Detection of a point mutation in sphingolipid activator protein-1 mRNA in patients with a variant form of metachromatic leukodystrophy
| Autor: | Xun-Ling Zhang, Mohammad A. Rafi, Gregory Degala, David A. Wenger |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Arylsulfatase A
Sphingolipid Activator Proteins Glycosylation genetic structures RNA Splicing Molecular Sequence Data Biophysics Biology Biochemistry Polymerase Chain Reaction Saposins Complementary DNA medicine Humans RNA Messenger Molecular Biology Gene Glycoproteins Base Sequence Activator (genetics) Point mutation Cell Biology Leukodystrophy Metachromatic medicine.disease Molecular biology Sphingolipid eye diseases Metachromatic leukodystrophy Mutation Oligonucleotide Probes |
| Zdroj: | Biochemical and biophysical research communications. 166(2) |
| ISSN: | 0006-291X |
| Popis: | The lysosomal degradation of sulfatide requires the specific enzyme, arylsulfatase A, as well as a heat stable protein called sphingolipid activator protein-1 (SAP-1). While most patients with metachromatic leukodystrophy have defects in arylsulfatase A, some patients have defects in SAP-1. SAP-1 is coded for by a gene on human chromosome 10 that also codes for three other proposed SAP. Examination of the cDNA from two siblings with SAP-1 deficiency revealed a point mutation of nucleotide #650 (counting from the initiation ATG) which is in the SAP-1 coding domain. This C to T transition changed the codon from threonine (ACC) to one coding for isoleucine (ATC). This eliminated the only glycosylation site in mature SAP-1 and could explain the findings made at the protein level. |
| Databáze: | OpenAIRE |
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