- Volume 15 Issue 4
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Cloning of cDNA Encoding PAS-4 Glycoprotein, an Integral Glycoprotein of Bovine Mammary Epithelial Cell Membrane
- Hwangbo, Sik (Faculty of Life Science and Technology, Sungkyunkwan University) ;
- Lee, Soo-Won (Faculty of Life Science and Technology, Sungkyunkwan University) ;
- Kanno, Chouemon (Department of applied Biochemistry, Faculty of Agriculture, Utsunomiya University)
- Received : 2001.07.05
- Accepted : 2001.10.10
- Published : 2002.04.01
Bovine PAS-4 is an integral membrane glycoprotein expressed in mammary epithelial cells. Complementary DNA (cDNA) cloning of PAS-4 was performed by reverse-transcriptase polymerase chain reaction (RT-PCR) with oligonucleotide probes based on it's amino terminal and internal tryptic-peptides. The cloned PAS-4 cDNA was 1,852 nucleotides (nt) long and its open reading frame (ORF) was encoded 1,413 base long. The deduced amino acid sequence indicated that PAS-4 consisted of 471 amino acid residues with molecular weight of 52,796, bearing 8 potential N-glycosylation sites and 9 cysteine residues. Partial bovine CD36 cDNA from liver also was sequenced and the homology of both nucleotide sequence was 94%. Most of the identical amino acid residues were in the luminal/extracellular domains. Contrary to PAS-4, bovine liver CD36 displays 6 potential N-glycosylation sites, which were located, except for those at positions 101 and 171, at same positions as PAS-4 cDNA. Cysteine residues of PAS-4 and CD36 were same at position and in numbers. Northern blot analysis showed that PAS-4 was widely expressed, although its mRNA steady-state levels vary considerably among the analyzed cell types. PAS-4 possessed hydrophobic amino acid segments near the amino- and carboxyl-termini. Two short cytoplasmic tails of the amino- and carboxyl-terminal ends constituted of a 5-7 and 8-11 amino acid residues, respectively.
Supported by : Korea Research Foundation
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