N-Glycosylation of Carnosinase Influences Protein Secretion and Enzyme Activity: Implications for Hyperglycemia
Laboratory studyHumansOther animals
- Design
- Laboratory study
- What was measured
- Secretion and activity of carnosinase (CN1) in Cos-7 cells with blocked or deleted N-glycosylation sites, under normal and 25 mmol/L glucose; serum CN1 activity in (CTG)5 homozygous diabetic patients versus genotype-matched healthy controls.
What the authors reported
Tunicamycin completely inhibited CN-1 secretion in transfected Cos-7 cells. Deleting all three N-glycosylation sites was needed to reduce secretion, and enzyme activity was already diminished with two sites deleted. In medium with 25 mmol/L glucose the immature 61 kDa CN-1 band was not detected, with increased GlcNAc in cell lysates and more CN-1 in supernatants. Homozygous (CTG)5 diabetic patients had significantly higher serum CN-1 activity than genotype-matched healthy controls. The authors conclude hyperglycaemia enhances CN-1 secretion and activity, so poor glucose control might raise CN-1 even with the (CTG)5 allele.
Limits of this study
Mostly cell-line work; patient numbers not stated in abstract. Full text not read.
Source
PubMed 20460427 · doi:10.2337/db09-0868
Entry checked against PubMed abstract (E-utilities) on 2026-10-19. The dose shown is the dose the researchers used. It is not a recommendation. How to read this page.