BST1

Last updated
BST1
Protein BST1 PDB 1isf.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases BST1 , CD157, bone marrow stromal cell antigen 1
External IDs OMIM: 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 Mb Chr 5: 43.98 – 44 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/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]

Contents

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

Related Research Articles

<span class="mw-page-title-main">Nicotinamide adenine dinucleotide</span> Chemical compound which is reduced and oxidized

Nicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine nucleobase and the other, nicotinamide. NAD exists in two forms: an oxidized and reduced form, abbreviated as NAD+ and NADH (H for hydrogen), respectively.

<span class="mw-page-title-main">CD34</span> Cluster of differentiation protocol that identifies cell surface antigens.

CD34 is a transmembrane phosphoglycoprotein protein encoded by the CD34 gene in humans, mice, rats and other species.

<span class="mw-page-title-main">CD31</span> Mammalian protein found in Homo sapiens

Platelet endothelial cell adhesion molecule (PECAM-1) also known as cluster of differentiation 31 (CD31) is a protein that in humans is encoded by the PECAM1 gene found on chromosome17q23.3. PECAM-1 plays a key role in removing aged neutrophils from the body.

<span class="mw-page-title-main">CD38</span> Protein-coding gene in the species Homo sapiens

CD38 (cluster of differentiation 38), also known as cyclic ADP ribose hydrolase is a glycoprotein found on the surface of many immune cells (white blood cells), including CD4+, CD8+, B lymphocytes and natural killer cells. CD38 also functions in cell adhesion, signal transduction and calcium signaling.

<span class="mw-page-title-main">Sirtuin</span> Enzyme

Sirtuins are a family of signaling proteins involved in metabolic regulation. They are ancient in animal evolution and appear to possess a highly conserved structure throughout all kingdoms of life. Chemically, sirtuins are a class of proteins that possess either mono-ADP-ribosyltransferase or deacylase activity, including deacetylase, desuccinylase, demalonylase, demyristoylase and depalmitoylase activity. The name Sir2 comes from the yeast gene 'silent mating-type information regulation 2', the gene responsible for cellular regulation in yeast.

<span class="mw-page-title-main">Cyclic ADP-ribose</span> Chemical compound

Cyclic ADP-ribose, frequently abbreviated as cADPR, is a cyclic adenine nucleotide (like cAMP) with two phosphate groups present on 5' OH of the adenosine (like ADP), further connected to another ribose at the 5' position, which, in turn, closes the cycle by glycosidic bonding to the nitrogen 1 (N1) of the same adenine base (whose position N9 has the glycosidic bond to the other ribose). The N1-glycosidic bond to adenine is what distinguishes cADPR from ADP-ribose (ADPR), the non-cyclic analog. cADPR is produced from nicotinamide adenine dinucleotide (NAD+) by ADP-ribosyl cyclases (EC 3.2.2.5) as part of a second messenger system.

<span class="mw-page-title-main">Nicotinic acid adenine dinucleotide phosphate</span> Chemical compound

Nicotinic acid adenine dinucleotide phosphate (NAADP) is a Ca2+-mobilizing second messenger synthesised in response to extracellular stimuli. Like its mechanistic cousins, IP3 and cyclic adenosine diphosphoribose (Cyclic ADP-ribose), NAADP binds to and opens Ca2+ channels on intracellular organelles, thereby increasing the intracellular Ca2+ concentration which, in turn, modulates sundry cellular processes (see Calcium signalling). Structurally, it is a dinucleotide that only differs from the house-keeping enzyme cofactor, NADP by a hydroxyl group (replacing the nicotinamide amino group) and yet this minor modification converts it into the most potent Ca2+-mobilizing second messenger yet described. NAADP acts across phyla from plants to humans.

<span class="mw-page-title-main">Adenosine diphosphate ribose</span> Chemical compound

Adenosine diphosphate ribose (ADPR) is an ester molecule formed into chains by the enzyme poly ADP ribose polymerase. ADPR is created from cyclic ADP-ribose (cADPR) by the CD38 enzyme using nicotinamide adenine dinucleotide (NAD+) as a cofactor.

