Journal article
Aberrant mitochondria in a bethlem myopathy patient with a homozygous amino acid substitution that destabilizes the Collagen VI α2(VI) chain
LK Zamurs, MA Idoate, E Hanssen, A Gomez-Ibañez, P Pastor, SR Lamandé
Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2015
Abstract
Background: Collagen VI amino acid substitutions are common, and it is difficult to determine if they are pathogenic. Results: COL6A2 p.D871N chains are abnormal and cannot assemble. Alternatively spliced chains lacking the mutation cannot functionally substitute. Conclusion: COL6A2 p.D871N is a recessive mutation. Significance: Protein studies reveal the consequences of amino acid substitutions in the globular domains of collagen VI.
Grants
Awarded by National Health & Medical Research Council of Australia
Funding Acknowledgements
This work was supported in part by Project Grant 491252 and Research Fellowship 436903 (to S. R. L.) from the National Health & Medical Research Council of Australia, the Murdoch Childrens Research Institute, and the Victorian Government's Operational Infrastructure Support Program.