Li X, Tedder T F
Department of Immunology, Duke University Medical Center, Durham, North Carolina 27710, USA.
Genomics. 1999 Feb 1;55(3):345-7. doi: 10.1006/geno.1998.5653.
Sulfation is essential for the generation of functional vascular endothelial cell ligands for the leukocyte adhesion molecule, L-selectin. Therefore, human vascular endothelium cDNA libraries were screened to identify sulfotransferases homologous to chicken chondroitin 6-sulfotransferase (C6ST). Two sulfotransferases were identified: CHST2, a novel 530-amino-acid sulfotransferase with a carboxyl-terminal region that was 45 and 43% homologous with those of human and chicken C6ST, respectively, and CHST1, which was identical to human C6ST. Northern blot analysis showed that CHST2 was broadly expressed among tissues. The CHST2 gene mapped to human chromosome 3q24 close to 3q25. Thus, this study identified two sulfotransferases expressed by vascular endothelial cells that may contribute to the generation of L-selectin ligands during inflammatory responses.
硫酸化对于生成白细胞粘附分子L-选择素的功能性血管内皮细胞配体至关重要。因此,对人血管内皮cDNA文库进行筛选,以鉴定与鸡软骨素6-硫酸转移酶(C6ST)同源的硫酸转移酶。鉴定出了两种硫酸转移酶:CHST2,一种新型的530个氨基酸的硫酸转移酶,其羧基末端区域分别与人及鸡C6ST的羧基末端区域有45%和43%的同源性;以及CHST1,它与人C6ST相同。Northern印迹分析表明CHST2在多种组织中广泛表达。CHST2基因定位于人染色体3q24,靠近3q25。因此,本研究鉴定出两种由血管内皮细胞表达的硫酸转移酶,它们可能在炎症反应过程中有助于L-选择素配体的生成。