<span class="mw-page-title-main">ADP-ribosylation</span> Addition of one or more ADP-ribose moieties to a protein.

ADP-ribosylation is the addition of one or more ADP-ribose moieties to a protein. It is a reversible post-translational modification that is involved in many cellular processes, including cell signaling, DNA repair, gene regulation and apoptosis. Improper ADP-ribosylation has been implicated in some forms of cancer. It is also the basis for the toxicity of bacterial compounds such as cholera toxin, diphtheria toxin, and others.

<span class="mw-page-title-main">PARP1</span> Mammalian protein found in Homo sapiens

Poly [ADP-ribose] polymerase 1 (PARP-1) also known as NAD+ ADP-ribosyltransferase 1 or poly[ADP-ribose] synthase 1 is an enzyme that in humans is encoded by the PARP1 gene. It is the most abundant of the PARP family of enzymes, accounting for 90% of the NAD+ used by the family. PARP1 is mostly present in cell nucleus, but cytosolic fraction of this protein was also reported.

NAD<sup>+</sup> glycohydrolase Enzyme

In enzymology, a NAD+ glycohydrolase (EC 3.2.2.5) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">ADP-ribosyl cyclase</span>

In enzymology, a ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase (EC 3.2.2.6) is a bifunctional enzyme that catalyzes the chemical reaction

In enzymology, a NAD+-diphthamide ADP-ribosyltransferase (EC 2.4.2.36) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">CEACAM6</span> Mammalian protein found in Homo sapiens

Carcinoembryonic antigen-related cell adhesion molecule 6 (CEACAM6) also known as CD66c, is a member of the carcinoembryonic antigen (CEA) gene family..

<span class="mw-page-title-main">NMNAT1</span> Protein-coding gene in the species Homo sapiens

Nicotinamide mononucleotide adenylyltransferase 1 (NMNAT1) is an enzyme that in humans is encoded by the nmnat1 gene. It is a member of the nicotinamide-nucleotide adenylyltransferases (NMNATs) which catalyze nicotinamide adenine dinucleotide (NAD) synthesis.

<span class="mw-page-title-main">PARP4</span> Enzyme

Poly [ADP-ribose] polymerase 4 is an enzyme that in humans is encoded by the PARP4 gene.

<span class="mw-page-title-main">CEACAM8</span> Mammalian protein found in Homo sapiens

Carcinoembryonic antigen-related cell adhesion molecule 8 (CEACAM8) also known as CD66b, is a member of the carcinoembryonic antigen (CEA) gene family. Its main function is cell adhesion, cell migration, and pathogen binding.

<span class="mw-page-title-main">PARP2</span> Protein-coding gene in the species Homo sapiens

Poly [ADP-ribose] polymerase 2 is an enzyme that in humans is encoded by the PARP2 gene. It is one of the PARP family of enzymes.

<span class="mw-page-title-main">Tetherin</span> Mammalian protein found in Homo sapiens

Tetherin, also known as bone marrow stromal antigen 2, is a lipid raft associated protein that in humans is encoded by the BST2 gene. In addition, tetherin has been designated as CD317. This protein is constitutively expressed in mature B cells, plasma cells and plasmacytoid dendritic cells, and in many other cells, it is only expressed as a response to stimuli from IFN pathway.

Since haematopoietic stem cells cannot be isolated as a pure population, it is not possible to identify them under a microscope. Therefore, there are many techniques to isolate haematopoietic stem cells (HSCs). HSCs can be identified or isolated by the use of flow cytometry where the combination of several different cell surface markers is used to separate the rare HSCs from the surrounding blood cells. HSCs lack expression of mature blood cell markers and are thus, called Lin-. Lack of expression of lineage markers is used in combination with detection of several positive cell-surface markers to isolate HSCs. In addition, HSCs are characterized by their small size and low staining with vital dyes such as rhodamine 123 or Hoechst 33342.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000109743 – Ensembl, May 2017
  2. 1 2 3 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. 1 2 "Entrez Gene: BST1 bone marrow stromal cell antigen 1".
  8. 1 2 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. 1 2 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. 1 2 3 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

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