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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)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
277
issue
6
pages
4565 - 4572
publisher
ASBMB
external identifiers
  • wos:000173813900101
  • pmid:11726670
  • scopus:0037040276
ISSN
1083-351X
DOI
10.1074/jbc.M110583200
language
English
LU publication?
yes
id
e42a10ba-0aea-40cd-b4e1-b99f83e9b36c (old id 343452)
date added to LUP
2007-10-23 11:07:52
date last changed
2017-10-22 03:47:52
@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    = {ASBMB},
  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},
  volume       = {277},
  year         = {2002},
}