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The C5 domain of the collagen VI alpha 3(VI) chain is critical for extracellular microfibril formation and is present in the extracellular matrix of cultured cells

Lamande, SR ; Mörgelin, Matthias LU ; Adams, NE ; Selan, C and Allen, JM (2006) In Journal of Biological Chemistry 281(24). p.16607-16614
Abstract
Collagen VI, a microfibrillar protein found in virtually all connective tissues, is composed of three distinct subunits, alpha 1(VI), alpha 2(VI), and alpha 3(VI), which associate intracellularly to form triple helical heterotrimeric monomers then dimers and tetramers. The secreted tetramers associate end-to-end to form beaded microfibrils. Although the basic steps in assembly and the structure of the tetramers and microfibrils are well defined, details of the interacting protein domains involved in assembly are still poorly understood. To explore the role of the C-terminal globular regions in assembly, alpha 3(VI) cDNA expression constructs with C-terminal truncations were stably transfected into SaOS-2 cells. Control alpha 3(VI) N6-C5... (More)
Collagen VI, a microfibrillar protein found in virtually all connective tissues, is composed of three distinct subunits, alpha 1(VI), alpha 2(VI), and alpha 3(VI), which associate intracellularly to form triple helical heterotrimeric monomers then dimers and tetramers. The secreted tetramers associate end-to-end to form beaded microfibrils. Although the basic steps in assembly and the structure of the tetramers and microfibrils are well defined, details of the interacting protein domains involved in assembly are still poorly understood. To explore the role of the C-terminal globular regions in assembly, alpha 3(VI) cDNA expression constructs with C-terminal truncations were stably transfected into SaOS-2 cells. Control alpha 3(VI) N6-C5 chains with an intact C-terminal globular region (subdomains C1-C5), and truncated alpha 3(VI) N6-C1, N6-C2, N6-C3, and N6-C4 chains, all associated with endogenous alpha 1(VI) and alpha 2(VI) to form collagen VI monomers, dimers and tetramers, which were secreted. These data demonstrate that subdomains C2-C5 are not required for monomer, dimer or tetramer assembly, and suggest that the important chain selection interactions involve the C1 subdomains. In contrast to tetramers containing control alpha 3(VI) N6-C5 chains, tetramers containing truncated alpha 3(VI) chains were unable to associate efficiently end-to-end in the medium and did not form a significant extracellular matrix, demonstrating that the alpha 3(VI) C5 domain plays a crucial role in collagen VI microfibril assembly. The alpha 3(VI) C5 domain is present in the extracellular matrix of SaOS-2 N6-C5 expressing cells and fibroblasts demonstrating that processing of the C-terminal region of the alpha 3(VI) chain is not essential for microfibril formation. (Less)
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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
281
issue
24
pages
16607 - 16614
publisher
ASBMB
external identifiers
  • wos:000238165700053
  • scopus:33745225191
ISSN
1083-351X
DOI
10.1074/jbc.M510192200
language
English
LU publication?
yes
id
49ff3a48-995f-454d-8e2b-e178334b2b41 (old id 406807)
date added to LUP
2016-04-01 11:42:40
date last changed
2021-08-25 03:31:32
@article{49ff3a48-995f-454d-8e2b-e178334b2b41,
  abstract     = {Collagen VI, a microfibrillar protein found in virtually all connective tissues, is composed of three distinct subunits, alpha 1(VI), alpha 2(VI), and alpha 3(VI), which associate intracellularly to form triple helical heterotrimeric monomers then dimers and tetramers. The secreted tetramers associate end-to-end to form beaded microfibrils. Although the basic steps in assembly and the structure of the tetramers and microfibrils are well defined, details of the interacting protein domains involved in assembly are still poorly understood. To explore the role of the C-terminal globular regions in assembly, alpha 3(VI) cDNA expression constructs with C-terminal truncations were stably transfected into SaOS-2 cells. Control alpha 3(VI) N6-C5 chains with an intact C-terminal globular region (subdomains C1-C5), and truncated alpha 3(VI) N6-C1, N6-C2, N6-C3, and N6-C4 chains, all associated with endogenous alpha 1(VI) and alpha 2(VI) to form collagen VI monomers, dimers and tetramers, which were secreted. These data demonstrate that subdomains C2-C5 are not required for monomer, dimer or tetramer assembly, and suggest that the important chain selection interactions involve the C1 subdomains. In contrast to tetramers containing control alpha 3(VI) N6-C5 chains, tetramers containing truncated alpha 3(VI) chains were unable to associate efficiently end-to-end in the medium and did not form a significant extracellular matrix, demonstrating that the alpha 3(VI) C5 domain plays a crucial role in collagen VI microfibril assembly. The alpha 3(VI) C5 domain is present in the extracellular matrix of SaOS-2 N6-C5 expressing cells and fibroblasts demonstrating that processing of the C-terminal region of the alpha 3(VI) chain is not essential for microfibril formation.},
  author       = {Lamande, SR and Mörgelin, Matthias and Adams, NE and Selan, C and Allen, JM},
  issn         = {1083-351X},
  language     = {eng},
  number       = {24},
  pages        = {16607--16614},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {The C5 domain of the collagen VI alpha 3(VI) chain is critical for extracellular microfibril formation and is present in the extracellular matrix of cultured cells},
  url          = {http://dx.doi.org/10.1074/jbc.M510192200},
  doi          = {10.1074/jbc.M510192200},
  volume       = {281},
  year         = {2006},
}