Endogenous oligonucleotides of human milk and their possible biological function.

Abstract

Oligonucleotides (ON) 4 to 60 nucleotides in length were isolated by ion-exchange chromatography on a column with Fractogel TSK DEAE-650 (M) from human milk which was hydrolyzed with proteinase K. ON from 60 to 16 nucleotides were degraded by RNase A but were resistant to DNase I, and, thus, they were ribooligonucleotides. In the presence of [gamma-32P]ATP, ON and heparin inhibited the phosphorylation of 38- and 20-kD milk proteins and failed to affect the phosphorylation of a 76-kD protein. Human milk is believed to contain polyanion-dependent and polyanion-independent protein kinases. The influence of the ON on the activity of the cytotoxic fraction of human milk alpha-lactalbumin towards human mammary gland carcinoma MCF-7 cells was studied. The ON inhibited the cytostatic and cytotoxic effects of alpha-lactalbumin. Synthetic oligonucleotides and heparin had similar effects. The endogenous ON are suggested to be involved in the regulation of cytotoxic activity of human milk.

• Authors: Y Y Kit, E V Kuligina, A M Onishchenko, L V Yurchenko, I V Romannikova, V A Richter, V V Vlassov
• Journal: Biochemistry. Biokhimiia (Biochemistry (Mosc)) Vol. 64 Issue 8 Pg. 896-900 (Aug 1999) ISSN: 0006-2979 [Print] United States
• PMID: 10498805 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Milk Proteins
• Oligoribonucleotides
• Heparin
• Ribonuclease, Pancreatic

Topics

• Chromatography, Ion Exchange
• Electrophoresis, Agar Gel
• Electrophoresis, Polyacrylamide Gel
• Female
• Heparin (pharmacology)
• Humans
• Milk Proteins (metabolism)
• Milk, Human (chemistry, physiology)
• Oligoribonucleotides (chemistry, isolation & purification, pharmacology)
• Phosphorylation
• Ribonuclease, Pancreatic