Amino acid sequence and the cellular location of the Na(+)-dependent D-glucose symporters (SGLT1) in the ovine enterocyte and the parotid acinar cell

• Published in: Biochemical journal 1995-11, Vol.312 ( Pt 1) (1), p.293-300
• Main Authors: Tarpey, P S, Wood, I S, Shirazi-Beechey, S P, Beechey, R B
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Cell Membrane - chemistry; Cell Polarity; Cloning, Molecular; Glucose - metabolism; Histocompatibility Antigens Class I - analysis; Immunoelectrophoresis; Immunohistochemistry; Intestinal Mucosa - chemistry; Membrane Glycoproteins; Membrane Proteins - analysis; Membrane Proteins - chemistry; Molecular Sequence Data; Monosaccharide Transport Proteins - analysis; Monosaccharide Transport Proteins - chemistry; Parotid Gland - chemistry; Protein Sorting Signals - metabolism; Sequence Homology, Amino Acid; Sheep; Sodium - metabolism; Sodium-Glucose Transporter 1; Sodium-Potassium-Exchanging ATPase - analysis
• ISSN: 0264-6021; 1470-8728
• DOI: 10.1042/bj3120293

The Na(+)-dependent D-glucose symporter has been shown to be located on the basolateral domain of the plasma membrane of ovine parotid acinar cells. This is in contrast to the apical location of this transporter in the ovine enterocyte. The amino acid sequences of these two proteins have been determined. They are identical. The results indicated that the signals responsible for the differential targeting of these two proteins to the apical and the basal domains of the plasma membrane are not contained within the primary amino acid sequence.