The enigmatic role of glutamyl aminopeptidase (BP-1/6C3 antigen) in immune system development.
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.
Wang
J
J
Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
Lin
Q
Q
Wu
Q
Q
Cooper
M D
MD
D000626:Aminopeptidases / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D000818:Animals; D001402:B-Lymphocytes / Q000378:metabolism; D043384:Glutamyl Aminopeptidase; D006801:Humans; D007107:Immune System / Q000254:growth & development; D015851:Interleukin-7 / Q000494:pharmacology; D008666:Metalloendopeptidases / Q000737:chemistry / Q000276:immunology / Q000378:metabolism / Q000502:physiology*
D015851:Interleukin-7; D000626:Aminopeptidases; D043384:Glutamyl Aminopeptidase; C062906:BP-1-6C3 antigen; D008666:Metalloendopeptidases