Lysine malonylation and propionylation are prevalent in human lens proteins.
Exp Eye Res
; 190: 107864, 2020 01.
Article
in En
| MEDLINE
| ID: mdl-31678036
ABSTRACT
Acylated lysine residues represent major chemical modifications in proteins. We investigated the malonylation and propionylation of lysine residues (MalK, PropK) in the proteins of aging human lenses. Western blot results showed that the two modifications are present in human lens proteins. Liquid chromatography-mass spectrometry (LC-MS/MS) results showed 4-18 and 4-32â¯pmol/mg protein of MalK and PropK, respectively, in human lens proteins with no apparent changes related to aging. Mass spectrometry results revealed that MalK- and PropK-modified lysine residues are present in all major crystallins, other cytosolic proteins, and membrane and cytoskeletal proteins of the lens. Several mitochondrial and cytosolic proteins in cultured human lens epithelial cells showed MalK and PropK modifications. Sirtuin 3 (SIRT3) and sirtuin 5 (SIRT5) were present in human lens epithelial and fiber cells. Moreover, lens epithelial cell lysate deacylated propionylated and malonylated lysozyme. The absence of SIRT3 and SIRT5 led to higher PropK and MalK levels in mouse lenses. Together, these data suggest that MalK and PropK are widespread modifications in lens and SIRT3 and SIRT5 could regulate their levels in lens epithelial cells.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Propionates
/
Crystallins
/
Sirtuins
/
Sirtuin 3
/
Lens, Crystalline
/
Lysine
/
Malonates
Limits:
Animals
/
Humans
/
Middle aged
Language:
En
Journal:
Exp Eye Res
Year:
2020
Document type:
Article
Affiliation country:
United States