The Xenopus laevis cortical granule lectin:: cDNA cloning, developmental expression, and identification of the eglectin family of lectins
The Xenopus laevis cortical granule lectin:: cDNA cloning, developmental expression, and identification of the eglectin family of lectins
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DOI：
10.1016/s1095-6433(03)00269-1
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发表时间：
2004-01-01
影响因子：
2.3
通讯作者：
Hedrick, JL
中科院分区：
文献类型：
--
作者：
Chang, BY;Peavy, TR;Hedrick, JL
非洲爪蟾卵皮质颗粒、钙依赖性、半乳糖基特异性凝集素参与卵包膜受精层的形成，并在建立多精受精阻断中发挥作用。我们报告了凝集素的 cDNA 克隆、卵子发生和早期发育过程中皮质颗粒凝集素基因的表达，以及新凝集素家族的鉴定。皮质颗粒凝集素的翻译cDNA具有信号肽、298个氨基酸的结构序列、分子量32.7K、包含N-糖基化的共有序列位点和纤维蛋白原结构域。凝集素 cDNA 在卵子发生的早期阶段表达。凝集素糖蛋白水平在发育过程中保持恒定，其中 2/3 的凝集素与细胞外卵周间隙和卵/胚胎受精包膜相关。卵巢中的凝集素 mRNA 水平比其他成体组织高 100 至 1000 倍。该凝集素与先前鉴定的凝集素家族没有序列同源性。该凝集素与来自海鞘、七鳃鳗、青蛙、小鼠和人类的九个翻译的 cDNA 序列具有 41-88% 的氨基酸同一性。基于这些糖蛋白的保守碳水化合物结合和结构特性，我们提出了一个新的凝集素家族，即eglectin家族。 (C) 2003 Elsevier Inc. 保留所有权利。
A Xenopus laevis egg cortical granule, calcium-dependent, galactosyl-specific lectin participates in forming the fertilization layer of the egg envelope and functions in establishing a block to polyspermy. We report the cDNA cloning of the lectin, expression of the cortical granule lectin gene during oogenesis and early development, and identification of a new family of lectins. The translated cDNA for the cortical granule lectin had a signal peptide, a structural sequence of 298 amino acids, a molecular weight of 32.7 K, contained consensus sequence sites for N-glycosylation and a fibrinogen domain. The lectin cDNA was expressed during early stages of oogenesis. Lectin glycoprotein levels were constant during development with 2/3 of the lectin associated with the extracellular perivitelline space and the egg/embryo fertilization envelope. Lectin mRNA levels were from 100- to 1000-fold greater in ovary than in other adult tissues. The lectin had no sequence homology to the previously identified lectin families. The lectin had 41-88% amino acid identity with nine translated cDNA sequences from an ascidian, lamprey, frog, mouse, and human. Based on the conserved carbohydrate binding and structural properties of these glycoproteins, we propose a new family of lectins, the eglectin family. (C) 2003 Elsevier Inc. All rights reserved.