Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE
Volume 1587, Issue 1, Pages 60-64Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0925-4439(02)00066-2
Keywords
ABCA1; HDL cholesterol deficiency; mutation
Funding
- NHLBI NIH HHS [HL-61369] Funding Source: Medline
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The recent discovery of an ATP-binding cassette transporter, ABCA1, as an important regulator of high density lipoprotein (HDL) metabolism and reverse cholesterol transport has facilitated the identification of novel variants associated with HDL cholesterol deficiency states. Vie identified a subject with HDL cholesterol deficiency (4 mg/dl) who developed and died of complications related to cerebral amyloid angiopathy (CAA). The proband had a compound heterozygous mutation. One mutation was a G3295T substitution with conversion of asparagine to tyrosine (D1099Y) in ABCA1. The single-base substitution at codon 1099 resulted in the abolition of an RsaI cleavage site. The proband and affected individuals having another mutation were heterozygotes for T5966C kith phenylalanine converted to serine (F2009S). The presence of the T5966C mutation was detected by restriction digestion with Hinf1. These variants were not identified in over 400 chromosomes of healthy subjects, In the kindred, family members heterozygous for the ABCA1 variant exhibited low levels of HDL cholesterol. Direct sequencing of all coding regions and splice site junctions of other HDL candidate genes revealed no additional mutations, indicating that combined defective ABCA1 alleles may result in familial HDL deficiency. (C) 2002 Elsevier Science B.V. All rights reserved.
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