期刊
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE
卷 1852, 期 10, 页码 2287-2291出版社
ELSEVIER
DOI: 10.1016/j.bbadis.2015.06.014
关键词
Neuronal ceroid lipofuscinoses; NCLs; ATP synthase; Subunit c; CLN; Storage body characterisation; Lysosomal storage disease; Protein storing disease
资金
- US National Institutes of Health [NS11238, NS32348, NS40297, NS053559]
- Batten Disease Support and Research Association
- Neurological Foundation of New Zealand
- Medical Research Council (UK)
- Massey University, New Zealand
- Lincoln University, New Zealand
The discoveries of specific protein storage in the NCLs, particularly of subunit c of ATP synthase in most, and the sphingolipid activator proteins, SAPs or saposins A and D in CLN1, CLN10 and an unassigned form are reviewed. The subunit c stored in the relevant NCLs is the complete mature molecule including an unusual modification found only in animal species, trimethylation of its lysine-43. Because of its strongly hydrophobic and lipid-like properties subunit c is easily overlooked or incorrectly described. This is becoming more of a problem as subunit c is not detected in standard proteomic investigations. Methods are reviewed that allow its unequivocal characterisation. Subunit c storage and cellular storage body accumulation do not cause the neuropathology characteristic of these diseases. The function of the trimethyl group on lysine-43 of subunit c is considered, along with some indications of where its normal turnover may be disrupted in the NCLs. (C) 2015 Elsevier B.V. All rights reserved.
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