Cited by 294Steroid Chemistry and BiochemistryCholesterol and Lipid MetabolismAdrenal Hormones and Disorders

The DOI matches its Crossref record; 124 of the 126 references it cites were found in a registry or an index; none of the 196 sources its claims cite is checked for support yet.

Novel activities of CYP11A1 and their potential physiological significance

Open access
Slominski, Andrzej T., Li, Wei, Kim, Tae-Kang, Semak, Igor, Wang, Jin, Zjawiony, Jordan K., Tuckey, Robert C.·2015·The Journal of Steroid Biochemistry and Molecular Biology

Abstract

CYP11A1, found only in vertebrates, catalyzes the first step of steroidogenesis where cholesterol is converted to pregnenolone. The purified enzyme, also converts desmosterol and plant sterols including campesterol and β-sitosterol, to pregnenolone. Studies, initially with purified enzyme, reveal that 7-dehydrocholesterol (7DHC), ergosterol, lumisterol 3, and vitamins D3 and D2 also serve as substrates for CYP11A1, with 7DHC being better and vitamins D3 and D2 being poorer substrates than cholesterol. Adrenal glands, placenta, and epidermal keratinocytes can also carry out these conversions and 7-dehydropregnenolone has been detected in the epidermis, adrenal glands, and serum, and 20-hydroxyvitamin D3 was detected in human serum and the epidermis. Thus, this metabolism does appear to occur in vivo, although its quantitative importance and physiological role remain to be established. CYP11A1 action on 7DHC in vivo is further supported by detection of Δ7steroids in Smith-Lemli-Opitz syndrome patients. The activity of CYP11A1 is affected by the structure of the substrate with sterols having steroidal or Δ7-steroidal structures undergoing side chain cleavage following hydroxylations at C22 and C20. In contrast, metabolism of vitamin D involves sequential hydroxylations that start at C20 but do not lead to cleavage. Molecular modeling using the crystal structure of CYP11A1 predicts that other intermediates of cholesterol synthesis could also serve as substrates for CYP11A1. Finally, CYP11A1-derived secosteroidal hydroxy-derivatives and Δ7steroids are biologically active when administered in vitro in a manner dependent on the structure of the compound and the lineage of the target cells, suggesting physiological roles for these metabolites. This article is part of a special issue entitled ‘SI: Steroid/Sterol signaling’.

Overview

Integrity signals

Registry

Crossref · 10.1016/j.jsbmb.2014.11.010

Cites

124 of 124 references verified0 citation errors · 0 not checkable

Statistics

Nothing to recompute.

Verification

Claims the paper makes

0 of 196 cited sources checked · 0 supported · 0 flagged

Show all 50 claims

  • It may state two separate claims as one. 51
  • Probably not a substantial claim. 2
52 of 52
  • The authors state this as an assumption.

    All CYP11A1 forms convert cholesterol to pregnenolone to initiate de novo steroidogenesis.

    “All are assumed to convert cholesterol to pregnenolone to initiate de novo steroidogenesis.”
  • The paper relies on this without support.

    Docking scores from molecular modeling predict whether a compound is a CYP11A1 substrate.

    “We observed excellent docking scores for several compounds listed in Table 1 that were comparable to cholesterol or hydroxycholesterol substrates.”
    “An excellent docking score for 8-dehydrocholesterol in conjunction with the presence of Δ8-steroids in body fluids of SLOS patients [60,61,63,64], predicts that it is also a substrate for CYP11A1 that undergoes cleavage of its side chain similar to 7-DHC and cholesterol.”
  • The paper relies on this without support.

    22R-hydroxycholesterol specifically inhibits CYP11A1, so almost complete inhibition indicates that CYP11A1 mediates the reaction.

    “The involvement of CYP11A1 in the conversion of D2 to 20(OH) D2, 20(OH)D2 to 17,20(OH)2D2, and the prodrug 1α(OH)D2 to 1,20 (OH)2D2 was demonstrated by its almost complete inhibition by 22R-hydroxycholesterol when placental and adrenal mitochondria were used to run the reaction [9].”
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Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

Each contradiction between two passages listed here was confirmed by an independent check.

