissues.}},
author = {{Isogai, Z and Aspberg, Anders and Keene, DR and Ono, RN and Reinhardt, DP and Sakai, LY}},
issn = {{1083-351X}},
language = {{eng}},
number = {{6}},
pages = {{4565--4572}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{Versican interacts with fibrillin-1 and links extracellular microfibrils to other connective tissue networks}},
url = {{http://dx.doi.org/10.1074/jbc.M110583200}},
doi = {{10.1074/jbc.M110583200}},
volume = {{277}},
year = {{2002}},
}