@article{HernandezTrianaKrollProlletal.1996,
  author    = {Hernandez-Triana, Manuel and Kroll, J{\"u}rgen and Proll, J{\"u}rgen and Noack, Jutta and Petzke, Klaus-J{\"u}rgen},
  title     = {Benzyl-isothiocyanate (BITC) decreases quality of egg white proteins in rats},
  year      = {1996},
  language  = {en}
}
@article{HesseJaschkeKanzleiteretal.2012,
  author    = {Hesse, Deike and Jaschke, Alexander and Kanzleiter, Timo and Witte, Nicole and Augustin, Robert and Hommel, Angela and P{\"u}schel, Gerhard Paul and Petzke, Klaus-J{\"u}rgen and Joost, Hans-Georg and Schupp, Michael and Sch{\"u}rmann, Annette},
  title     = {GTPase ARFRP1 is essential for normal hepatic glycogen storage and insulin-like growth factor 1 secretion},
  series = {Molecular and cellular biology},
  volume    = {32},
  journal   = {Molecular and cellular biology},
  number    = {21},
  publisher = {American Society for Microbiology},
  address   = {Washington},
  issn      = {0270-7306},
  doi       = {10.1128/MCB.00522-12},
  pages     = {4363 -- 4374},
  year      = {2012},
  abstract  = {The GTPase ADP-ribosylation factor-related protein 1 (ARFRP1) is located at the trans-Golgi compartment and regulates the recruitment of Arf-like 1 (ARL1) and its effector golgin-245 to this compartment. Here, we show that liver-specific knockout of Arfrp1 in the mouse (Arfrp1(liv-/-)) resulted in early growth retardation, which was associated with reduced hepatic insulin-like growth factor 1 (IGF1) secretion. Accordingly, suppression of Arfrp1 in primary hepatocytes resulted in a significant reduction of IGF1 release. However, the hepatic secretion of IGF-binding protein 2 (IGFBP2) was not affected in the absence of ARFRP1. In addition, Arfrp1(liv-/-) mice exhibited decreased glucose transport into the liver, leading to a 50\% reduction of glycogen stores as well as a marked retardation of glycogen storage after fasting and refeeding. These abnormalities in glucose metabolism were attributable to reduced protein levels and intracellular retention of the glucose transporter GLUT2 in Arfrp1(liv-/-) livers. As a consequence of impaired glucose uptake into the liver, the expression levels of carbohydrate response element binding protein (ChREBP), a transcription factor regulated by glucose concentration, and its target genes (glucokinase and pyruvate kinase) were markedly reduced. Our data indicate that ARFRP1 in the liver is involved in the regulation of IGF1 secretion and GLUT2 sorting and is thereby essential for normal growth and glycogen storage.},
  language  = {en}
}
@article{PetzkeSchuppeRohnetal.2005,
  author    = {Petzke, Klaus-J{\"u}rgen and Schuppe, S. and Rohn, Sascha and Rawel, Harshadrai Manilal and Kroll, J{\"u}rgen},
  title     = {Chlorogenic acid moderately decreases the quality of whey proteins in rats},
  issn      = {0021-8561},
  year      = {2005},
  abstract  = {During processing and storage, phenolic compounds (PCs) may react with food protein bound amino acids (AAs). Such reactions have been reported to change physicochemical and to decrease in vitro digestion properties of proteins. A rat growth and nitrogen (N) balance study was conducted to prove whether derivatization with chlorogenic acid (CA) affects the nutritional quality of beta-lactoglobulin (beta-LG). Test diets (10\% protein level) contained nonderivatized beta-LG (LG, treated under omission of CA), low derivatization level beta-LG (LGL), high derivatization level beta-LG (LGH), or casein supplemented with L-methionine (0.3\% of diet; C+met) as an internal standard. An additional group received untreated beta-LG supplemented with pure CA (1.03\% of diet; LG+CA). The AA composition of test proteins, plasma AAs, and liver glutathione (GSH) concentrations were determined. Protein digestibility-corrected amino acid score (PDCAAS) was calculated using human or rat AA requirement patterns and rat fecal digestibility values. N excretion was significantly higher in feces and lower in urine of rats fed with LGH as compared to LG and LGL. Consequently, true N digestibility (TND) was significantly lower with LGH as compared to LG and LGL. The lower content of methionine, cysteine, lysine, and tryptophan in LGH corresponded to a reduced TND. Net protein utilization (NPU) was not different between treated beta-LG fed diet groups but was lower than in LG+CA and C+met fed groups. Only at a relatively high level of derivatization with CA, the otherwise good nutritional quality of beta-LG is affected so that TND is reduced, while NPU still remains unaffected. Derivatization of beta-LG with CA does not seem to lead to an additional deficiency in a specific indispensable AA in growing rats fed with 10\% protein},
  language  = {en}
}
@article{RohnPetzkeRaweletal.2006,
  author    = {Rohn, Sascha and Petzke, Klaus-J{\"u}rgen and Rawel, Harshadrai Manilal and Kroll, J{\"u}rgen},
  title     = {Reactions of chlorogenic acid and quercetin with a soy protein isolate - Influence on the in vivo food protein quality in rats},
  series = {Molecular nutrition \& food research : bioactivity, chemistry, immunology, microbiology, safety, technology},
  volume    = {50},
  journal   = {Molecular nutrition \& food research : bioactivity, chemistry, immunology, microbiology, safety, technology},
  publisher = {Wiley},
  address   = {Weinheim},
  issn      = {1613-4125},
  doi       = {10.1002/mnfr.200600043},
  pages     = {696 -- 704},
  year      = {2006},
  abstract  = {Plant phenolic compounds are known to interact with proteins producing changes in the food (e.g., biological value (BV), color, taste). Therefore, the in vivo relevance, especially, of covalent phenolprotein reactions on protein quality was studied in a rat bioassay. The rats were fed protein derivatives at a 10\% protein level. Soy proteins were derivatized with chlorogenic acid and quercetin (derivatization levels: 0.056 and 0.28 mmol phenolic compound/gram protein). Analysis of nitrogen in diets, urine, and fecal samples as well as the distribution of amino acids were determined. Depending on the degree of derivatization, the rats fed with soy protein derivatives showed an increased excretion of fecal and urinary nitrogen. As a result, true nitrogen digestibility, BV, and net protein utilization were adversely affected. Protein digestibility corrected amino acid score was decreased for lysine, tryptophan, and sulfur containing amino acids.},
  language  = {en}
}