HUMAN CATHEPSIN-D PRECURSOR IS ASSOCIATED WITH A 60-KDA GLYCOSYLATED POLYPEPTIDE
HUMAN CATHEPSIN-D PRECURSOR IS ASSOCIATED WITH A 60-KDA GLYCOSYLATED POLYPEPTIDE
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DOI：
10.1016/s0006-291x(05)80141-x
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发表时间：
1992-01-15
影响因子：
3.1
通讯作者：
HASILIK, A
中科院分区：
文献类型：
--
作者：
GRASSEL, S;HASILIK, A
人组织蛋白酶 D 是作为 53 kDa 前体合成的。它的大部分被分离到溶酶体区室中并进行蛋白水解断裂。使用交联试剂，我们发现大部分前体与一种独特的蛋白质相关，在变性和还原条件下，该蛋白质被表征为 60 kDa 的糖肽。对在已知影响细胞内转运的药物（脱氧野尻霉素、布雷菲德菌素 A 和 NH4Cl）存在下培养的细胞进行的研究表明，与组织蛋白酶 D 前体的结合发生在合成后早期，并且在分泌后至少部分维持。
Human cathepsin D is synthesized as a 53 kDa precursor. Most of it is segregated into lysosomal compartments and subjected to a proteolytic fragmentation. Using a cross-linking reagent we show that a large proportion of the precursor is associated with a distinct protein which - under denaturing and reducing conditions - is characterized as a 60 kDa glycopeptide. Studies on cells cultured in the presence of drugs known to affect the intracellular transport (deoxynojirimycin, brefeldin A and NH4Cl) indicated that the association with cathepsin D precursor occurs early after the synthesis and is at least partially maintained after secretion.