1997
DOI: 10.1080/15216549700201111
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Use of transport mutants to examine the identity and expression of GLUT isoforms in rat cardiac myoblasts

Abstract: Two different spontaneous glucose transport (GLUT) mutants were used to examine the identity and properties of proteins involved in rat cardiac myoblast glucose transport processes. The parental clone, H9C2, possessed a high (HAHT) and a low (LAHT) affinity hexose transport process, and the GLUT 1, 3 and 4 isoforms. Mutant RCM was devoid of HAHT, the GLUT 3 transcript, and a 41 kDa protein recognizable by an anti‐mouse GLUT 3 Ab. Mutant EZ‐4 was impaired in the GLUT 3 and 4 isoforms, and in HAHT and LAHT. Thes… Show more

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Cited by 3 publications
(2 citation statements)
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“…This contrasts with an earlier western blot study showing GLUT3 in testis and brain but not in the human heart (5). In rat cardiomyoblasts GLUT1, 3 and 4 were noted to be present but GLUT3 contributed more to high affinity hexose transport than GLUT1 (6). Taken together, these data suggest a more predominant role for GLUT3 during cardiac development.…”
Section: Glucose Transporter Expression In the Heartcontrasting
confidence: 99%
“…This contrasts with an earlier western blot study showing GLUT3 in testis and brain but not in the human heart (5). In rat cardiomyoblasts GLUT1, 3 and 4 were noted to be present but GLUT3 contributed more to high affinity hexose transport than GLUT1 (6). Taken together, these data suggest a more predominant role for GLUT3 during cardiac development.…”
Section: Glucose Transporter Expression In the Heartcontrasting
confidence: 99%
“…GLUT3 has been found in both adult and fetal heart. Compared with GLUT1 and GLUT4, GLUT3 has a much higher affinity for hexose (72, 131). Although the sequence of GLUT8 shares 29% identical to GLUT1, whether GLUT8 regulates glucose transport in the heart is still unknown.…”
Section: Glucose Transporter In the Heartmentioning
confidence: 99%