Reduced c27-steroid 26-hydroxylase activity in heterozygotes for cerebrotendinous xanthomatosis

Steinar Skrede; I. Björkhem; E. A. Kvittingen; C. East; Scott M Grundy; Sverre Skrede

doi:10.1080/00365518809085752

Reduced c₂₇-steroid 26-hydroxylase activity in heterozygotes for cerebrotendinous xanthomatosis

Steinar Skrede, I. Björkhem, E. A. Kvittingen, C. East, Scott M Grundy, Sverre Skrede

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

C₂7-steroid 26-hydroxylase activity in fibroblasts from two heterozygotes for CTX was determined, using an optimized enzyme assay. With 5βcholestane-3α 7α 12αtriol, 5βcholestane-3α 7αdiol, 7αhydroxy-4-cholesten-3-one or 7αhydroxycholesterol as substrates, the activities were about 50% of those of control cells. The K_m for the substrates was not increased in the CTX heterozygotes. These findings support that deficiency of the C₂₇-steroid 26-hydroxylase is the primary enzymatic defect in CTX.

Original language	English (US)
Pages (from-to)	425-429
Number of pages	5
Journal	Scandinavian Journal of Clinical and Laboratory Investigation
Volume	48
Issue number	5
DOIs	https://doi.org/10.1080/00365518809085752
State	Published - 1988

Keywords

Cerebrotendinous xanthomatosis
Cholesterol metabolism
Heterozygote detection

ASJC Scopus subject areas

Clinical Biochemistry

Access to Document

10.1080/00365518809085752

Cite this

@article{47cef2aebb594fe1895436fafe522e9f,

title = "Reduced c27-steroid 26-hydroxylase activity in heterozygotes for cerebrotendinous xanthomatosis",

abstract = "C27-steroid 26-hydroxylase activity in fibroblasts from two heterozygotes for CTX was determined, using an optimized enzyme assay. With 5βcholestane-3α 7α 12αtriol, 5βcholestane-3α 7αdiol, 7αhydroxy-4-cholesten-3-one or 7αhydroxycholesterol as substrates, the activities were about 50% of those of control cells. The Km for the substrates was not increased in the CTX heterozygotes. These findings support that deficiency of the C27-steroid 26-hydroxylase is the primary enzymatic defect in CTX.",

keywords = "Cerebrotendinous xanthomatosis, Cholesterol metabolism, Heterozygote detection",

author = "Steinar Skrede and I. Bj{\"o}rkhem and Kvittingen, {E. A.} and C. East and Grundy, {Scott M} and Sverre Skrede",

note = "Funding Information: We acknowledge the technical assistance of Anne Marie Lund. This was was supported by The Norwegian Research Council for Science and the Humanities (project 13.10.99-009) and the Swedish Medical Research Council (project 03X-3141). Study of patient H.E. was supported by the Veterans Administration, grant HL 29252 (National Institutes of I lealthlHDSI DHHS), National Institutes of Health grant M01-RR00633. and U. S. Public IIealth Service training grant AM 06307.",

year = "1988",

doi = "10.1080/00365518809085752",

language = "English (US)",

volume = "48",

pages = "425--429",

journal = "Scandinavian Journal of Clinical and Laboratory Investigation",

issn = "0036-5513",

publisher = "Informa Healthcare",

number = "5",

}

TY - JOUR

T1 - Reduced c27-steroid 26-hydroxylase activity in heterozygotes for cerebrotendinous xanthomatosis

AU - Skrede, Steinar

AU - Björkhem, I.

AU - Kvittingen, E. A.

AU - East, C.

AU - Grundy, Scott M

AU - Skrede, Sverre

N1 - Funding Information: We acknowledge the technical assistance of Anne Marie Lund. This was was supported by The Norwegian Research Council for Science and the Humanities (project 13.10.99-009) and the Swedish Medical Research Council (project 03X-3141). Study of patient H.E. was supported by the Veterans Administration, grant HL 29252 (National Institutes of I lealthlHDSI DHHS), National Institutes of Health grant M01-RR00633. and U. S. Public IIealth Service training grant AM 06307.

PY - 1988

Y1 - 1988

N2 - C27-steroid 26-hydroxylase activity in fibroblasts from two heterozygotes for CTX was determined, using an optimized enzyme assay. With 5βcholestane-3α 7α 12αtriol, 5βcholestane-3α 7αdiol, 7αhydroxy-4-cholesten-3-one or 7αhydroxycholesterol as substrates, the activities were about 50% of those of control cells. The Km for the substrates was not increased in the CTX heterozygotes. These findings support that deficiency of the C27-steroid 26-hydroxylase is the primary enzymatic defect in CTX.

AB - C27-steroid 26-hydroxylase activity in fibroblasts from two heterozygotes for CTX was determined, using an optimized enzyme assay. With 5βcholestane-3α 7α 12αtriol, 5βcholestane-3α 7αdiol, 7αhydroxy-4-cholesten-3-one or 7αhydroxycholesterol as substrates, the activities were about 50% of those of control cells. The Km for the substrates was not increased in the CTX heterozygotes. These findings support that deficiency of the C27-steroid 26-hydroxylase is the primary enzymatic defect in CTX.

KW - Cerebrotendinous xanthomatosis

KW - Cholesterol metabolism

KW - Heterozygote detection

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VL - 48

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EP - 429

JO - Scandinavian Journal of Clinical and Laboratory Investigation

JF - Scandinavian Journal of Clinical and Laboratory Investigation

IS - 5

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