BST1

From Wikipedia, the free encyclopedia
BST1
Protein BST1 PDB 1isf.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesBST1, CD157, bone marrow stromal cell antigen 1
External IDsOMIM: 600387 MGI: 105370 HomoloGene: 3198 GeneCards: BST1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004334

NM_009763

RefSeq (protein)

NP_004325

NP_033893

Location (UCSC)Chr 4: 15.7 – 15.74 MbChr 5: 43.82 – 43.84 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Bst1 (Bone marrow stromal cell antigen 1, ADP-ribosyl cyclase 2, CD157) is an enzyme that in humans is encoded by the BST1 gene.[5][6][7] CD157 is a paralog of CD38, both of which are located on chromosome 4 (4p15) in humans.[8]

Bst1 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.[7]

CD157 and CD38 are both members of the ADP-ribosyl cyclase family of enzymes that catalyze the formation of nicotinamide and adenosine diphosphate ribose (ADPR) or cyclic ADP-ribose (cADPR) from NAD+, although CD157 is a much weaker catalyst than CD38.[9][10][11] cADPR is required for regulation of Ca22+ in cells.[10] Only CD38 hydrolyzed cADPR to ADPR.[11] CD38 is widely expressed in tissues, whereas CD157 is primarily found in gut and lymphoid tissue.[11]

CD157 has an important role in controlling the migration of leukocytes, the adhesion of leukocytes to blood vessel walls, and the passage of leukocytes through blood vessel walls.[8]

CD157 contributes to macrophage killing of the Mycobacterium tuberculosis bacteria responsible for tuberculosis.[12]

CD157 is highly expressed in acute myeloid leukemia, and is being evaluated as a diagnostic sign, as a treatment target, and as a means of monitoring treatment progress.[13]

BST1 and BST2 genes are unregulated by the Nicotinamide (NAM) metabolism pathway.[14]

See also[]

  • Cluster of differentiation

References[]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000109743 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029082 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Ferrero E, Lo Buono N, Morone S, Parrotta R (2017). "Human canonical CD157/Bst1 is an alternatively spliced isoform masking a previously unidentified primate-specific exon included in a novel transcript". Scientific Reports. 7 (1): 159231. Bibcode:2017NatSR...715923F. doi:10.1038/s41598-017-16184-w. PMC 5698419. PMID 29162908.
  6. ^ Kaisho T, Ishikawa J, Oritani K, Inazawa J, Tomizawa H, Muraoka O, Ochi T, Hirano T (Jul 1994). "BST-1, a surface molecule of bone marrow stromal cell lines that facilitates pre-B-cell growth". Proc Natl Acad Sci U S A. 91 (12): 5325–9. Bibcode:1994PNAS...91.5325K. doi:10.1073/pnas.91.12.5325. PMC 43987. PMID 8202488.
  7. ^ a b "Entrez Gene: BST1 bone marrow stromal cell antigen 1".
  8. ^ a b Quarona V, Zaccarello G, Chillemi A (2013). "CD38 and CD157: a long journey from activation markers to multifunctional molecules". . 84 (4): 207–217. doi:10.1002/cyto.b.21092. PMID 23576305. S2CID 205732787.
  9. ^ Higashida H, Hashii M, Tanaka Y, Matsukawa S (2019). "CD38, CD157, and RAGE as Molecular Determinants for Social Behavior". Cells. 9 (1): 62. doi:10.3390/cells9010062. PMC 7016687. PMID 31881755.
  10. ^ a b Malavasi F, Deaglio S, Funaro A, Ferrero E, Horenstein AL, Ortolan E, Vaisitti T, Aydin S (2008). "Evolution and function of the ADP ribosyl cyclase/CD38 gene family in physiology and pathology". Physiological Reviews. 88 (3): 841–886. doi:10.1152/physrev.00035.2007. PMID 18626062.
  11. ^ a b c Rajman L, Chwalek K, Sinclair DA (2018). "Therapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence". Cell Metabolism. 27 (3): 529–547. doi:10.1016/j.cmet.2018.02.011. PMC 6342515. PMID 29514064.
  12. ^ Glaría E, Valled AF (2020). "Roles of CD38 in the Immune Response to Infection". Cells. 9 (1): 228. doi:10.3390/cells9010228. PMC 7017097. PMID 31963337.
  13. ^ Yakymiv Y, Augeri S, Fissolo G, Peola S (2019). "CD157: From Myeloid Cell Differentiation Marker to Therapeutic Target in Acute Myeloid Leukemi". Cells. 8 (12): 1580. doi:10.3390/cells8121580. PMC 6952987. PMID 31817547.
  14. ^ Jung J, Kim LJ, Wang X, Wu Q, Sanvoranart T, Hubert CG; et al. (2017). "Nicotinamide metabolism regulates glioblastoma stem cell maintenance". JCI Insight. 2 (10). doi:10.1172/jci.insight.90019. PMC 5436539. PMID 28515364.{{cite journal}}: CS1 maint: multiple names: authors list (link)

External links[]

  • Human BST1 genome location and BST1 gene details page in the UCSC Genome Browser.
  • Overview of all the structural information available in the PDB for UniProt: Q10588 (Human ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2) at the PDBe-KB.

Further reading[]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


Retrieved from ""