  • D2 product has conflicting hydroxyl counts

    Minor

    The reaction sequence labels the 17,20,24-hydroxylated D2 product as having two hydroxyl groups, while the next paragraph labels the same product as having three.

  • D3 product keeps a dihydroxy label after another hydroxylation

    Minor

    The stated CYP27B1 reaction adds a hydroxyl group at position 1 to 20,23-dihydroxyvitamin D3, but labels the resulting three-position product as dihydroxy. Elsewhere the paper labels that product as trihydroxy.

  • D3 pathway gives inconsistent notation for its final product

    Minor

    The tissue-pathway summary labels its final 17,20,23-hydroxylated product with "(OH)32," whereas the earlier pathway labels the same product with "(OH)3."

3 of 3

Citations

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Show all 126 references

2 of the 126 references couldn’t be matched to a known paper.

Research works printed but not linked: 5

  1. Zhu, 2012, Vitamin D 25-hydroxylase – four decades of searching, are we there yet?, Arch. Biochem. Biophys., 523, 30, 10.1016/j.abb.2012.01.013 · DOI
  2. Zehnder, 2001, Extrarenal expression of 25-hydroxyvitamin d(3)-1 alpha-hydroxylase, J. Clin. Endocrinol. Metab., 86, 888
  3. Sakaki, 2005, Metabolism of vitamin D3 by cytochromes P450, Front. Biosci., 10, 119
  4. Tuckey, 2011, Production of 22-hydroxy metabolites of vitamin D3 by cytochrome p450scc (CYP11A1) and analysis of their biological activities on skin cells, Drug Metab. Dispos., 39, 1577, 10.1124/dmd.111.040071 · DOI · Paper page
  5. Tieu, 2012, Metabolism of cholesterol, vitamin D3 and 20-hydroxyvitamin D3 incorporated into phospholipid vesicles by human CYP27A1, J. Steroid Biochem. Mol. Biol., 129, 163, 10.1016/j.jsbmb.2011.11.012 · DOI · Paper page

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Metadata

Authors
Slominski, A. T., Li, W., Kim, T.-K., Semak, I., Wang, J., Zjawiony, J. K., & Tuckey, R. C.
Affiliations
  • University of Tennessee Health Science Center (US)
  • Belarusian State University (BY)
  • University of Mississippi (US)
  • The University of Western Australia (AU)
Corresponding author
  • Slominski, Andrzej T.
  • Tuckey, Robert C.
Venue
The Journal of Steroid Biochemistry and Molecular Biology
Publisher
Elsevier BV
Published
2015-07
Volume
151
Pages
25-37
ISSN
0960-0760 (ISSN-L)
OpenAlex
W1966916284
Cited by
292
References
126
Citations by year
2026: 12 · 2025: 11 · 2024: 29 · 2023: 28 · 2022: 28 · 2021: 37 · 2020: 36 · 2019: 24 · 2018: 19 · 2017: 20 · 2016: 28 · 2015: 19
FWCI
2.17
Type
journal article
Language
en
Open access
Locations
  • The Journal of Steroid Biochemistry and Molecular Biology (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • UWA Profiles and Research Repository (UWA) (submittedVersion)
  • BSU Digital Library (Belarusian State University) (submittedVersion, cc-by)
Funders
NIH (R01AR052190, R02AR052190, R21AR066505-01A1, 1R01AR056666-01A2)
Topics
  • Physical Sciences › Chemistry › Organic Chemistry › Steroid Chemistry and Biochemistry
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
  • Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adrenal Hormones and Disorders
Keywords
CYP11A1, pregnenolone synthesis, cholesterol, 7-dehydrocholesterol, vitamin D metabolism, secosteroids, desmosterol, campesterol, β-sitosterol, ergosterol, lumisterol, Smith-Lemli-Opitz syndrome, substrate specificity, enzyme crystal structure, molecular modeling, epidermal keratinocytes, adrenal gland, placenta, steroid hormone signaling
MeSH terms
Animals, Cholecalciferol, Cholesterol Side-Chain Cleavage Enzyme, Dehydrocholesterols, Ergocalciferols, Humans, Sterols

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