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      Faropenem Medoxomil

      Author(s): 1 , 2 , 3
      Publication date Created:
      Publication date (Electronic):
      Journal: Annals of Pharmacotherapy
      Publisher: SAGE Publications

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          Abstract

          <p class="first" id="d1811022e65">To review the literature concerning the in vitro activity, pharmacokinetic properties, in vivo efficacy, and adverse events associated with a new penem antibiotic, faropenem medoxomil. </p>

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          Vancomycin-resistant enterococci.

          Y Çetinkaya, P Falk, C. G. Mayhall (2000)
          After they were first identified in the mid-1980s, vancomycin-resistant enterococci (VRE) spread rapidly and became a major problem in many institutions both in Europe and the United States. Since VRE have intrinsic resistance to most of the commonly used antibiotics and the ability to acquire resistance to most of the current available antibiotics, either by mutation or by receipt of foreign genetic material, they have a selective advantage over other microorganisms in the intestinal flora and pose a major therapeutic challenge. The possibility of transfer of vancomycin resistance genes to other gram-positive organisms raises significant concerns about the emergence of vancomycin-resistant Staphylococcus aureus. We review VRE, including their history, mechanisms of resistance, epidemiology, control measures, and treatment.
          Article 0 comments Cited 193 times – based on 0 reviews     Review now
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            Pseudomonas aeruginosa reveals high intrinsic resistance to penem antibiotics: penem resistance mechanisms and their interplay.

            K. Okamoto, N Gotoh, T Nishino (2001)
            Pseudomonas aeruginosa exhibits high intrinsic resistance to penem antibiotics such as faropenem, ritipenem, AMA3176, sulopenem, Sch29482, and Sch34343. To investigate the mechanisms contributing to penem resistance, we used the laboratory strain PAO1 to construct a series of isogenic mutants with an impaired multidrug efflux system MexAB-OprM and/or impaired chromosomal AmpC beta-lactamase. The outer membrane barrier of PAO1 was partially eliminated by inducing the expression of the plasmid-encoded Escherichia coli major porin OmpF. Susceptibility tests using the mutants and the OmpF expression plasmid showed that MexAB-OprM and the outer membrane barrier, but not AmpC beta-lactamase, are the main mechanisms involved in the high intrinsic penem resistance of PAO1. However, reducing the high intrinsic penem resistance of PAO1 to the same level as that of penem-susceptible gram-negative bacteria such as E. coli required the loss of either both MexAB-OprM and AmpC beta-lactamase or both MexAB-OprM and the outer membrane barrier. Competition experiments for penicillin-binding proteins (PBPs) revealed that the affinity of PBP 1b and PBP 2 for faropenem were about 1.8- and 1.5-fold lower, than the respective affinity for imipenem. Loss of the outer membrane barrier, MexAB, and AmpC beta-lactamase increased the susceptibility of PAO1 to almost all penems tested compared to the susceptibility of the AmpC-deficient PAO1 mutants to imipenem. Thus, it is suggested that the high intrinsic penem resistance of P. aeruginosa is generated from the interplay among the outer membrane barrier, the active efflux system, and AmpC beta-lactamase but not from the lower affinity of PBPs for penems.
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              p-aminohippuric acid transport at renal apical membrane mediated by human inorganic phosphate transporter NPT1.

              I Tamai, H Uchino, E. Takeda … (2000)
              Organic anions are secreted into urine via organic anion transporters across the renal basolateral and apical membranes. However, no apical membrane transporter for organic anions such as p-aminohippuric acid (PAH) has yet been identified. In the present study, we showed that human NPT1, which is present in renal apical membrane, mediates the transport of PAH. The K(m) value for PAH uptake was 2.66 mM and the uptake was chloride ion sensitive. These results are compatible with those reported for the classical organic anion transport system at the renal apical membrane. PAH transport was inhibited by various anionic compounds. Human NPT1 also accepted uric acid, benzylpenicillin, faropenem, and estradiol-17beta-glucuronide as substrates. Considering its chloride ion sensitivity, Npt1 is expected to function for secretion of PAH from renal proximal tubular cells. This is the first molecular demonstration of an organic anion transport function for PAH at the renal apical membrane. Copyright 2000 Academic Press.
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                Author and article information

                Journal
                Title: Annals of Pharmacotherapy
                Abbreviated Title: Ann Pharmacother
                Publisher: SAGE Publications
                ISSN (Print): 1060-0280
                ISSN (Electronic): 1542-6270
                Publication date Created: December 04 2016
                Publication date Created: January 2008
                Publication date (Electronic): December 04 2016
                Publication date (Print): January 2008
                Volume: 42
                Issue: 1
                Pages: 80-90
                Affiliations
                [1 ]Pharmacy Practice, Midwestern University Chicago College of Pharmacy, Downers Grove, IL
                [2 ]Clinical Specialist, Infectious Diseases, Department of Pharmacy, Rush University Medical Center, Chicago, IL
                [3 ]Pharmacy Manager, Dominicks Pharmacy, Chicago, IL
                Article
                DOI: 10.1345/aph.1G232
                PubMed ID: 18094341
                SO-VID: b4980250-8ae0-43e3-b113-090363320812
                Copyright © © 2008
                License:

                http://journals.sagepub.com/page/policies/text-and-data-mining-license

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