Cloning and expression of a mammalian Na+/amino acid cotransporter with sequence similarity to Na+/glucose cotransporters.

Kong, Cheng-Te; Yet, Shaw‐Fang; Lever, Julia E.

doi:10.1016/s0021-9258(18)53880-1

Cited by 123 publications

(5 citation statements)

References 34 publications

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“…These are System A (Felipe et al, 1992) and System XAG-(the present paper). A common sequence motif between the The sequences aligned are the guinea-pig glucose regulated protein, grp78 (Ting et al, 1987), mouse calreticulin (Smith and Koch, 1989), the LLCPK-1 cell-line putative System A transporter, SAAT1 (Kong et al, 1993), and the rabbit small-intestine excitatory high-affinity glutamate transporter, EAACl (Kanai and Hediger, 1992). suggest that a protein of 77 kDa, which may correspond to grp78, is also up-regulated by amino acid starvation in NBL-l cells.…”

Section: Discussionmentioning

confidence: 99%

Regulation of the glutamate transporter by amino acid deprivation and associated effects on the level of EAAC1 mRNA in the renal epithelial cell line NBL-I

Plakidou-Dymock

McGivan

1993

Biochemical Journal

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The glutamate transport system of the bovine renal epithelial cell line NBL-1 was studied. The Km for Na(+)-dependent glutamate transport was found to be 13.8 +/- 2.4 microM (Vmax. 365 +/- 19.2 pmol/3 min per mg) and for Na(+)-dependent aspartate transport 4.5 +/- 1.1 microM (Vmax. 108 +/- 6.3 pmol/3 min per mg). The Km values are in close agreement with those expected for high-affinity Na(+)-dependent glutamate transport by System XAG-. Upon deprivation of amino acids, the Vmax. for Na+/aspartate co-transport rose to 203 +/- 6.0 pmol/3 min per mg (Km 3.8 +/- 0.5 microns). A probe was constructed to the high-affinity excitatory amino acid carrier (EAAC1) [Kanai and Hediger (1992) Nature (London) 360, 467-471]. The probe hybridized to a 3.5 kb transcript. On deprivation of amino acids, the level of EAAC1 mRNA decreased sharply before the measurable increase in transport levels, but was subsequently restored to control levels. A motif, which we propose is linked to amino acid deprivation, was found in the EAAC1 primary sequence.

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Section: Discussionmentioning

confidence: 99%

Regulation of the glutamate transporter by amino acid deprivation and associated effects on the level of EAAC1 mRNA in the renal epithelial cell line NBL-I

Plakidou-Dymock

McGivan

1993

Biochemical Journal

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“…Full-length cDNA sequences of SGLT3 include those isolated from mouse kidney (SGLT3-b, this study), the pig LLC-PK 1 cell line [3], and human small intestine with the GenBank accession number AJ133127. Figure 6 shows the alignment of the full-length amino acid sequences of the above SGLT3s.…”

Section: Amino Acid Comparison Of Mouse Pig and Human Sglt3 Sequencesmentioning

confidence: 99%

“…In recent years, another member of SGLT family, SGLT3, has been identified. SGLT3 cDNA was first isolated from a pig kidney epithelial cell line, LLC-PK 1 , and has also been variously designated as SAAT1 or pSGLT2 [3,4]. In mouse, analysis of the chromosome 10 DNA sequence had predicted two reverse-oriented genes, Slc5a4a and Slc5a4b, encode SGLT3 homologous proteins [5].…”

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confidence: 99%

Mouse kidney expresses mRNA of four highly related sodium-glucose cotransporters: Regulation by cadmium

Tabatabai¹,

Blumenthal²,

Lewand³

et al. 2003

Kidney International

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“…SGLT2 is a low-affinity glucose transporter that is predominantly located on the apical membrane of renal proximal convoluted tubules, and is presumably responsible for the reabsorption of D-glucose from the glomerular filtrate (Wells et al, 1992;Kanai et al, 1994). SGLT3 was originally cloned as a renal amino acid cotransporter in swine (Kong et al, 1993) and was later reclassified as a member of the SGLT family (Mackenzie et al, 1994). However, its function may need to be reevaluated because human SGLT3 apparently does not transport glucose (Wright and Turk, 2004).…”

Section: Introductionmentioning

confidence: 99%

Cloning and Expression of Bovine Sodium/Glucose Cotransporters

Zhao

Zheng

Wall

et al. 2005

Journal of Dairy Science

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The Na+-dependent glucose cotransporters (SGLT) are a family of glucose transporters that mediate an active, sodium-linked transport process against an electrochemical gradient. The SGLT are known to play important roles in absorption of dietary D-glucose and D-galactose from the intestinal lumen and in the reabsorption of D-glucose from the glomerular filtrate in kidney. To study the role and regulation of SGLT in tissues of lactating cows, we cloned and sequenced the full-length cDNA of bovine SGLT1 and SGLT5. Open reading frame analysis predicted that bovine SGLT1 is composed of 664 amino acids with a molecular weight of approximately 73 kDa, and SGLT5 is composed of 597 amino acids with a molecular weight of approximately 65 kDa. The deduced amino acid sequence of bovine SGLT1 is 48% identical and 66% conserved relative to that of bSGLT5. The amino acid sequence of bovine SGLT1 is 97, 88, 87, 86, 85, and 84% identical to sheep, mouse, rat, horse, human, and rabbit SGLT1, respectively. In contrast, the amino acid sequence of bSGLT5 is relatively divergent among species, being 85, 64, and 48% identical to rabbit, human, and rat SGLT5, respectively. Bovine SGLT retain the characteristic structural features of SGLT1 proteins described in other species, including membrane-spanning helices and glucose transporter motifs. The major in vitro transcription and translation product of bovine SGLT1 cDNA migrated at an apparent molecular weight of 52 kDa. In the presence of canine microsomal membranes, the translation product increased to 53 kDa, suggesting glycosylation. The SGLT1 mRNA was most abundant in bovine intestine, at intermediate levels in bovine kidney, and at lower levels in bovine mammary gland, liver, and lung. No SGLT1 mRNA was detected in bovine spleen, skeletal muscle, or testes. Expression of SGLT5 mRNA was found predominantly in bovine kidney, only at very low levels in bovine testes, skeletal muscle, and spleen, and was essentially undetectable in bovine mammary gland, liver, lung, and small intestine. Abundance of SGLT1 mRNA in bovine mammary gland increased more than 4-fold during late pregnancy and early lactation. The sequence and expression data reported in this paper lay the groundwork for future studies aimed at unraveling the functional roles of SGLT in supporting milk production and maintaining glucose homeostasis during lactation.

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Cloning and expression of a mammalian Na+/amino acid cotransporter with sequence similarity to Na+/glucose cotransporters.

Cited by 123 publications

References 34 publications

Regulation of the glutamate transporter by amino acid deprivation and associated effects on the level of EAAC1 mRNA in the renal epithelial cell line NBL-I

Regulation of the glutamate transporter by amino acid deprivation and associated effects on the level of EAAC1 mRNA in the renal epithelial cell line NBL-I

Mouse kidney expresses mRNA of four highly related sodium-glucose cotransporters: Regulation by cadmium

Cloning and Expression of Bovine Sodium/Glucose Cotransporters

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