Two novel point mutations in the lecithin:cholesterol acyltransferase (LCAT) gene resulting in LCAT deficiency: LCAT (G873 deletion) and LCAT (Gly344–&gt;Ser)

Moriyama, Kengo; Sasaki, Jun; Takami, Noboru; Maeda, Eiichi; Matsunaga, Akira; Takada, Yoichi; Midorikawa, Koji; Yanase, Toshihiko; Yoshino, Gen

doi:10.1016/s0022-2275(20)39714-5

Cited by 23 publications

(2 citation statements)

References 46 publications

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“…G344S, T347M. These two mutations are associated with FLD in two separate probands (33,34). The G344S mutation was identified in a Japanese patient who had 10% of normal LCAT mass and no measurable activity (34) (Table 1).…”

Section: Structural Effects Of Point Mutations In the Lcat Gene: Point Mutations Associated With Fldmentioning

confidence: 99%

Effects of natural mutations in lecithin:cholesterol acyltransferase on the enzyme structure and activity

Peelman

Verschelde

Vanloo

et al. 1999

Journal of Lipid Research

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A molecular model was built for human lecithin:cholesterol acyltransferase (LCAT) based upon the structural homology between this enzyme and lipases (Peelman et al. 1998. Prot. Sci. 7: 585-597). We proposed that LCAT belongs to the ␣ / ␤ hydrolase fold family, and that the central domain of LCAT consists of a mixed seven-stranded ␤ -pleated sheet with four ␣ -helices and loops linking the ␤ -strands. The catalytic triad of LCAT was identified as Asp345 and His377, as well as Ser181. This model is used here for the interpretation of the structural defects linked to the point mutations identified in LCAT, which cause either familial LCAT deficiency (FLD) or fish-eye disease (FED). We show that these mutations occur in separate domains of the 3D structure of the enzyme. Most mutations causing familial LCAT deficiency are either clustered in the vicinity of the catalytic triad or affect conserved structural elements in LCAT. Most mutations causing fish-eye disease are localized on the outer hydrophilic surface of the amphipathic helical segments. These mutations affect only minimally the overall structure of the enzyme, but are likely to impair the interaction of the enzyme with its co-factor and/ or substrate.-

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Section: Structural Effects Of Point Mutations In the Lcat Gene: Point Mutations Associated With Fldmentioning

confidence: 99%

Effects of natural mutations in lecithin:cholesterol acyltransferase on the enzyme structure and activity

Peelman

Verschelde

Vanloo

et al. 1999

Journal of Lipid Research

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“…This article contains supplemental data ( 63 , 64 , 65 , 66 , 67 , 68 , 69 , 70 , 71 , 72 , 73 , 74 , 75 , 76 , 77 , 78 , 79 , 80 , 81 , 82 , 83 , 84 , 85 , 86 , 87 , 88 , 89 , 90 , 91 , 92 , 93 , 94 , 95 , 96 , 97 , 98 , 99 , 100 , 101 , 102 , 103 , 104 , 105 , 106 , 107 , 108 , 109 , 110 , 111 , 112 , 113 , 114 , 115 , 116 , 117 , 118 , 119 , 120 , 121 , 122 , 123 , 124 , 125 , 126 , 127 , 128 , 129 , 130 , 131 , 132 , 133 , …”

Section: Supplemental Dataunclassified

A systematic review of the natural history and biomarkers of primary lecithin:cholesterol acyltransferase deficiency

Vitali

Bajaj

Nguyen

et al. 2022

Journal of Lipid Research

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This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

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Störungen des Lipid- und Lipoproteinstoffwechsels

Julius¹,

Pietzsch²,

Hanefeld³

2000

Monogen Bedingte Erbkrankheiten 1

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Two novel point mutations in the lecithin:cholesterol acyltransferase (LCAT) gene resulting in LCAT deficiency: LCAT (G873 deletion) and LCAT (Gly344–>Ser)

Cited by 23 publications

References 46 publications

Effects of natural mutations in lecithin:cholesterol acyltransferase on the enzyme structure and activity

Effects of natural mutations in lecithin:cholesterol acyltransferase on the enzyme structure and activity

A systematic review of the natural history and biomarkers of primary lecithin:cholesterol acyltransferase deficiency

Störungen des Lipid- und Lipoproteinstoffwechsels

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