RUPTURE OF RAT-LIVER LYSOSOMES MEDIATED BY L-AMINO-ACID ESTERS
RUPTURE OF RAT-LIVER LYSOSOMES MEDIATED BY L-AMINO-ACID ESTERS
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DOI：
10.1016/0005-2736(73)90114-4
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发表时间：
1973-01-01
期刊：
影响因子：
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通讯作者：
KAPLAN, A
中科院分区：
文献类型：
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作者：
GOLDMAN, R;KAPLAN, A
用0.5-20 mM α-L-氨基酸酯处理大鼠肝溶酶体悬液导致溶酶体酶活性的潜伏期逐渐丧失。溶酶体悬浮液中酸性磷酸酶活性的增加与这些悬浮液的浊度的降低相关。酯介导的浊度降低依赖于酯浓度、悬浮介质的pH和离子强度。氨基酸酯的d-立体异构体没有表现出相当的破坏溶酶体的能力。发现α-l-氨基酸酯是中性溶酶体酯酶和转肽酶活性的底物。右旋立体异构体的降解速率要低得多。这些数据支持这样的假设，即酯依赖性溶酶体破裂是由酯与结构或功能性溶酶体蛋白的特异性相互作用介导的。
Treatment of rat liver lysosome suspensions with 0.5–20 mM α-l-amino acid esters results in a progressive loss of latency of lysosomal enzyme activity. The increase in available acid phosphatase activity in lysosomal suspensions is correlated with the decrease of turbidity of these suspensions. Ester mediated turbidity decrease is dependent upon ester concentration, and the pH and ionic strength of the suspending medium.d-Stereoisomers of amino acid esters do not exhibit comparable capacity to damage lysosomes.α-l-Amino acid esters were found to be substrates for neutral lysosomal esterase and transpeptidase activity. Thed-stereoisomers are degraded at much lower rates. These data support the hypothesis that ester dependent lysosomal rupture is mediated by the specific interaction of the ester with a structural or functional lysosomal protein.