The enigmatic role of glutamyl aminopeptidase (BP-1/6C3 antigen) in immune system development

Immunological Reviews
J WangM D Cooper

Abstract

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.

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Citations

Feb 27, 2001·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·C AntczakB Bauvois
Nov 7, 2002·Toxicon : Official Journal of the International Society on Toxinology·Elaine Gasparello-Clemente, Paulo Flávio Silveira
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Apr 29, 1998·Immunological Reviews·J W Goding, M C Howard

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