Disease relevance of BST1

• A 15-mer random peptide phage library was screened with a soluble form of BST-1 expressed in baculovirus-infected insect cells [1].

High impact information on BST1

• The deduced amino acid sequence of BST-1 exhibited 33% identity with CD38 [2].
• BST-1 expression was enhanced in rheumatoid arthritis patient-derived bone marrow stromal cell lines that were previously shown to have an enhanced ability to support the growth of a pre-B-cell line as compared with stromal cell lines derived from healthy donors [2].
• BST-1, a surface molecule of bone marrow stromal cell lines that facilitates pre-B-cell growth [2].
• BST-1 was expressed in a wide range of tissues and in umbilical vein endothelial cells, whereas it was scarcely expressed in a variety of hematopoietic cell lines [2].
• The gene for BST-1 was assigned to chromosome 14q32.3, where immunoglobulin heavy-chain genes are clustered [2].

Biological context of BST1

• Cross-linking of BST-1 overexpressed on a transfectant induced tyrosine phosphorylation of p130, dephosphorylation of the 100-kDa protein, and growth inhibition [3].
• The human BST-1 gene consisted of nine exons and eight introns [4].
• We have previously identified and cloned BST-1 as a molecule which is overexpressed on the bone marrow stromal cell lines derived from patients with rheumatoid arthritis and which has the ability to support the pre-B cell growth [3].
• Since these events include enhanced cell proliferation and since the bone marrow harbors both ectoenzymes that generate cADPR from NAD(+) (CD38 and BST-1), we investigated the effects of extracellular cADPR on human hemopoietic progenitors (HP) [5].
• The two synthetic peptides corresponding to the identified sequences were shown to antagonize each other's ability to inhibit the binding of the two isolated phage to BST-1, suggesting that they bind at a common binding site on BST-1 [1].

Anatomical context of BST1

• BST-1 is an ectoenzyme expressed on human bone marrow Stromal cells and myeloid lineage cells, having both ADP-ribosyl cyclase and cyclic ADP-ribose (cADPR) hydrolase activities [4].
• As a step toward elucidating the physiological role of cADPR in insulin secretion we examined whether BST-1 is expressed in pancreatic islet cells [6].
• Human BST-1 expressed on myeloid cells functions as a receptor molecule [3].
• In this report, we demonstrate that human BST-1 was expressed on monocytes, granulocytes in the peripheral blood of healthy donors, and macrophages matured in vitro [3].
• Markers indicative for a facilitated recruitment and stimulation of hematopoetic progenitor cells (HPC), including BST-1 and SDF-1, were also induced [7].

Associations of BST1 with chemical compounds

• We determined the crystal structures of the extracellular region of human BST-1 at atomic resolution in the free form and in complexes with five substrate analogues: nicotinamide, NMN, ATPgammaS, ethenoNADP, and ethenoNAD [8].
• cADP-ribose, which is produced by ecto-ADP-ribosyl cyclase of CD38 or bone marrow stromal cell antigen-1 (BST-1), is a key regulator of Ca2+-induced calcium release in an Ins(1,4,5)P3-independent manner [1].
• It has an apparent molecular mass of 38.5 kDa on SDS-PAGE gel stained with Coomassie blue and is recognized on Western blots by a rabbit polyclonal antibody against BST-1 [9].

Other interactions of BST1

• The human CD38 gene: polymorphism, CpG island, and linkage to the CD157 (BST-1) gene [10].

Analytical, diagnostic and therapeutic context of BST1

• In this paper, we report the molecular cloning of a stromal cell line-derived glycosyl-phosphatidylinositol-anchored molecule, BST-1, that facilitates pre-B-cell growth [2].

References