PMID: 8603082Mar 13, 1996Paper

Cloning and sequencing of the monocarboxylate transporter from mouse Ehrlich Lettré tumour cell confirms its identity as MCT1 and demonstrates that glycosylation is not required for MCT1 function

Biochimica Et Biophysica Acta
L CarpenterA P Halestrap

Abstract

Lactate transport is mediated in most tissues by H+-monocarboxylate-- cotransporters (MCTs). We have cloned and sequenced the lactate transporter from Ehrlich Lettré tumour cells by using the polymerase chain reaction (PCR) to amplify MCT1-related sequence from cDNA. The sequence is 93% and 87% identical to MCT1 from Chinese hamster and human respectively and so represents mouse MCT1. Most differences between MCT1 from Chinese hamster and mouse are conservative substitutions, located in hydrophilic parts of the molecule. Specific antipeptide antibodies confirm the presence of MCT1 protein in membranes from Ehrlich Lettré tumour cells. One difference between the mouse and Chinese hamster MCT1 is the absence of a predicted external consensus sequence for N-linked glycosylation in the mouse sequence. Using N-glycanase-F treatment and an in vitro translation system, we provide evidence that this glycosylation site is not actually utilised in Chinese hamster MCT1. These results are discussed in relation to current understanding of the roles of glycosylation of membrane proteins.

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Citations

Mar 13, 2012·Journal of Bioenergetics and Biomembranes·Céline PinheiroFátima Baltazar
Aug 4, 1997·The American Journal of Cardiology·A P HalestrapN T Price
Nov 2, 2005·Proceedings of the National Academy of Sciences of the United States of America·Ami A DeoraEnrique Rodriguez-Boulan
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Oct 15, 2014·International Journal of Molecular Sciences·Nelma Pértega-Gomes, Fátima Baltazar
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Nov 7, 2019·Physics in Medicine and Biology·Stefan BartzschMoeava Tehei
Jan 3, 2013·Magnetic Resonance in Medicine : Official Journal of the Society of Magnetic Resonance in Medicine·Mikko I KettunenKevin M Brindle
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