BST1

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
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesBST1, CD157, bone marrow stromal cell antigen 1
External IDsOMIM: 600387 MGI: 105370 HomoloGene: 3198 GeneCards: BST1
Gene location (Human)
Chr.Chromosome 4 (human)[1]
Band4p15.32Start15,703,065 bp[1]
End15,738,313 bp[1]
RNA expression pattern
More reference expression data
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: 43.82 – 43.84 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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 cyclic ADP-ribose (cADPR) from NAD+, although CD157 is a much weaker catalyst than CD38.[9][10] cADPR is required for regulation of Ca22+ in cells.[10]

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 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.[11]


See also

References

  1. GRCh38: Ensembl release 89: ENSG00000109743 - Ensembl, May 2017
  2. 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. "Entrez Gene: BST1 bone marrow stromal cell antigen 1".
  8. 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. PMID 23576305.
  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. 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. 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.

Further reading

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


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