TY  - JOUR
A1  - Dietrich, Stefan
A1  - Jacobs, Simone
A1  - Zheng, Ju-Sheng
A1  - Meidtner, Karina
A1  - Schwingshackl, Lukas
A1  - Schulze, Matthias Bernd
T1  - Gene-lifestyle interaction on risk of type 2 diabetes
BT  - A systematic review
JF  - Obesity reviews : an official journal of the International Association for the Study of Obesity
N2  - The pathophysiological influence of gene-lifestyle interactions on the risk to develop type 2 diabetes (T2D) is currently under intensive research. This systematic review summarizes the evidence for gene-lifestyle interactions regarding T2D incidence. MEDLINE, EMBASE, and Web of Science were systematically searched until 31 January 2019 to identify publication with (a) prospective study design; (b) T2D incidence; (c) gene-diet, gene-physical activity, and gene-weight loss intervention interaction; and (d) population who are healthy or prediabetic. Of 66 eligible publications, 28 reported significant interactions. A variety of different genetic variants and dietary factors were studied. Variants at TCF7L2 were most frequently investigated and showed interactions with fiber and whole grain on T2D incidence. Further gene-diet interactions were reported for, eg, a western dietary pattern with a T2D-GRS, fat and carbohydrate with IRS1 rs2943641, and heme iron with variants of HFE. Physical activity showed interaction with HNF1B, IRS1, PPAR gamma, ADRA2B, SLC2A2, and ABCC8 variants and weight loss interventions with ENPP1, PPAR gamma, ADIPOR2, ADRA2B, TNF alpha, and LIPC variants. However, most findings represent single study findings obtained in European ethnicities. Although some interactions have been reported, their conclusiveness is still low, as most findings were not yet replicated across multiple study populations.
KW  - diet
KW  - gene-lifestyle interaction
KW  - incident type 2 diabetes
KW  - physical activity
KW  - weight loss intervention
Y1  - 2019
U6  - https://doi.org/10.1111/obr.12921
SN  - 1467-7881
SN  - 1467-789X
VL  - 20
IS  - 11
SP  - 1557
EP  - 1571
PB  - Wiley
CY  - Hoboken
ER  - 
TY  - JOUR
A1  - Wittenbecher, Clemens
A1  - Ouni, Meriem
A1  - Kuxhaus, Olga
A1  - Jähnert, Markus
A1  - Gottmann, Pascal
A1  - Teichmann, Andrea
A1  - Meidtner, Karina
A1  - Kriebel, Jennifer
A1  - Grallert, Harald
A1  - Pischon, Tobias
A1  - Boeing, Heiner
A1  - Schulze, Matthias Bernd
A1  - Schürmann, Annette
T1  - Insulin-Like Growth Factor Binding Protein 2 (IGFBP-2) and the Risk of Developing Type 2 Diabetes
JF  - Diabetes : a journal of the American Diabetes Association
N2  - Recent studies suggest that insulin-like growth factor binding protein 2 (IGFBP-2) may protect against type 2 diabetes, but population-based human studies are scarce. We aimed to investigate the prospective association of circulating IGFBP-2 concentrations and of differential methylation in the IGFBP-2 gene with type 2 diabetes risk.
Y1  - 2019
U6  - https://doi.org/10.2337/db18-0620
SN  - 0012-1797
SN  - 1939-327X
VL  - 68
IS  - 1
SP  - 188
EP  - 197
PB  - American Diabetes Association
CY  - Alexandria
ER  - 
TY  - JOUR
A1  - Kroeger, Janine
A1  - Meidtner, Karina
A1  - Stefan, Norbert
A1  - Guevara, Marcela
A1  - Kerrison, Nicola D.
A1  - Ardanaz, Eva
A1  - Aune, Dagfinn
A1  - Boeing, Heiner
A1  - Dorronsoro, Miren
A1  - Dow, Courtney
A1  - Fagherazzi, Guy
A1  - Franks, Paul W.
A1  - Freisling, Heinz
A1  - Gunter, Marc J.
A1  - Maria Huerta, Jose
A1  - Kaaks, Rudolf
A1  - Key, Timothy J.
A1  - Khaw, Kay Tee
A1  - Krogh, Vittorio
A1  - Kuehn, Tilman
A1  - Mancini, Francesca Romana
A1  - Mattiello, Amalia
A1  - Nilsson, Peter M.
A1  - Olsen, Anja
A1  - Overvad, Kim
A1  - Palli, Domenico
A1  - Ramon Quiros, J.
A1  - Rolandsson, Olov
A1  - Sacerdote, Carlotta
A1  - Sala, Nuria
A1  - Salamanca-Fernandez, Elena
A1  - Sluijs, Ivonne
A1  - Spijkerman, Annemieke M. W.
A1  - Tjonneland, Anne
A1  - Tsilidis, Konstantinos K.
A1  - Tumino, Rosario
A1  - van der Schouw, Yvonne T.
A1  - Forouhi, Nita G.
