Lane T A, Beutler E, West C, Lamkin G
Transfusion. 1984 Mar-Apr;24(2):153-6. doi: 10.1046/j.1537-2995.1984.24284173348.x.
A marked reduction of granulocyte chemotactic function accompanies the storage of granulocyte concentrates. Since chemotaxis is energy dependent, we studied energy metabolism in stored neutrophils. We and others have reported that stored neutrophils have a defect in their energy metabolism. We found that defective adenosine triphosphate maintenance in stored neutrophils was occult in resting cells, but was unmasked by an energy-intensive stimulus, phagocytosis. In studies reported here, we sought to determine if defective adenosine triphosphate maintenance during granulocyte storage was related to altered glycolytic enzyme activity. We studied the activity of glycolytic enzymes in fresh and stored, resting and stimulated (opsonized zymosan) neutrophils. The following enzyme activities showed no major changes during storage, in resting or stimulated neutrophils: hexokinase, phosphofructokinase, aldolase, glucose phosphate isomerase, triose phosphate isomerase, glyceraldehyde phosphate dehydrogenase, phosphoglycerate kinase, phosphoglyceromutase, enolase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase, glutathione reductase, and glutathione peroxidase. In contrast, pyruvate kinase activity consistently increased during storage. In 6 units, pyruvate kinase activity increased by 75 percent after 24 hours of storage at room temperature and by 198 percent after 48 hours. The storage-associated increase in pyruvate kinase activity was not inhibited by cycloheximide. Stimulation of neutrophils by phagocytosis of opsonized zymosan also produced striking increases in the pyruvate kinase activity of both fresh and stored cells. Additional studies indicated that the increases in pyruvate kinase activity observed during storage and after phagocytosis were associated with an increase in the availability of pyruvate kinase activity in the supernatant fraction of neutrophil sonicates. Total pyruvate kinase activity in sonicates of neutrophils was unchanged by storage or particle ingestion.(ABSTRACT TRUNCATED AT 250 WORDS)
粒细胞趋化功能的显著降低伴随着粒细胞浓缩物的储存过程。由于趋化作用依赖能量，我们研究了储存中性粒细胞的能量代谢。我们及其他人曾报道储存的中性粒细胞存在能量代谢缺陷。我们发现，储存中性粒细胞中三磷酸腺苷维持缺陷在静息细胞中不明显，但在能量密集型刺激（吞噬作用）下会显现出来。在本文报道的研究中，我们试图确定粒细胞储存期间三磷酸腺苷维持缺陷是否与糖酵解酶活性改变有关。我们研究了新鲜的和储存的、静息的和受刺激的（经调理的酵母聚糖）中性粒细胞中糖酵解酶的活性。在储存期间，无论是静息还是受刺激的中性粒细胞，以下酶活性均无重大变化：己糖激酶、磷酸果糖激酶、醛缩酶、磷酸葡萄糖异构酶、磷酸丙糖异构酶、甘油醛 - 3 - 磷酸脱氢酶、磷酸甘油酸激酶、磷酸甘油酸变位酶、烯醇化酶、乳酸脱氢酶、葡萄糖 - 6 - 磷酸脱氢酶、谷胱甘肽还原酶和谷胱甘肽过氧化物酶。相比之下，丙酮酸激酶活性在储存期间持续增加。在6个单位中，丙酮酸激酶活性在室温下储存24小时后增加了75%，48小时后增加了198%。储存相关的丙酮酸激酶活性增加不受放线菌酮抑制。经调理的酵母聚糖吞噬刺激中性粒细胞也使新鲜和储存细胞的丙酮酸激酶活性显著增加。进一步研究表明，储存期间和吞噬后观察到的丙酮酸激酶活性增加与中性粒细胞超声裂解物上清液部分中丙酮酸激酶活性的可用性增加有关。中性粒细胞超声裂解物中的总丙酮酸激酶活性不受储存或颗粒摄取的影响。（摘要截短于250字）
