When scientists changed one amino acid in the creatine transporter (from alanine to proline at position 285), it didn't change how well beta-guanidinopropionic acid, cyclocreatine, or gamma-guanidinobutyric acid could block the transporter in frog cells.

Scientific Claim

The A285P mutant of the human CRT-1 creatine transporter in Xenopus oocytes is inhibited by beta-guanidinopropionic acid, cyclocreatine, and gamma-guanidinobutyric acid as effectively as the wild type, indicating that this mutation does not affect sensitivity to these inhibitors in this experimental system.

Source Excerpt

“The inhibitors beta-guanidinopropionic acid, cyclocreatine, and gamma-guanidinobutyric acid also inhibited the uptake activity of the Ala285 to Pro285 (A285P) mutant as effectively as that of the wild type.”

Evidence from Studies

Supporting Studies

Molecular characterization of the human CRT-1 creatine transporter expressed in Xenopus oocytes.

In Vitro

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Evidence Assessment

Supported

The study directly compared the inhibition of the wild-type and A285P mutant creatine transporter by specific inhibitors in Xenopus oocytes. The finding indicates that the mutation at position 285 does not affect sensitivity to these particular inhibitors in this experimental system.

Source Study

Molecular characterization of the human CRT-1 creatine transporter expressed in Xenopus oocytes.

Score: 2

DOI: 10.1006/abbi.1998.0959

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