Differential effects of milk proteins, BSA and soy protein on 4NQO- or MNNG-induced SCEs in V79 cells.
The possible antimutagenic effects of five different proteins against the mutagen 4-nitroquinoline 1-oxide (4NQO) were assessed in a mammalian cell system, using the sister chromatid exchange (SCE) test in Chinese hamster cells (V79). For this purpose the proteins casein, bovine serum albumin (BSA), soy protein, total whey protein and beta-lactoglobulin were studied, as well as pepsin-hydrolysed casein. In addition, the effect of casein on 1-methyl-1-nitroso-3-nitroguanidine (MNNG) was studied. The proteins were tested at a concentration of 1.15% (w/v). Casein was studied over a concentration range of 0 to 1.15% (w/v). A non-toxic concentration was used for the mutagens. Casein hydrolysis by pepsin took place in vitro, simulating human stomach conditions, which resulted in 84% non-casein-N and 16% remaining casein-N. Casein significantly inhibited SCE induction by 4NQO (inhibition 78%, at 1.15% casein, P < 0.05) and by MNNG (83%, at 1.15% casein, P < 0.01). BSA also significantly inhibited 4NQO-induced SCEs (94%, at 1.15% BSA; P < 0.01). However, soy protein, the whey protein fraction of milk and beta-lactoglobulin showed no inhibitory effects. Pepsin-hydrolysed casein inhibited SCE induction by 4NQO and MNNG to a similar extent as non-hydrolysed casein. It is concluded that casein, its pepsin hydrolysis products and BSA may protect mammalian cells against certain genotoxic compounds, whereas other milk proteins, such as whey protein, beta-lactoglobulin and soy protein, do not have this protective action. Although the mechanism of antimutagenicity is unknown, it seems plausible that the protein acts as a blocking agent by chemical or physical interaction with the mutagens. The accessibility of protein molecules and the presence of nucleophilic binding sites may be decisive factors in determining antimutagenic properties of proteins.
Department of Toxicology, Wageningen Agricultural University, The Netherlands.
I E
IE
Bosselaers
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PW
Caessens
M A
MA
Van Boekel
G M
GM
Alink
D015112:4-Nitroquinoline-1-oxide / Q000633:toxicity; D000818:Animals; D016587:Antimutagenic Agents / Q000378:metabolism / Q000494:pharmacology*; D016466:CHO Cells; D002364:Caseins / Q000378:metabolism / Q000494:pharmacology*; D002417:Cattle; D006224:Cricetinae; D003412:Cricetulus; D004249:DNA Damage / Q000187:drug effects; D004260:DNA Repair / Q000187:drug effects; D004305:Dose-Response Relationship, Drug; D006868:Hydrolysis; D007782:Lactoglobulins / Q000378:metabolism / Q000494:pharmacology; D008769:Methylnitronitrosoguanidine / Q000633:toxicity; D008894:Milk Proteins / Q000378:metabolism / Q000494:pharmacology; D008954:Models, Biological; D009154:Mutation / Q000187:drug effects / Q000235:genetics; D010434:Pepsin A / Q000494:pharmacology; D014674:Plant Proteins, Dietary / Q000378:metabolism / Q000494:pharmacology*; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000378:metabolism / Q000494:pharmacology*; D012854:Sister Chromatid Exchange / Q000187:drug effects*; D030262:Soybean Proteins; D013025:Glycine max; D000067816:Whey Proteins
D016587:Antimutagenic Agents; D002364:Caseins; D007782:Lactoglobulins; D008894:Milk Proteins; D014674:Plant Proteins, Dietary; D030262:Soybean Proteins; D000067816:Whey Proteins; D008769:Methylnitronitrosoguanidine; D012710:Serum Albumin, Bovine; D015112:4-Nitroquinoline-1-oxide; D010434:Pepsin A