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SULT1A1

From Wikipedia, the free encyclopedia
SULT1A1
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesSULT1A1, HAST1/HAST2, P-PST, PST, ST1A1, ST1A3, STP, STP1, TSPST1, sulfotransferase family 1A member 1, ts-PST, P-PST 1
External IDsOMIM: 171150; HomoloGene: 134950; GeneCards: SULT1A1; OMA:SULT1A1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

RefSeq (protein)

NP_001046
NP_803565
NP_803566
NP_803878
NP_803880

n/a

Location (UCSC)Chr 16: 28.6 – 28.62 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

Sulfotransferase 1A1 is an enzyme that in humans is encoded by the SULT1A1 gene.[3][4][5]

Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. This gene encodes one of two phenol sulfotransferases with thermostable enzyme activity. Multiple alternatively spliced variants that encode two isoforms have been identified for this gene.[5]

The SULT1A1 enzyme is expressed in outer roots sheath of hair follicles. Minoxidil, the only US FDA approved topical drug for re-growing hair in male and female pattern hair loss (androgenetic alopecia patients) is a pro-drug. Minoxidil is converted to its active form (minoxidil sulfate) by the hair sulfotransferase enzyme (SULT1A1).[6] A large variability in sulfotransferase enzyme expression in hair is observed among people. Low sulfotransferase activity was found to be predictive to lack of response to topical minoxidil for hair re-growth.[7] In a clinical study, a novel formula using a hypoxia mimetic pathway demonstrated to increase SULT1A1 activity in human subjects in-vivo.[8]

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000196502Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ Dooley TP, Obermoeller RD, Leiter EH, Chapman HD, Falany CN, Deng Z, Siciliano MJ (November 1993). "Mapping of the phenol sulfotransferase gene (STP) to human chromosome 16p12.1-p11.2 and to mouse chromosome 7". Genomics. 18 (2): 440–3. doi:10.1006/geno.1993.1494. PMID 8288252.
  4. ^ Dooley TP, Huang Z (November 1996). "Genomic organization and DNA sequences of two human phenol sulfotransferase genes (STP1 and STP2) on the short arm of chromosome 16". Biochemical and Biophysical Research Communications. 228 (1): 134–40. doi:10.1006/bbrc.1996.1628. PMID 8912648.
  5. ^ a b "SULT1A1 sulfotransferase family 1A member 1 [ Homo sapiens (human) ]".
  6. ^ McCoy J, Goren A, Naccarato T, Kovacevic M, Situm M, Skudar VL, Lotti T (2019). "Identification of the sulfotransferase iso-enzyme primarily responsible for the bio-activation of topical minoxidil". Journal of Biological Regulators and Homeostatic Agents. 33 (3): 817–819. PMID 31184104.
  7. ^ Goren A, Shapiro J, Roberts J, McCoy J, Desai N, Zarrab Z, et al. (2015). "Clinical utility and validity of minoxidil response testing in androgenetic alopecia". Dermatologic Therapy. 28 (1): 13–6. doi:10.1111/dth.12164. PMID 25112173. S2CID 205082682.
  8. ^ Ramos PM, McCoy J, Wambier C, Shapiro J, Vañó-Galvan S, Sinclair R, Goren A (May 2020). "Novel topical booster enhances follicular sulfotransferase activity in patients with androgenetic alopecia: a new strategy to improve minoxidil response". Journal of the European Academy of Dermatology and Venereology. 34 (12): e799–e800. doi:10.1111/jdv.16645. hdl:11343/278544. PMID 32432358. S2CID 218755089.

Further reading

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