Department of Animal Science, Texas A&M University, College Station, TX, 77843-2471, USA.
Animal Nutrition, Graduate School of Agricultural Science, Tohoku University, Sendai, 980-8572, Japan.
Amino Acids. 2021 Nov;53(11):1739-1748. doi: 10.1007/s00726-021-03084-7. Epub 2021 Oct 6.
Polyamines (putrescine, spermidine, and spermine) are synthesized primarily from ornithine via ornithine decarboxylase (ODC) in mammals. Although avian tissues contain ODC activity, little is known about intracellular sources of ornithine for their polyamine synthesis. This study tested the hypothesis that arginase and proline oxidase contribute to polyamine synthesis in chickens. Kidney, jejunum, leg muscle, and liver from 0-, 7-, 14- and 21-day-old broiler chickens were assayed for the activities of arginase, proline oxidase (POX), ornithine aminotransferase (OAT), and ornithine decarboxylase (ODC). Kidney slices were also used to determine C-polyamine synthesis from [U-C]arginine and [U-C]proline. Furthermore, these tissues and plasma were analyzed for polyamines. Results indicate that all tissues contained OAT (mitochondrial) and ODC (cytosolic) activities, but arginase and POX activities were only detected in the mitochondria of chicken kidneys. Renal POX and arginase activities were greater at 7 days of age compared to newly hatched birds, and declined by Day 14. Renal arginase activity was greater at 21 days compared to 14 days of age, but there was no change in renal POX activity during that same period. Concentrations of polyamines in the kidneys and plasma were greater on Day 7 compared to Day 0 and decreased thereafter on Days 14 and 21. Kidney slices readily converted arginine and proline into polyamines, with peak rates being on Day 7. Concentrations of putrescine, spermidine and spermine in the plasma of chickens were about 20- to 100-fold greater than those in mammals. Our results indicate that polyamines are synthesized from arginine and proline in avian kidneys. Unlike mammals, polyamines released from the kidneys are likely the major source of polyamines in the blood and other extra-renal tissues in chickens.
多胺(腐胺、精脒和精胺)主要通过哺乳动物中的鸟氨酸脱羧酶(ODC)从鸟氨酸合成。尽管禽类组织中含有 ODC 活性,但关于其多胺合成的鸟氨酸细胞内来源知之甚少。本研究检验了这样一个假设,即精氨酸酶和脯氨酸氧化酶有助于鸡的多胺合成。对 0、7、14 和 21 日龄肉鸡的肾脏、空肠、腿部肌肉和肝脏进行了精氨酸酶、脯氨酸氧化酶(POX)、鸟氨酸氨基转移酶(OAT)和鸟氨酸脱羧酶(ODC)的活性测定。还使用肾切片测定了[U-C]精氨酸和[U-C]脯氨酸的 C-多胺合成。此外,还分析了这些组织和血浆中的多胺。结果表明,所有组织均含有 OAT(线粒体)和 ODC(细胞质)活性,但仅在鸡肾脏的线粒体中检测到精氨酸酶和 POX 活性。与刚孵化的雏鸡相比,肾脏 POX 和精氨酸酶活性在 7 日龄时更高,并在 14 日龄时下降。与 14 日龄相比,21 日龄肾脏精氨酸酶活性更高,但在此期间肾脏 POX 活性没有变化。肾脏和血浆中的多胺浓度在 7 日龄时高于 0 日龄,此后在 14 日龄和 21 日龄时降低。肾切片可轻易将精氨酸和脯氨酸转化为多胺,峰值出现在第 7 天。鸡血浆中腐胺、精脒和精胺的浓度比哺乳动物高约 20-100 倍。我们的结果表明,多胺是在禽类肾脏中从精氨酸和脯氨酸合成的。与哺乳动物不同,从肾脏释放的多胺可能是鸡血液和其他肾外组织中多胺的主要来源。