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

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Heterogeneity of Collagen VI Microfibrils: Structural Analysis of Non-collagenous Regions. / Maaß, Tobias; Bayley, Christopher P; Mörgelin, Matthias; Lettmann, Sandra; Bonaldo, Paolo; Paulsson, Mats; Baldock, Clair; Wagener, Raimund.

In: Journal of Biological Chemistry, Vol. 291, No. 10, 2016, p. 5247-5258.

Research output: Contribution to journalArticle

Harvard

Maaß, T, Bayley, CP, Mörgelin, M, Lettmann, S, Bonaldo, P, Paulsson, M, Baldock, C & Wagener, R 2016, 'Heterogeneity of Collagen VI Microfibrils: Structural Analysis of Non-collagenous Regions.', Journal of Biological Chemistry, vol. 291, no. 10, pp. 5247-5258. https://doi.org/10.1074/jbc.M115.705160

APA

Maaß, T., Bayley, C. P., Mörgelin, M., Lettmann, S., Bonaldo, P., Paulsson, M., Baldock, C., & Wagener, R. (2016). Heterogeneity of Collagen VI Microfibrils: Structural Analysis of Non-collagenous Regions. Journal of Biological Chemistry, 291(10), 5247-5258. https://doi.org/10.1074/jbc.M115.705160

CBE

Maaß T, Bayley CP, Mörgelin M, Lettmann S, Bonaldo P, Paulsson M, Baldock C, Wagener R. 2016. Heterogeneity of Collagen VI Microfibrils: Structural Analysis of Non-collagenous Regions. Journal of Biological Chemistry. 291(10):5247-5258. https://doi.org/10.1074/jbc.M115.705160

MLA

Vancouver

Author

Maaß, Tobias ; Bayley, Christopher P ; Mörgelin, Matthias ; Lettmann, Sandra ; Bonaldo, Paolo ; Paulsson, Mats ; Baldock, Clair ; Wagener, Raimund. / Heterogeneity of Collagen VI Microfibrils: Structural Analysis of Non-collagenous Regions. In: Journal of Biological Chemistry. 2016 ; Vol. 291, No. 10. pp. 5247-5258.

RIS

TY - JOUR

T1 - Heterogeneity of Collagen VI Microfibrils: Structural Analysis of Non-collagenous Regions.

AU - Maaß, Tobias

AU - Bayley, Christopher P

AU - Mörgelin, Matthias

AU - Lettmann, Sandra

AU - Bonaldo, Paolo

AU - Paulsson, Mats

AU - Baldock, Clair

AU - Wagener, Raimund

PY - 2016

Y1 - 2016

N2 - 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.

AB - 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.

U2 - 10.1074/jbc.M115.705160

DO - 10.1074/jbc.M115.705160

M3 - Article

C2 - 26742845

VL - 291

SP - 5247

EP - 5258

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 1083-351X

IS - 10

ER -