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Characterization of POMT2, a novel member of the PMT protein O-mannosyltransferase family specifically localized to the acrosome of mammalian spermatids.
Glycobiology ( IF 3.4 ) Pub Date : 2002-12-04 , DOI: 10.1093/glycob/cwf086
Tobias Willer 1 , Werner Amselgruber , Rainer Deutzmann , Sabine Strahl
Affiliation  

Over the past few years it has emerged that O-mannosyl glycans are not restricted to yeasts and fungi but are also present in higher eukaryotes, including humans. They play a substantial role in the onset of muscular dystrophy and neuronal migration disorders, like muscle-eye-brain disease. Protein O-mannosyltransferase genes (PMTs) are evolutionarily conserved from yeast to human; however, little is known about these enzymes in higher eukaryotes. In this study, we cloned the first PMT2 subfamily members from human (hPOMT2), mouse (mPomt2), and Drosophila (DmPOMT2). A detailed characterization of the mammalian POMT2, with emphasis on mouse Pomt2, shows that mammalian POMT2 is predominantly expressed in testis tissue. Due to differential transcription initiation of the mPomt2 gene, two distinct mRNA species that vary in length are formed. The shorter transcript is present in all somatic tissues examined. Expression of the corresponding hPOMT2 cDNA in mammalian cells identified POMT2 as an integral membrane protein of the endoplasmic reticulum with an apparent molecular weight of 83 kDa. The longer mPomt2 transcript is restricted to testis and encodes a testis-specific mPOMT2 protein isoform. Using in situ hybridization and immunolocalization, we demonstrate that in testis tissue mPOMT2 localizes to maturing spermatids and is abundant within the acrosome, a sperm-specific organelle essential for fertilization. Our data suggest a novel and specific role for the putative protein O-mannosyltransferase POMT2 in the maturation and/or function of sperm in mammals.

中文翻译:

POMT2的表征,它是PMT蛋白O-甘露糖基转移酶家族的一个新成员,专门定位于哺乳动物精子的顶体。

在过去的几年中,已经发现O-甘露糖基聚糖不仅限于酵母和真菌,而且还存在于包括人在内的高级真核生物中。它们在肌肉营养不良和神经元迁移失调的发作中起重要作用,例如肌肉眼脑疾病。蛋白质O-甘露糖基转移酶基因(PMT)从酵母到人类在进化上是保守的;然而,对于高等真核生物中的这些酶知之甚少。在这项研究中,我们从人(hPOMT2),小鼠(mPomt2)和果蝇(DmPOMT2)克隆了第一个PMT2亚家族成员。哺乳动物POMT2的详细表征(重点放在小鼠Pomt2上)表明,哺乳动物POMT2主要在睾丸组织中表达。由于mPomt2基因的差异转录起始,形成了两个不同的长度不同的mRNA。较短的转录本存在于所有检查的体细胞组织中。相应的hPOMT2 cDNA在哺乳动物细胞中的表达将POMT2鉴定为表观分子量为83 kDa的内质网的完整膜蛋白。较长的mPomt2转录物仅限于睾丸,并编码睾丸特异性mPOMT2蛋白同工型。使用原位杂交和免疫定位,我们证明在睾丸组织中,mPOMT2定位于成熟的精子,并在顶体中丰富,顶体是受精所必需的精子特异性细胞器。我们的数据表明,推定的蛋白质O-甘露糖基转移酶POMT2在哺乳动物精子的成熟和/或功能中具有新颖而特殊的作用。相应的hPOMT2 cDNA在哺乳动物细胞中的表达将POMT2鉴定为表观分子量为83 kDa的内质网的完整膜蛋白。较长的mPomt2转录物仅限于睾丸,并编码睾丸特异性mPOMT2蛋白同工型。使用原位杂交和免疫定位,我们证明在睾丸组织中,mPOMT2定位于成熟的精子,并在顶体中丰富,顶体是受精所必需的精子特异性细胞器。我们的数据表明,推定的蛋白质O-甘露糖基转移酶POMT2在哺乳动物精子的成熟和/或功能中具有新颖而特殊的作用。相应的hPOMT2 cDNA在哺乳动物细胞中的表达将POMT2鉴定为表观分子量为83 kDa的内质网的完整膜蛋白。较长的mPomt2转录物仅限于睾丸,并编码睾丸特异性mPOMT2蛋白同工型。使用原位杂交和免疫定位,我们证明在睾丸组织中,mPOMT2定位于成熟的精子,并在顶体中丰富,顶体是受精所必需的精子特异性细胞器。我们的数据表明,推定的蛋白质O-甘露糖基转移酶POMT2在哺乳动物精子的成熟和/或功能中具有新颖而特殊的作用。较长的mPomt2转录物仅限于睾丸,并编码睾丸特异性mPOMT2蛋白同工型。使用原位杂交和免疫定位,我们证明在睾丸组织中,mPOMT2定位于成熟的精子,并在顶体中丰富,顶体是受精所必需的精子特异性细胞器。我们的数据表明,推定的蛋白质O-甘露糖基转移酶POMT2在哺乳动物精子的成熟和/或功能中具有新颖而特殊的作用。较长的mPomt2转录物仅限于睾丸,并编码睾丸特异性mPOMT2蛋白同工型。使用原位杂交和免疫定位,我们证明在睾丸组织中,mPOMT2定位于成熟的精子,并在顶体中丰富,顶体是受精所必需的精子特异性细胞器。我们的数据表明,推定的蛋白质O-甘露糖基转移酶POMT2在哺乳动物精子的成熟和/或功能中具有新颖而特殊的作用。
更新日期:2019-11-01
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