ArticleDiabetes2010
N-glycosylation of carnosinase influences protein secretion and enzyme activity: implications for hyperglycemia.
Article in Diabetes, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 43 citations in OpenAlex.
- CNDP1 (CTG)Scientific reports · 2026Article
- A comprehensive review on physiological and biological activities of carnosine: turning from preclinical facts to potential clinical applications.Naunyn-Schmiedeberg's archives of pharmacology · 2025Review
- Serum carnosinase 1, an early indicator for incident microalbuminuria in type 1 diabetes.Journal of diabetes and metabolic disorders · 2024Article
- State of the Art in the Development of Human Serum Carnosinase Inhibitors.Molecules (Basel, Switzerland) · 2024Review
- Association Between Serum Carnosinase Concentration and Activity and Renal Function Impairment in a Type-2 Diabetes Cohort.Frontiers in pharmacology · 2022Article
- In-depth Site-specific Analysis of N-glycoproteome in Human Cerebrospinal Fluid and Glycosylation Landscape Changes in Alzheimer's Disease.Molecular & cellular proteomics : MCP · 2021Article
- Human carnosinase 1 overexpression aggravates diabetes and renal impairment in BTBRJournal of molecular medicine (Berlin, Germany) · 2020Article
- [Advances in salivary protein glycosylation and its relationship with systemic and oral diseases].Hua xi kou qiang yi xue za zhi = Huaxi kouqiang yixue zazhi = West China journal of stomatology · 2018Review
- Carnosinase, diabetes mellitus and the potential relevance of carnosinase deficiency.Journal of inherited metabolic disease · 2018Review
- Article
- Intrinsic carnosine metabolism in the human kidney.Amino acids · 2015Article
- N-glycosylation is essential for ileal ASBT function and protection against proteases.American journal of physiology. Cell physiology · 2015Article
- Sex specific association between carnosinase gene CNDP1 and cardiovascular mortality in patients with type 2 diabetes (ZODIAC-22).Journal of nephrology · 2015Article
- Salivary protein glycosylation as a noninvasive biomarker for assessment of glycemia.Journal of diabetes science and technology · 2015Article
- Carnosinases, their substrates and diseases.Molecules (Basel, Switzerland) · 2014Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
objectiveThe (CTG)(n) polymorphism in the serum carnosinase (CN-1) gene affects CN-1 secretion. Since CN-1 is heavily glycosylated and glycosylation might influence protein secretion as well, we tested the role of N-glycosylation for CN-1 secretion and enzyme activity. We also tested whether CN-1 secretion is changed under hyperglycemic conditions.
resultsN-glycosylation of CN-1 was either inhibited by tunicamycin in pCSII-CN-1-transfected Cos-7 cells or by stepwise deletion of its three putative N-glycosylation sites. CN-1 protein expression, N-glycosylation, and enzyme activity were assessed in cell extracts and supernatants. The influence of hyperglycemia on CN-1 enzyme activity in human serum was tested in homozygous (CTG)(5) diabetic patients and healthy control subjects. Tunicamycin completely inhibited CN-1 secretion. Deletion of all N-glycosylation sites was required to reduce CN-1 secretion efficiency. Enzyme activity was already diminished when two sites were deleted. In pCSII-CN-1-transfected Cos-7 cells cultured in medium containing 25 mmol/l d-glucose, the immature 61 kilodaltons (kDa) CN-1 immune reactive band was not detected. This was paralleled by an increased GlcNAc expression in cell lysates and CN-1 expression in the supernatants. Homozygous (CTG)(5) diabetic patients had significantly higher serum CN-1 activity compared with genotype-matched, healthy control subjects.
conclusionsWe conclude that apart from the (CTG)(n) polymorphism in the signal peptide of CN-1, N-glycosylation is essential for appropriate secretion and enzyme activity. Since hyperglycemia enhances CN-1 secretion and enzyme activity, our data suggest that poor blood glucose control in diabetic patients might result in an increased CN-1 secretion even in the presence of the (CTG)(5) allele.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.