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Complete cDNA encoding human phospholipid transfer protein from human endothelial cells.

1994; Elsevier BV; Volume: 269; Issue: 12 Linguagem: Inglês

10.1016/s0021-9258(17)37120-x

1083-351X

Joseph R. Day, J J Albers, Catherine Lofton–Day, Terri L. Gilbert, Andrew Ching, Francis James Grant, Patrick J. O’Hara, Santica M. Marcovina, J L Adolphson,

Metabolism and Genetic Disorders

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).