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6 results on '"Grams, Sabine"'

1. Low adherence to CKD-specific dietary recommendations associates with impaired kidney function, dyslipidemia, and inflammation

Author

Kaesler, Nadine, Baid-Agrawal, Seema, Grams, Sabine, Nadal, Jennifer, Schmid, Matthias, Schneider, Markus P., and Eckardt, Kai-Uwe

Subjects
Chronic kidney failure -- Diet therapy -- Complications and side effects, Patient compliance -- Influence, Inflammation -- Risk factors, Dyslipidemias -- Risk factors, Food/cooking/nutrition, Health
Abstract

Background/Objectives A diet following chronic kidney disease (CKD)-specific recommendations is considered essential for optimal management of patients with CKD. However, data on the adherence to these recommendations and its implications for health-relevant biomarkers are lacking. The objectives were to estimate adherence to CKD-specific dietary recommendations, to identify characteristics and lifestyle variables associated with poor adherence, and to investigate the relationship of adherence with biomarkers. Methods In this cross-sectional analysis, average dietary intake was estimated in 3193 participants with moderately severe CKD enrolled into the observational multicenter German CKD study using a food frequency questionnaire. A CKD diet score was developed to assess adherence to CKD-specific dietary recommendations based on intake of sodium, potassium, fiber, protein, sugar, and cholesterol. The associations of dietary adherence with characteristics, lifestyle variables, and biomarker levels were determined. Results Logistic regression analysis revealed younger age, higher body mass index, male gender, lower educational attainment, various lifestyle variables (cigarette smoking, infrequent alcohol consumption, low physical activity), and lower estimated glomerular filtrate rate associated with lower adherence to dietary recommendations. Low adherence to dietary recommendations was further associated with dyslipidemia, higher uric acid, and C-reactive protein levels. Associations between low dietary adherence and biomarkers were mostly driven by low intake of fiber and potassium, and high intake of sugar and cholesterol. Conclusions This study revealed differential characteristics and biomarkers associated with lower adherence to CKD-specific dietary recommendations. Promotion of CKD-specific dietary recommendations may help to mitigate the adverse prognosis in CKD patients., Author(s): Nadine Kaesler [sup.1] , Seema Baid-Agrawal [sup.2] , Sabine Grams [sup.3] , Jennifer Nadal [sup.4] , Matthias Schmid [sup.4] , Markus P. Schneider [sup.5] [sup.6] , Kai-Uwe Eckardt [sup.5] [...]

Published
2021
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5. In VivoModulation of the Acidic N-Glycans from Rat Liver Dipeptidyl Peptidase IV by N-Propanoyl-d-mannosamine

Author

Stehling, Peer, Grams, Sabine, Nuck, Rolf, Grunow, Detlef, Reutter, Werner, and Gohlke, Martin

Abstract

Derivatives of N-acyl-d-mannosamine differing in the N-acyl-side chain can be metabolically converted into neuraminic acids with corresponding N-acyl side chains. In the present study we show the in vivomodulation of sialic acids in membrane-bound dipeptidyl peptidase IV (CD 26) from rat liver after administration of N-propanoyl-d-mannosamine. Treatment of rats with this unphysiological precursor resulted in an incorporation of N-propanoylneuraminic acid into N-linked glycans of dipeptidyl peptidase IV.

Published
1999
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6. Domain-Specific N-Glycosylation of the Membrane Glycoprotein Dipeptidylpeptidase IV (CD26) Influences its Subcellular Trafficking, Biological Stability, Enzyme Activity and Protein Folding

Author

Fan, Hua, Meng, Wenmao, Kilian, Christiane, Grams, Sabine, and Reutter, Werner

Abstract

Dipeptidyl peptidase IV (DPPIV, CD26) is an N-glycosylated type II plasma membrane protein. The primary structure of rat wild-type DPPIV contains eight potential N-glycosylation sites. To investigate the role of N-glycosylation in the function of DPPIV, three of its asparagine residues were separately converted to glutamine by site-directed mutagenesis. The resulting N-glycosylation mutants of rat DPPIV were studied in stable transfected Chinese hamster ovary cells. All three N-glycosylation mutants of DPPIV showed a reduced half-life, as well as differing degrees of inhibition of the processing of their N-glycans. Mutation of the first (Asn83?Gln) or eighth (Asn686?Gln) N-glycosylation site had only a small effect on its enzymatic activity, cell-surface expression and dimer formation, whereas the mutation of the sixth N-glycosylation site (Asn319?Gln) abolished the enzymatic activity, eliminated cell-surface expression and prevented the dimerization of the DPPIV protein. The mutant Gln319DPPIV is retained in the cytoplasm and its degration was drastically increased. Our data suggest that the N-glycosylation at Asn319 is involved in protein trafficking and correct protein folding.

Published
1997
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