Advanced

Heterogeneity of Collagen VI Microfibrils: Structural Analysis of Non-collagenous Regions.

Maaß, Tobias; Bayley, Christopher P; Mörgelin, Matthias LU ; Lettmann, Sandra; Bonaldo, Paolo; Paulsson, Mats; Baldock, Clair and Wagener, Raimund (2016) In Journal of Biological Chemistry 291(10). p.5247-5258
Abstract
Collagen VI, a collagen with uncharacteristically large N- and C-terminal non-collagenous regions, forms a distinct microfibrillar network in most connective tissues. It was long considered to consist of three genetically distinct α chains (α1, α2 and α3). Intracellularly heterotrimeric molecules associate to form dimers and tetramers, which are then secreted and assembled to microfibrils. The identification of three novel long collagen VI α chains α4, α5, and α6 led to the question if and how these may substitute for the long α3 chain in collagen VI assembly. Here we studied structural features of the novel long chains, and analyzed the assembly of these into tetramers and microfibrils. N- and C-terminal globular regions of collagen VI... (More)
Collagen VI, a collagen with uncharacteristically large N- and C-terminal non-collagenous regions, forms a distinct microfibrillar network in most connective tissues. It was long considered to consist of three genetically distinct α chains (α1, α2 and α3). Intracellularly heterotrimeric molecules associate to form dimers and tetramers, which are then secreted and assembled to microfibrils. The identification of three novel long collagen VI α chains α4, α5, and α6 led to the question if and how these may substitute for the long α3 chain in collagen VI assembly. Here we studied structural features of the novel long chains, and analyzed the assembly of these into tetramers and microfibrils. N- and C-terminal globular regions of collagen VI were recombinantly expressed and studied by SAXS. Ab initio models of the N-terminal globular regions of the α4, α5 and α6 chains showed a C-shaped structure similar to that found for the α3 chain. Single particle EM nanostructure of the N-terminal globular region of the α4 chain confirmed the C-shaped structure revealed by SAXS. Immuno EM of collagen VI extracted from tissue revealed that like the α3 chain the novel long chains assemble to homotetramers that are incorporated into mixed microfibrils. Moreover, SAXS models of the C-terminal globular regions of the α1, α2, α4, and α6 chains were generated. Interestingly, the α1, α2 and α4 C-terminal globular regions dimerize. These self-interactions may play a role in tetramer formation. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
291
issue
10
pages
5247 - 5258
publisher
ASBMB
external identifiers
  • pmid:26742845
  • wos:000371640600035
  • scopus:84964685813
ISSN
1083-351X
DOI
10.1074/jbc.M115.705160
language
English
LU publication?
yes
id
9366987e-c6e0-47d5-9e5b-48b0d6551858 (old id 8592781)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/26742845?dopt=Abstract
date added to LUP
2016-02-02 09:11:52
date last changed
2017-10-22 04:51:44
@article{9366987e-c6e0-47d5-9e5b-48b0d6551858,
  abstract     = {Collagen VI, a collagen with uncharacteristically large N- and C-terminal non-collagenous regions, forms a distinct microfibrillar network in most connective tissues. It was long considered to consist of three genetically distinct α chains (α1, α2 and α3). Intracellularly heterotrimeric molecules associate to form dimers and tetramers, which are then secreted and assembled to microfibrils. The identification of three novel long collagen VI α chains α4, α5, and α6 led to the question if and how these may substitute for the long α3 chain in collagen VI assembly. Here we studied structural features of the novel long chains, and analyzed the assembly of these into tetramers and microfibrils. N- and C-terminal globular regions of collagen VI were recombinantly expressed and studied by SAXS. Ab initio models of the N-terminal globular regions of the α4, α5 and α6 chains showed a C-shaped structure similar to that found for the α3 chain. Single particle EM nanostructure of the N-terminal globular region of the α4 chain confirmed the C-shaped structure revealed by SAXS. Immuno EM of collagen VI extracted from tissue revealed that like the α3 chain the novel long chains assemble to homotetramers that are incorporated into mixed microfibrils. Moreover, SAXS models of the C-terminal globular regions of the α1, α2, α4, and α6 chains were generated. Interestingly, the α1, α2 and α4 C-terminal globular regions dimerize. These self-interactions may play a role in tetramer formation.},
  author       = {Maaß, Tobias and Bayley, Christopher P and Mörgelin, Matthias and Lettmann, Sandra and Bonaldo, Paolo and Paulsson, Mats and Baldock, Clair and Wagener, Raimund},
  issn         = {1083-351X},
  language     = {eng},
  month        = {01},
  number       = {10},
  pages        = {5247--5258},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Heterogeneity of Collagen VI Microfibrils: Structural Analysis of Non-collagenous Regions.},
  url          = {http://dx.doi.org/10.1074/jbc.M115.705160},
  volume       = {291},
  year         = {2016},
}