In vivo studies have shown that the uptake of plasma arginine by the lactating porcine mammary gland greatly exceeds the output of arginine in milk, but little is known about the metabolic fate of arginine in this organ. The objective of this study was to quantify arginine catabolism via arginase and nitric oxide synthase pathways in the mammary tissue of sows on d 28 of lactation. Mammary tiss...

We hypothesized recently that arginine homeostasis is achieved in humans largely by modulating the rate of arginine degradation. We have tested this hypothesis further by measuring in vivo the whole body rate of conversion of arginine to ornithine and ornithine oxidation in six healthy young adults. Subjects received for 6 days an L-amino acid-based diet supplying an arginine-rich or arginine-f...

Enhanced arginase-induced arginine consumption is believed to play a key role in the pathogenesis of sickle cell disease-induced end organ failure. Enhancement of arginine availability with L-arginine supplementation exhibited less consistent results; however, L-citrulline, the precursor of L-arginine, may be a promising alternative. In this study, we determined the effects of L-citrulline comp...

This study characterizes the effects of L-arginine and NG-monomethyl L-arginine on dilator responsiveness of vascular tissue from Wistar-Kyoto rats and stroke-prone spontaneously hypertensive rats. Rings of abdominal aorta were suspended in tissue baths for measurement of isometric force. After contraction induced by phenylephrine, cumulative addition of acetylcholine, L-arginine, or A23187 to ...

Schimke, Robert T. (National Institutes of Health, Bethesda, Md.) and Michael F. Barile. Arginine metabolism in pleuropneumonia-like organisms isolated from mammalian cell culture. J. Bacteriol. 86:195-206. 1963.-Arginine degradation is a significant metabolic process for pleuropneumonia-like organisms (PPLO; Mycoplasma) isolated from cell culture. The conversion of arginine to ornithine in PPL...

PRMTs (protein arginine N-methyltransferases) specifically modify the arginine residues of key cellular and nuclear proteins as well as histone substrates. Like lysine methylation, transcriptional repression or activation is dependent upon the site and type of arginine methylation on histone tails. Recent discoveries imply that histone arginine methylation is an important modulator of dynamic c...