Wang J, Lin Q, Wu Q, Cooper M D
Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
Immunol Rev. 1998 Feb;161:71-7. doi: 10.1111/j.1600-065x.1998.tb01572.x.
The murine B-lymphocyte differentiation antigen BP-1/6C3, a homodimeric integral membrane protein composed of M, 140,000 subunits, has been identified as glutamyl aminopeptidase (EAP, EC 3.4.11.7). This ecto-enzyme cleaves acidic amino acid residues from the amino terminal of polypeptide substrates such as angiotensin II and cholecystokinin-8. Although BP-1/6C3/EAP is expressed by cells in many tissues, among hematopoietic cell lineages this ecto-enzyme is restricted to immature B-lineage cells where its expression is upregulated by interleukin-7 and viral transformation. BP-1/6C3/EAP thus serves as a valuable marker of progression along the B-cell differentiation pathway, but a corresponding biological role has not yet been established.
小鼠B淋巴细胞分化抗原BP-1/6C3是一种由分子量为140,000的亚基组成的同型二聚体整合膜蛋白,已被鉴定为谷氨酰胺氨基肽酶(EAP,EC 3.4.11.7)。这种胞外酶可从多肽底物如血管紧张素II和胆囊收缩素-8的氨基末端切割酸性氨基酸残基。尽管BP-1/6C3/EAP在许多组织的细胞中都有表达,但在造血细胞谱系中,这种胞外酶仅限于未成熟的B谱系细胞,其表达在白细胞介素-7和病毒转化作用下上调。因此,BP-1/6C3/EAP可作为B细胞分化途径进展的重要标志物,但尚未确定其相应的生物学作用。