Transporter ATP binding

The role of other ABC-efHux transporters (ATP-binding cassette transporters) such as MRPs and BCRP was also intensively investigated over the past decade. However, most studies investigating the importance of ABC transporters for drug disposition were performed with different cell lines and animal models. In comparison to P-glycoprotein, only limited human data are available about the role of ABC transporters on drug disposition. In this chapter mainly human data will be discussed. For more detailed description and in vitro data about MRPs see Section 15.3. 

Xu J, Liu Y, Yang Y, Bates S, Zhang JT. Characterization of oligomeric human half ABC transporter ATP-binding cassette G2. J Biol Chem 2004 279 19781-19789. 

Loscher, W. and Potschka, H. (2005) Blood-brain barrier active efflux transporters ATP-binding cassette gene family. NeuroRx, 2, 86-98. 

Ruble T, Trottmann M, Lorenz RL (2004) Stimulation of CD36 and the key effector of reverse cholesterol transport ATP-binding cassette Al in monocytoid cells by niacin. Biochem Pharmacol 67 411 19 Sakurada T, Orimo H, Okabe H, et al. (1976) Purification and properties of cholesterol ester hydrolase from... 

A Oligopeptide permease B Oligopeptide transport ATP binding protein or Oligopeptide permease C Hypothetical protien D Hypothetical protein E Hypothetical protein F Phosphomannomutase G ABC transporter. 

Jones, P.M. George, A.M (2007). Nucleotide-dependent allostery within the ABC transporter ATP-binding cassette a compnitational study of the MJ0796 dimer. Biol Chem, Vol.282, No.31, pp. 22793-803... 

FIGURE 10.18 A model for the structure of the a-factor transport protein in the yeast plasma membrane. Gene duplication has yielded a protein with two identical halves, each half containing six transmembrane helical segments and an ATP-binding site. Like the yeast a-factor transporter, the multidrug transporter is postulated to have 12 transmembrane helices and 2 ATP-binding sites. 

Currently, five different molecular classes of mdr efflux pumps are known [5], While pumps of the the ATP-binding cassette (ABC) transporter superfamily are driven by ATP hydrolysis, the other four superfamilies called resistance-nodulation-division (RND), major facilitator superfamily (MFS), multidrug and toxic compound extrusion (MATE), and small multidrag resistance transporter (SMR) are driven by the proton-motive force across the cytoplasmic membrane. Usually a single pump protein is located within the cytoplasmic membrane. However, the RND-type pumps which are restricted to Gram-negative bacteria consist of two additional components, a periplasmic membrane fusion protein (MFP) which connects the efflux pump to an outer... 

SURs are members of the ATP-binding cassette (ABC) family of proteins ( ABC transporters) with a typical ABC core consisting of two bundles of six... 

ATP-binding cassette (ABC) transporters are efflux pumps that derive the energy needed for drug extrusion from the hydrolysis of ATP. Bacterial ABC antibiotic efflux transporter encoded on plasmids is a significant... 

Jessup W, Gelissen IC, Gaus K, Kritharides L (2006) Roles of ATP binding cassette transporters Al and Gl, scavenger receptor BI and membrane lipid domains in cholesterol export from macrophages. Curr Opin Lipidol 17(3) 247-57... 

Figure 25-5. Metabolism of high-density lipoprotein (HDL) in reverse cholesteroi transport. (LCAT, lecithinxholesterol acyltransferase C, cholesterol CE, cholesteryl ester PL, phospholipid A-l, apolipoprotein A-l SR-Bl, scavenger receptor B1 ABC-1, ATP binding cassette transporter 1.) Prep-HDL, HDLj, HDL3—see Table 25-1. Surplus surface constituents from the action of lipoprotein lipase on chylomicrons and VLDL are another source of preP-HDL. Hepatic lipase activity is increased by androgens and decreased by estrogens, which may account for higher concentrations of plasma HDLj in women.

Chearwae, W. et al.. Modulation of the function of the multidrug resistance-linked ATP-binding transporter ABCG2 by the cancer chemopreventive agent curcumin. Mol. Cancer Then, 5, 1995, 2006. 

Although the sequence identity averaged over the whole length of the molecule is generally low among different P-type ion transport ATPases, the conserved sequences around the phosphate acceptor aspartyl group and in the ATP binding domain are well preserved [30,32,46]. Structure predictions based on the hydropathy plots... 

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