Complete cDNA encoding human phospholipid transfer protein from human endothelial cells

Phospholipid transfer protein, with an apparent molecular mass of 81 kDa, was purified from human plasma. The NH2-terminal amino acid sequence of a 51-kDa proteolytic fragment obtained from phospholipid transfer protein allowed degenerate primers to be designed for polymerase chain reaction and the...

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Bibliographic Details
Published in:The Journal of biological chemistry 1994-03, Vol.269 (12), p.9388-9391
Main Authors: DAY, J. R, ALBERS, J. J, LOFTON-DAY, C. E, GILBERT, T. L, CHING, A. F. T, GRANT, F. J, O'HARA, P. J, MARCOVINA, S. M, ADOLPHSON, J. L
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Base Sequence
Binding and carrier proteins
Biological and medical sciences
Carrier Proteins - genetics
cDNA
Cell Line
Cloning, Molecular
DNA, Complementary - genetics
Endothelium, Vascular - chemistry
Fundamental and applied biological sciences. Psychology
Gene Expression
genes
Humans
man
Membrane Proteins - genetics
Molecular Sequence Data
nucleotide sequence
phospholipid transfer protein
Phospholipid Transfer Proteins
plasma proteins
prediction
Proteins
RNA, Messenger - genetics
Sequence Alignment
Sequence Homology, Amino Acid
Tissue Distribution
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Summary:Phospholipid transfer protein, with an apparent molecular mass of 81 kDa, was purified from human plasma. The NH2-terminal amino acid sequence of a 51-kDa proteolytic fragment obtained from phospholipid transfer protein allowed degenerate primers to be designed for polymerase chain reaction and the eventual isolation of a full-length cDNA from a human endothelial cDNA library. The cDNA is 1,750 base pairs in length and contains an open reading frame of 1,518 nucleotides encoding a leader of 17 amino acids and a mature protein of 476 residues. Northern blot analysis shows a single mRNA transcript of approximately 1.8 kilobases with a wide tissue distribution. The gene was mapped to chromosome 20 using a human/rodent somatic cell hybrid mapping panel. Phospholipid transfer protein was found to be homologous to human cholesteryl ester transfer protein, human lipopolysaccharide-binding protein, and human neutrophil bactericidal permeability increasing protein (20, 24, and 26% identity, respectively).
ISSN:0021-9258
1083-351X
DOI:10.1016/s0021-9258(17)37120-x