Abstract
Human CD157/BST-1 and CD38 are dual receptor-enzymes derived by gene duplication that belong to the ADP ribosyl cyclase gene family. First identified over 30 years ago as Mo5 myeloid differentiation antigen and 10 years later as Bone Marrow Stromal Cell Antigen 1 (BST-1), CD157 proved not to be restricted to the myeloid compartment and to have a diversified functional repertoire ranging from immunity to cancer and metabolism. Despite being a NAD+-metabolizing ectoenzyme anchored to the cell surface through a glycosylphosphatidylinositol moiety, the functional significance of human CD157 as an enzyme remains unclear, while its receptor role emerged from its discovery and has been clearly delineated with the identification of its high affinity binding to fibronectin. The aim of this review is to provide an overview of the immunoregulatory functions of human CD157/BST-1 in physiological and pathological conditions. We then focus on CD157 expression in hematological tumors highlighting its emerging role in the interaction between acute myeloid leukemia and extracellular matrix proteins and its potential utility for monoclonal antibody targeted therapy in this disease.
Highlights
CD157 is a glycosylphosphatidylinositol (GPI)-anchored glycoprotein, discovered over three decades ago and originally designated as Mo5 myeloid cell differentiation marker [1]
CD157 is expressed in mouse brain, especially during embryonic development, it has been speculated that it might be involved in the processes of neuronal development that relates to neurologic disorders such as Parkinson’s disease (PD) and autism spectrum disorders (ASD) [16]
We have discussed the basic knowledge of human CD157 addressing its role in the immune system where, besides being a myeloid cell surface marker, it has a central role in the interaction between cells and the extracellular matrix
Summary
CD157 is a glycosylphosphatidylinositol (GPI)-anchored glycoprotein, discovered over three decades ago and originally designated as Mo5 myeloid cell differentiation marker [1]. Our laboratory described a second CD157/BST-1 transcript which encompasses an additional exon interposed between exons 1 and 2 of the BST1 gene (Figure 1) This 10-exon transcript encodes a protein of 333 amino acids, named CD157-002. This serendipitous finding revealed that human CD157 is so far the only member of the ARC gene family regulated by alternative splicing. Human BST1 variants have been described with four single-nucleotide polymorphisms (SNPs) identified as risk factors for sporadic late-onset Parkinson’s disease (PD) in a Japanese GWA study [7], and in the Northern Han Chinese population [8,9], while this finding remains controversial in the European population [10,11]. CD157 is expressed in mouse brain, especially during embryonic development, it has been speculated that it might be involved in the processes of neuronal development that relates to neurologic disorders such as PD and ASD [16]
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