Creatine and the creatine transporter: a review

Snow, Rod and Murphy, Robyn M. 2001, Creatine and the creatine transporter: a review, Molecular and cellular biochemistry, vol. 224, no. 1-2, pp. 169-181, doi: 10.1023/A:1011908606819.

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Title Creatine and the creatine transporter: a review
Author(s) Snow, RodORCID iD for Snow, Rod
Murphy, Robyn M.
Journal name Molecular and cellular biochemistry
Volume number 224
Issue number 1-2
Start page 169
End page 181
Publisher Kluwer Academic Publishers
Place of publication Dordrecht, Netherlands
Publication date 2001-08
ISSN 1573-4919
Keyword(s) nutritional supplement
neuromuscular diseases
genetic regulation
Summary The cellular role of creatine (Cr) and Cr phosphate (CrP) has been studied extensively in neural, cardiac and skeletal muscle. Several studies have demonstrated that alterations in the cellular total Cr (Cr + CrP) concentration in these tissues can produce marked functional and/or structural change. The primary aim of this review was to critically evaluate the literature that has examined the regulation of cellular total Cr content. In particular, the review focuses on the regulation of the activity and gene expression of the Cr transporter (CreaT), which is primarily responsible for cellular Cr uptake. Two CreaT genes (CreaT1 and CreaT2) have been identified and their chromosomal location and DNA sequencing have been completed. From these data, putative structures of the CreaT proteins have been formulated. Transcription products of the CreaT2 gene are expressed exclusively in the testes, whereas CreaT1 transcripts are found in a variety of tissues. Recent research has measured the expression of the CreaT1 protein in several tissues including neural, cardiac and skeletal muscle. There is very little information available about the factors regulating CreaT gene expression. There is some evidence that suggests the intracellular Cr concentration may be involved in the regulatory process but there is much more to learn before this process is understood. The activity of the CreaT protein is controlled by many factors. These include substrate concentration, transmembrane Na+ gradients, cellular location, and various hormones. It is also likely that transporter activity is influenced by its phosphorylation state and by its interaction with other plasma membrane proteins. The extent of CreaT protein glycosylation may vary within cells, the functional significance of which remains unclear.
Language eng
DOI 10.1023/A:1011908606819
Field of Research 060110 Receptors and Membrane Biology
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2001, Kluwer Academic Publishers
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