BST1
ADP-ribosyl cyclase 2 is an enzyme that in humans is encoded by the BST1 gene.[1][2]
Bone marrow stromal cell antigen-1 is a stromal cell line-derived glycosylphosphatidylinositol-anchored molecule that facilitates pre-B-cell growth. The deduced amino acid sequence exhibits 33% similarity with CD38. BST1 expression is enhanced in bone marrow stromal cell lines derived from patients with rheumatoid arthritis. The polyclonal B-cell abnormalities in rheumatoid arthritis may be, at least in part, attributed to BST1 overexpression in the stromal cell population.[2]
See also
References
Further reading
- Ortolan E, Vacca P, Capobianco A, et al. (2003). "CD157, the Janus of CD38 but with a unique personality.". Cell Biochem. Funct. 20 (4): 309–22. doi:10.1002/cbf.978. PMID 12415565.
- Lee BO, Ishihara K, Denno K, et al. (1996). "Elevated levels of the soluble form of bone marrow stromal cell antigen 1 in the sera of patients with severe rheumatoid arthritis.". Arthritis Rheum. 39 (4): 629–37. doi:10.1002/art.1780390414. PMID 8630113.
- Kajimoto Y, Miyagawa J, Ishihara K, et al. (1996). "Pancreatic islet cells express BST-1, a CD38-like surface molecule having ADP-ribosyl cyclase activity.". Biochem. Biophys. Res. Commun. 219 (3): 941–6. doi:10.1006/bbrc.1996.0327. PMID 8645283.
- Okuyama Y, Ishihara K, Kimura N, et al. (1997). "Human BST-1 expressed on myeloid cells functions as a receptor molecule.". Biochem. Biophys. Res. Commun. 228 (3): 838–45. doi:10.1006/bbrc.1996.1741. PMID 8941363.
- Muraoka O, Tanaka H, Itoh M, et al. (1997). "Genomic structure of human BST-1.". Immunol. Lett. 54 (1): 1–4. doi:10.1016/S0165-2478(96)02633-8. PMID 9030974.
- Wimazal F, Ghannadan M, Müller MR, et al. (2000). "Expression of homing receptors and related molecules on human mast cells and basophils: a comparative analysis using multi-color flow cytometry and toluidine blue/immunofluorescence staining techniques.". Tissue Antigens 54 (5): 499–507. doi:10.1034/j.1399-0039.1999.540507.x. PMID 10599889.
- Yamamoto-Katayama S, Sato A, Ariyoshi M, et al. (2001). "Site-directed removal of N-glycosylation sites in BST-1/CD157: effects on molecular and functional heterogeneity.". Biochem. J. 357 (Pt 2): 385–92. doi:10.1042/0264-6021:3570385. PMC 1221964. PMID 11439087. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1221964.
- Liang F, Qi RZ, Chang CF (2001). "Signalling of GPI-anchored CD157 via focal adhesion kinase in MCA102 fibroblasts.". FEBS Lett. 506 (3): 207–10. doi:10.1016/S0014-5793(01)02912-X. PMID 11602246.
- Yamamoto-Katayama S, Ariyoshi M, Ishihara K, et al. (2002). "Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities.". J. Mol. Biol. 316 (3): 711–23. doi:10.1006/jmbi.2001.5386. PMID 11866528.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Funaro A, Ortolan E, Ferranti B, et al. (2005). "CD157 is an important mediator of neutrophil adhesion and migration.". Blood 104 (13): 4269–78. doi:10.1182/blood-2004-06-2129. PMID 15328157.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4.". Nature 434 (7034): 724–31. doi:10.1038/nature03466. PMID 15815621.
- Liu T, Qian WJ, Gritsenko MA, et al. (2006). "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.". J. Proteome Res. 4 (6): 2070–80. doi:10.1021/pr0502065. PMC 1850943. PMID 16335952. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1850943.
PDB gallery
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1isf: Crystal Structure Analysis of BST-1/CD157
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1isg: Crystal Structure Analysis of BST-1/CD157 with ATPgammaS
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1ish: Crystal Structure Analysis of BST-1/CD157 complexed with ethenoNADP
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1isi: Crystal Structure Analysis of BST-1/CD157 complexed with ethenoNAD
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1isj: Crystal Structure Analysis of BST-1/CD157 complexed with NMN
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1ism: Crystal Structure Analysis of BST-1/CD157 complexed with nicotinamide
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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1-50 |
CD1 ( a-c, 1A, 1D, 1E) · CD2 · CD3 ( γ, δ, ε) · CD4 · CD5 · CD6 · CD7 · CD8 ( a) · CD9 · CD10 · CD11 ( a, b, c) · CD13 · CD14 · CD15 · CD16 ( A, B) · CD18 · CD19 · CD20 · CD21 · CD22 · CD23 · CD24 · CD25 · CD26 · CD27 · CD28 · CD29 · CD30 · CD31 · CD32 ( A, B) · CD33 · CD34 · CD35 · CD36 · CD37 · CD38 · CD39 · CD40 · CD41 · CD42 ( a, b, c, d) · CD43 · CD44 · CD45 · CD46 · CD47 · CD48 · CD49 ( a, b, c, d, e, f) · CD50
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51-100 |
CD51 · CD52 · CD53 · CD54 · CD55 · CD56 · CD57 · CD58 · CD59 · CD61 · CD62 ( E, L, P) · CD63 · CD64 ( A, B, C) · CD66 ( a, b, c, d, e, f) · CD68 · CD69 · CD70 · CD71 · CD72 · CD73 · CD74 · CD78 · CD79 ( a, b) · CD80 · CD81 · CD82 · CD83 · CD84 · CD85 ( a, d, e, h, j, k) · CD86 · CD87 · CD88 · CD89 · CD90 · CD91- CD92 · CD93 · CD94 · CD95 · CD96 · CD97 · CD98 · CD99 · CD100
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101-150 |
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151-200 |
CD151 · CD152 · CD153 · CD154 · CD155 · CD156 ( a, b, c) · CD157 · CD158 ( a, d, e, i, k) · CD159 ( a, c) · CD160 · CD161 · CD162 · CD163 · CD164 · CD166 · CD167 ( a, b) · CD168 · CD169 · CD170 · CD171 · CD172 ( a, b, g) · CD174 · CD177 · CD178 · CD179 ( a, b) · CD181 · CD182 · CD183 · CD184 · CD185 · CD186 · CD191 · CD192 · CD193 · CD194 · CD195 · CD196 · CD197 · CDw198 · CDw199 · CD200
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201-250 |
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251-300 |
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301-350 |
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