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EnglishLong chain fatty acids are translocated as carnitine esters across the mitochondrial inner membrane by carnitine acylcarnitine translocase (CACT). We report functional studies on the mutant CACT proteins from a severe and a mild patient with CACT deficiency. CACT activities in fibroblasts of both patients were markedly deficient with some residual activity (<1%) in the milder patient. Palmitate oxidation activity in cells from the severe patient was less than 5% but in the milder patient approximately 27% residual activity was found. Sequencing of the CACT cDNAs revealed a c.241G>A (G81R) in the severe and a c.955insC mutation (C-terminal extension of 21 amino acids (CACT(+21aa)) in the milder patient. The effect of both mutations on the protein was studied in a sensitive expression system based on the ability of human CACT to functionally complement a CACT-deletion strain of yeast. Expression in this strain revealed significant residual activity for CACT(+21aa), while the CACT(G81R) was inactive.
Functional analysis of mutant human carnitine acylcarnitine translocases in yeast / IJLST L.; VAN ROERMUND C.W.; IACOBAZZI V; OOSTEIM W.; RUITER J.P.; WILLIAMS J.C.; PALMIERI F.; WANDERS R.J.. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - 280(2001), pp. 700-706.
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| Titolo: | Functional analysis of mutant human carnitine acylcarnitine translocases in yeast | |
| Autori: | ||
| Data di pubblicazione: | 2001 | |
| Rivista: | ||
| Citazione: | Functional analysis of mutant human carnitine acylcarnitine translocases in yeast / IJLST L.; VAN ROERMUND C.W.; IACOBAZZI V; OOSTEIM W.; RUITER J.P.; WILLIAMS J.C.; PALMIERI F.; WANDERS R.J.. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - 280(2001), pp. 700-706. | |
| Abstract: | Long chain fatty acids are translocated as carnitine esters across the mitochondrial inner membrane by carnitine acylcarnitine translocase (CACT). We report functional studies on the mutant CACT proteins from a severe and a mild patient with CACT deficiency. CACT activities in fibroblasts of both patients were markedly deficient with some residual activity (<1%) in the milder patient. Palmitate oxidation activity in cells from the severe patient was less than 5% but in the milder patient approximately 27% residual activity was found. Sequencing of the CACT cDNAs revealed a c.241G>A (G81R) in the severe and a c.955insC mutation (C-terminal extension of 21 amino acids (CACT(+21aa)) in the milder patient. The effect of both mutations on the protein was studied in a sensitive expression system based on the ability of human CACT to functionally complement a CACT-deletion strain of yeast. Expression in this strain revealed significant residual activity for CACT(+21aa), while the CACT(G81R) was inactive. | |
| Handle: | http://hdl.handle.net/11586/3738 | |
| Appare nelle tipologie: | 1.1 Articolo in rivista |
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