INTERACTIONS OF LABELED EPIDIDYMAL SECRETORY PROTEINS WITH SPERMATOZOA AFTER INJECTION OF S-35 METHIONINE IN THE MOUSE
INTERACTIONS OF LABELED EPIDIDYMAL SECRETORY PROTEINS WITH SPERMATOZOA AFTER INJECTION OF S-35 METHIONINE IN THE MOUSE
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DOI：
10.1095/biolreprod43.1.121
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发表时间：
1990-07-01
影响因子：
3.6
通讯作者：
ORGEBINCRIST, MC
中科院分区：
文献类型：
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作者：
CORNWALL, GA;VREEBURG, JT;ORGEBINCRIST, MC
在附睾运输过程中，附睾分泌蛋白与精子的顺序相互作用进行了研究。小鼠接受35 S-蛋氨酸注射，并在注射后不同时间通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析放射性标记的腔液和精子相关蛋白。大多数的腔液和精子相关蛋白被发现在附睾头在8小时，7天，这些蛋白质中的许多已被运送到附睾尾。两类附睾蛋白-精子相互作用的区域合成和分泌的基础上区分。主要类别包括在附睾头中合成、分泌和与精子结合的蛋白质。然而，在这一类中，蛋白质与精子的结合是可变的。例如，25 kDa的蛋白质在附睾转运过程中仍与精子大量结合，而40和35 kDa的蛋白质数量减少。其他蛋白质，如18 kDa的蛋白质没有保持与精子相关。另一类蛋白质（54，44，29 kDa）的合成和分泌的所有附睾区域，但仅结合到头部精子。大多数附睾蛋白似乎与精子紧密结合，因为精子在远端附睾中已经被未标记蛋白饱和，即使精子被腔液中的标记蛋白包围，精子仍然如此。这些研究表明，附睾分泌蛋白和精子之间发生了各种特定的相互作用，因为他们在附睾迁移和成熟。
The sequential interactions of epididymal secretory proteins with spermatozoa during epididymal transit were examined. Mice received injections of 35S-methionine, and the radiolabeled luminal fluid and sperm-associated proteins were analyzed by sodium dodecylsulfate-polyacrylamide gel electrophoresis at various times after injection. The majority of the luminal fluid and sperm-associated proteins were found in the caput epididymidis at 8 h; by 7 days, many of these proteins had been transported to the cauda epididymidis. Two classes of epididymal protein-sperm interactions were distinguished on the basis of regional synthesis and secretion. The major class consisted of proteins that were synthesized, secreted, and bound to spermatozoa in the caput epididymidis. In this class, however, the binding of proteins to the spermatozoa was variable. For example, a protein of 25 kDa remained associated with spermatozoa in substantial amounts during epididymal transit, while proteins of 40 and 35 kDa decreased in amount. Other proteins such as a protein of 18 kDa did not remain associated with spermatozoa. Another class of proteins (54, 44, 29 kDa) were synthesized and secreted from all epididymal regions but bound only to caput spermatozoa. Most of the epididymal proteins appeared to be tightly bound to the spermatozoa since spermatozoa already saturated with the unlabeled protein in the distal epididymis remained so even though the spermatozoa were surrounded by labeled proteins in the luminal fluid. These studies demonstrate that a variety of specific interactions occur between epididymal secretory proteins and spermatozoa as they migrate and mature in the epididymis.