BST1

In this article we will explore the topic of BST1 from a comprehensive and detailed perspective. We will delve into its origins, evolution, impact and relevance today, with the aim of providing a deep and enriching understanding of BST1. Throughout our journey, we will address different aspects and approaches that will allow us to enrich our knowledge and reflect on the importance of BST1 in various contexts. From its influence on society to its implications in different areas, BST1 invites us to delve into its meaning and scope, and this article seeks to be a complete guide to delve into its fascinating universe.

BST1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesBST1, CD157, bone marrow stromal cell antigen 1
External IDsOMIM: 600387; MGI: 105370; HomoloGene: 3198; GeneCards: BST1; OMA:BST1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

683

12182

Ensembl

ENSG00000109743

ENSMUSG00000029082

UniProt

Q10588

Q64277

RefSeq (mRNA)

NM_004334

NM_009763

RefSeq (protein)

NP_004325

NP_033893

Location (UCSC)Chr 4: 15.7 – 15.74 MbChr 5: 43.98 – 44 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 Ca2+ 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

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". Cytometry Part B. 84 (4): 207–217. doi:10.1002/cyto.b.21092. hdl:2318/134656. 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, Prager BC, Wallace LC, Jin X, Mack SC, Rich JN (May 2017). "Nicotinamide metabolism regulates glioblastoma stem cell maintenance". JCI Insight. 2 (10). doi:10.1172/jci.insight.90019. PMC 5436539. PMID 28515364.

Further reading

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


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