A1  - Sharp, Stephen J.
A1  - Langenberg, Claudia
A1  - Riboli, Elio
A1  - Schulze, Matthias Bernd
A1  - Wareham, Nicholas J.
T1  - Circulating Fetuin-A and Risk of Type 2 Diabetes
BT  - a mendelian randomization analysis
JF  - Diabetes : a journal of the American Diabetes Association
N2  - Fetuin-A, a hepatic-origin protein, is strongly positively associated with risk of type 2 diabetes in human observational studies, but it is unknown whether this association is causal. Weaimed to study the potential causal relation of circulating fetuin-A to risk of type 2 diabetes in a Mendelian randomization study with single nucleotide polymorphisms located in the fetuin-A-encoding AHSG gene. We used data from eight European countries of the European Prospective Investigation into Cancer and Nutrition (EPIC)-InterAct case-cohort study including 10,020 incident cases. Plasma fetuin-A concentration was measured in a subset of 965 subcohort participants and 654 case subjects. A genetic score of the AHSG single nucleotide polymorphisms was strongly associated with fetuin-A (28% explained variation). Using the genetic score as instrumental variable of fetuin-A, we observed no significant association of a 50 mu g/mL higher fetuin-A concentration with diabetes risk (hazard ratio 1.02 [95% CI 0.97, 1.07]). Combining our results with those from the DIAbetes Genetics Replication And Meta-analysis (DIAGRAM) consortium (12,171 case subjects) also did not suggest a clear significant relation of fetuin-A with diabetes risk. In conclusion, although there is mechanistic evidence for an effect of fetuin-A on insulin sensitivity and secretion, this study does not support a strong, relevant relationship between circulating fetuin-A and diabetes risk in the general population.
Y1  - 2018
U6  - https://doi.org/10.2337/db17-1268
SN  - 0012-1797
SN  - 1939-327X
VL  - 67
IS  - 6
SP  - 1200
EP  - 1205
PB  - American Diabetes Association
CY  - Alexandria
ER  - 
TY  - JOUR
A1  - Rawel, Harshadrai Manilal
A1  - Frey, Simone K.
A1  - Meidtner, Karina
A1  - Kroll, Jürgen
A1  - Schweigert, Florian J.
T1  - Determining the binding affinities of phenolic compounds to proteins by quenching of the intrinsic tryptophan fluorescence
JF  - Molecular nutrition & food research : bioactivity, chemistry, immunology, microbiology, safety, technology
N2  - The noncovalent binding of selected phenolic compounds (chlorogenic-, ferutic-, gallic acid, quercetin, rutin, and isoquercetin) to proteins (HSA, BSA, soy glycinin, and lysozyme) was studied by an indirect method applying the quenching of intrinsic tryptophan fluorescence. From the data obtained, the binding constants were calculated by nonlinear regression (one site binding; y = Bx/k + x). It has been reported that tannins inhibit human salivary amylase and that these complexes may reduce the development of cariogenic plaques. Further, amylase contains two tryptophan residues in its active site. Therefore, in a second part of the study involving 31 human subjects, evidence was sought for noncovalent interactions between the phenols of green tea and saliva proteins as measured by the fluorescence intensity. Amylase activity was determined before and after the addition of green tea to saliva of 31 subjects. Forty percent of the subjects showed an increase in amylase activity contrary to studies reporting only a decrease in activity. The interactions of tannin with amylase result in a decrease of its activity. It still remains to be elucidated why amylase does not react uniformly under conditions of applying green tea to saliva. Further, in terms of using phenols as caries inhibitors this finding should be of importance.
KW  - amylase activity
KW  - green tea phenols
KW  - protein-phenol binding
KW  - saliva proteins
KW  - tryptophan quenching
Y1  - 2006
U6  - https://doi.org/10.1002/mnfr.200600013
SN  - 1613-4125
VL  - 50
IS  - 8
SP  - 705
EP  - 713
PB  - Wiley
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Rawel, Harshadrai Manilal
A1  - Meidtner, Karina
A1  - Kroll, Jürgen
T1  - Binding of selected phenolic compounds to proteins
N2  - In the context of this study, the noncovalent binding of selected phenolic compounds (chlorogenic, ferulic, and gallic acids, quercetin, rutin, and isocluercetin) to different proteins (human serum albumin, bovine serum albumin, soy glycinin, and lysozyme) was studied with direct (Hummel- Dreyer/size exclusion chromatography) and/or indirect methods (fluorescence absorbance properties of the binding components). In the latter case, the measurement of the phenol binding was achieved by exploiting the intrinsic fluorescence emission properties of cluercetin as a probe. From the data obtained, the binding constants and the number of binding sites were calculated. The binding parameters were influenced by different factors, where, e.g., increasing temperature and ionic strength as well as decreasing pH cause a diminished binding. The structures of the proteins as determined by circular dichroism indicate changes in the tertiary structure with the secondary structure remaining intact
Y1  - 2005
SN  - 0021-8561
ER  -