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Cited by 15Cholesterol and Lipid MetabolismCancer, Lipids, and MetabolismAntifungal resistance and susceptibility

The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.

Molecular cloning and biochemical characterization of Candida albicans acyl-CoA:sterol acyltransferase, a potential target of antifungal agents

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Kim, Ki-Young, Shin, Yu-Kyong, Park, Jong-Chul, Kim, Jung-Ho, Yang, Hongyuan, Han, Dong-Min, Paik, Young-Ki·2004·Biochemical and Biophysical Research Communications
DOI 10.1016/j.bbrc.2004.05.076
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Abstract

To determine whether Candida albicans acyl CoA:sterol acyltransferase (ASAT) can be a potential target enzyme for the protoberberine derivative (HWY-289), we have isolated a gene encoding Ca-ASAT and examined inhibitory effects of HWY-289 on the overexpressed Ca-ASAT. HWY-289 specifically inhibits Ca-ASAT in a non-competitive manner in vitro (IC(50) [9.2microM], K(i) [5.15microM]). The cloned CaARE2 gene (1830 nucleotides [nt]) encodes active Ca-ASAT protein that exhibits a calculated molecular mass of 71.3kDa. The amino acid sequence of CaAre2p is 33.4% and 35.1% identical to those of Saccharomyces cerevisiae ScAre1p and ScAre2p homologues, respectively. Recombinant and endogenous Ca-ASAT displayed identical patterns of inhibition upon exposure to HWY-289 and a preference for cholesterol and oleoyl-CoA as substrates. Northern blot analysis showed that CaARE2 was activated by HWY-289, but not by CI-976 (a human acyl-coenzyme A:cholesterol acyltransferase inhibitor), in a dose-dependent manner (up to 5mg/L), suggesting different selectivities of action between HWY-289 and CI-976 on Ca-ASAT activity.

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Crossref · 10.1016/j.bbrc.2004.05.076

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37 of 37 references verified0 citation errors · 0 not checkable

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  • All these steryl ester metabolism genes are uncharacterized in C. albicans except ARE2, which has been verified as a sterol acyltransferase that uses cholesterol and oleoyl-CoA as substrates and is induced by ketoconazole.

    “All these genes are uncharacterized in C. albicans except ARE2 , which has been veri fi ed as a sterol acyltransferase that uses cholesterol and oleoyl-CoA as substrates and is induced by ketoconazole.”

    From The synthesis, regulation, and functions of sterols in Candida albicans: Well-known but still lots to learn (2016) · cites this paper as [47]

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Metadata

Authors
Kim, K.-Y., Shin, Y.-K., Park, J.-C., Kim, J.-H., Yang, H., Han, D.-M., & Paik, Y.-K.
Affiliations
  • Yonsei University (KR)
  • Hanwha Group (South Korea) (KR)
  • National University of Singapore (SG)
  • Wonkwang University (KR)
Corresponding author
Paik, Young-Ki
ORCID
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
2004-07
Volume
319
Issue
3
Pages
911-919
ISSN
0006-291X (ISSN-L)
DOI
10.1016/j.bbrc.2004.05.076
OpenAlex
W2006045510
Cited by
15
References
37
Citations by year
2025: 1 · 2024: 1 · 2021: 1 · 2020: 1 · 2019: 1 · 2017: 2 · 2016: 3 · 2014: 1
FWCI
0.63
Type
journal article
Language
en
Open access
Licence
Locations
  • Biochemical and Biophysical Research Communications (publishedVersion)
  • PubMed (publishedVersion)
  • National University of Singapore (submittedVersion)
  • YUHSpace (Yonsei University Medical Library) (submittedVersion, cc-by-nc-nd)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
  • Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
Keywords
Candida albicans, antifungal drug targets, enzyme inhibition, non-competitive inhibition, cholesterol, oleoyl-CoA, sterol biosynthesis, gene cloning
MeSH terms
Acyl Coenzyme A, Amino Acid Sequence, Anilides, Antifungal Agents, Base Sequence, Berberine, Candida albicans, Sterol O-Acyltransferase, Cloning, Molecular, Enzyme Inhibitors, Fungal Proteins, Humans, Molecular Sequence Data, Recombinant Proteins, Gene Expression Regulation, Fungal, Sequence Alignment, Sequence Homology, Amino Acid

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