scholarly journals Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors

1999 ◽  
Vol 344 (1) ◽  
pp. 135-143 ◽  
Author(s):  
Kiran T. MALHOTRA ◽  
Khushbeer MALHOTRA ◽  
Bertram H. LUBIN ◽  
Frans A. KUYPERS
Keyword(s):  
Plasma Membranes ◽  
Fetal Liver ◽  
Erythrocyte Membranes ◽  
Long Chain Fatty Acids ◽  
Mature Erythrocyte ◽  
Haemopoietic Stem Cells ◽  
Chain Acyl ◽  
Kidney Liver ◽  
Long Chain

Full-length cDNA species encoding two forms of acyl-CoA synthetase from a K-562 human erythroleukaemic cell line were cloned, sequenced and expressed. The first form, named long-chain acyl-CoA synthetase 5 (LACS5), was found to be a novel, unreported, human acyl-CoA synthetase with high similarity to rat brain ACS2 (91% identical). The second form (66% identical with LACS5) was 97% identical with human liver LACS1. The LACS5 gene encodes a highly expressed 2.9 kb mRNA transcript in human haemopoietic stem cells from cord blood, bone marrow, reticulocytes and fetal blood cells derived from fetal liver. An additional 6.3 kb transcript is also found in these erythrocyte precursors; 2.9 and 9.6 kb transcripts of LACS5 are found in human brain, but transcripts are virtually absent from human heart, kidney, liver, lung, pancreas, spleen and skeletal muscle. The 78 kDa expressed LACS5 protein used the long-chain fatty acids palmitic acid, oleic acid and arachidonic acid as substrates. Antibodies directed against LACS5 cross-reacted with erythrocyte membranes. We conclude that early erythrocyte precursors express at least two different forms of acyl-CoA synthetase and that LACS5 is present in mature erythrocyte plasma membranes.

Increased very long-chain fatty acids in erythrocyte membranes of patients with aceruloplasminemia

Neurology ◽  
1998 ◽  
Vol 50 (1) ◽  
pp. 130-136 ◽  
Author(s):  
H. Miyajima ◽  
J. Adachi ◽  
Y. Tatsuno ◽  
Y. Takahashi ◽  
M. Fujimoto ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Erythrocyte Membranes ◽  
Long Chain Fatty Acids ◽  
Long Chain ◽  
Chain Fatty Acids

scholarly journals ABC Transporter Subfamily D: Distinct Differences in Behavior between ABCD1–3 and ABCD4 in Subcellular Localization, Function, and Human Disease

2016 ◽  
Vol 2016 ◽  
pp. 1-11 ◽  
Author(s):  
Kosuke Kawaguchi ◽  
Masashi Morita
Keyword(s):  
Abc Transporters ◽  
Critical Role ◽  
Vitamin B ◽  
Long Chain Fatty Acids ◽  
Substrate Specificities ◽  
Related Disease ◽  
Chain Acyl ◽  
Membrane Bound ◽  
Branched Chain ◽  
Long Chain

ATP-binding cassette (ABC) transporters are one of the largest families of membrane-bound proteins and transport a wide variety of substrates across both extra- and intracellular membranes. They play a critical role in maintaining cellular homeostasis. To date, four ABC transporters belonging to subfamily D have been identified. ABCD1–3 and ABCD4 are localized to peroxisomes and lysosomes, respectively. ABCD1 and ABCD2 are involved in the transport of long and very long chain fatty acids (VLCFA) or their CoA-derivatives into peroxisomes with different substrate specificities, while ABCD3 is involved in the transport of branched chain acyl-CoA into peroxisomes. On the other hand, ABCD4 is deduced to take part in the transport of vitamin B12from lysosomes into the cytosol. It is well known that the dysfunction of ABCD1 results in X-linked adrenoleukodystrophy, a severe neurodegenerative disease. Recently, it is reported that ABCD3 and ABCD4 are responsible for hepatosplenomegaly and vitamin B12deficiency, respectively. In this review, the targeting mechanism and physiological functions of the ABCD transporters are summarized along with the related disease.

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