Inactive and highly active, proteolytically processed transglutaminase-5 in epithelial cells.
Inactive and highly active, proteolytically processed transglutaminase-5 in epithelial cells.
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上皮细胞中的非活性和高活性、蛋白水解加工的转谷氨酰胺酶 5。
DOI：
10.1038/jid.2008.146
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发表时间：
2008
期刊：
影响因子：
--
通讯作者：
G. Melino
中科院分区：
文献类型：
--
作者：
V. Pietroni;S. Di Giorgi;A. Paradisi;B. Ahvazi;E. Candi;G. Melino
转谷氨酰胺酶（transmartaminases，TG）是一种钙离子依赖性酶，能催化谷氨酰胺残基发生转酰胺作用，形成分子间的异肽键。这些酶参与各种生物现象，包括血液凝固、伤口愈合、细胞死亡、组织修复和角质形成细胞的终末分化。在TG家族成员中，TG 5是最新鉴定的酶之一，因此在功能水平上的特征较少。在这项工作中，我们报道了TG 5在杆状病毒表达系统和哺乳动物上皮细胞中被蛋白水解加工。类似于TG家族的其他成员-TG 1、TG 3和因子XIIIa -，TG 5全长酶具有非常低的酶活性，而53-kDa蛋白水解加工形式具有高活性。
Transglutaminases (TGs) are Ca(2+)-dependent enzymes capable of catalyzing transamidation of glutamine residues to form intermolecular isopeptide bonds. These enzymes are involved in various biological phenomena, including blood coagulation, wound healing, cell death, tissue repair, and terminal differentiation of keratinocytes. Among the TG-family members, TG5 is one of the latest identified enzymes and therefore the less characterized at the functional level. In this work, we reported that TG5 is proteolytically processed in the baculovirus expression system and in mammal epithelial cells. Similar to other members of the TG family-TG1, TG3, and factor XIIIa -, TG5 full-length enzyme has very low enzymatic activity, while the 53-kDa proteolytically processed form is highly active.