title: [Glycopeptides].
abstract: OBJECTIVE
  To review pharmacology, pharmacokinetic and therapeutic use of glycopeptides in intensive care units.
  
  
  METHODS
  Extraction from Medline database of French and English articles on glycopeptides and search along with major review articles.
  
  
  METHODS
  The collected articles were reviewed and selected according to their quality and originality. The more recent data were selected.
  
  
  RESULTS
  Glycopeptides are bactericidal antibiotics which are only active against Gram positive species acting by inhibiting peptidoglycan synthesis. They had been in clinical use for almost 30 years without high-level resistance underlining. For ten years, there have been disturbing reports of first, resistance to vancomycin in enterococcal species and more recently in strains of Staphylococcus aureus by complex and large mechanisms of action. This new resistances may lead to a therapeutic impasse and a fatal issue for infected patients. The only response to this situation is the respect of prescription rules and the careful use of antibiotics.
  
  
  CONCLUSIONS
  Considering their spectrum, glycopeptides are an antibiotic family which importance is fundamental to treat infected patients of intensive care units. Staff members of intensive care units are responsible for their good use.
authors.affiliation: Département d'anesthésie et de réanimation, hôpital Nord, Marseille, France.
authors.forename: M
authors.initials: M
authors.lastname: Léone
authors.forename: M L
authors.initials: ML
authors.lastname: Ayem
authors.forename: C
authors.initials: C
authors.lastname: Martin
mesh_terms: D000900:Anti-Bacterial Agents / Q000493:pharmacokinetics / Q000494:pharmacology / Q000627:therapeutic use; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000235:genetics / Q000502:physiology; D019729:Carbon-Oxygen Ligases / Q000235:genetics / Q000502:physiology; D002268:Carboxypeptidases; D003422:Critical Care; D003864:Depression, Chemical; D015195:Drug Design; D004347:Drug Interactions; D004352:Drug Resistance, Microbial; D004363:Drug Utilization; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006020:Glycopeptides; D006094:Gram-Positive Bacteria / Q000187:drug effects*; D016908:Gram-Positive Bacterial Infections / Q000188:drug therapy* / Q000453:epidemiology / Q000401:mortality; D006801:Humans; D007262:Infusions, Intravenous; D000077427:Lipoglycopeptides; D008565:Membrane Proteins; D009876:Operon; D010453:Peptide Synthases; D010457:Peptidoglycan / Q000096:biosynthesis; D046929:Serine-Type D-Ala-D-Ala Carboxypeptidase; D017334:Teicoplanin / Q000008:administration & dosage / Q000493:pharmacokinetics; D014157:Transcription Factors / Q000235:genetics / Q000502:physiology; D014640:Vancomycin / Q000008:administration & dosage / Q000493:pharmacokinetics / Q000031:analogs & derivatives; D020713:Vancomycin Resistance / Q000235:genetics
chemical_list: D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D004791:Enzyme Inhibitors; D006020:Glycopeptides; D000077427:Lipoglycopeptides; D008565:Membrane Proteins; D010457:Peptidoglycan; D014157:Transcription Factors; C071437:VanA ligase, Bacteria; C079913:VanB protein, Enterococcus; C092230:VanZ protein, Enterococcus faecium; C073902:VanR protein, bacteria; D017334:Teicoplanin; D014640:Vancomycin; D002268:Carboxypeptidases; D046929:Serine-Type D-Ala-D-Ala Carboxypeptidase; C117912:VanY protein, Bacteria; C091956:VanX dipeptidase; D019729:Carbon-Oxygen Ligases; D010453:Peptide Synthases; C122181:VanD protein, Enterococcus faecium; C100708:oritavancin