Work

Molecular cloning of the murine cMOAT ATPase

Year: 2000

Type: article

Abstract: cMOAT encodes an ATPase within the family of cMOAT/MRP ATPases that functions as an ATP dependent, multispecific anion transporter within the canalicular surface of hepatocytes that has pharmacologic significance. We describe here the cloning of a murine cMOAT cDNA isolated from mouse liver. The open reading frame of this cDNA incorporates 4627 nucleotides encoding 1309 amino acids with 77.5% and 86.7% identity with the human and rat encoded amino acids, respectively. Northern blotting showed that the expression of cMOAT mRNA occurs primarily in mouse liver in the form of two variants with approximately 5.6 and 7.8 kb of sequence each. cMOAT mRNA was also detected in mouse kidney at a low level but was not detected in other mouse organs or tumors except the Hep 1-6 murine hepatoma where expression was also in the form of the same two mRNA variants.

Source: Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression

DOI: 10.1016/s0167-4781(00)00132-9

Authors: Friederike Fritz, Jing Chen, Paula Hayes, F.M. Sirotnak

Institutions: Memorial Sloan Kettering Cancer Center, Cornell University

Language: English

Topic: Drug Transport and Resistance Mechanisms

Subfield: Oncology

Field: Medicine

Domain: Health Sciences

Open Access status: hybrid

Funders: National Institutes of Health, National Cancer Institute

Awards: MECHANISM-BASED THERAPEUTICS EXPLOITING TUMOR BIOLOGY, G546047228, G872256609, Cancer Center Support Grant