title: Hsp60 chaperonopathies and chaperonotherapy: targets and agents.
abstract: BACKGROUND
  Hsp60 (Cpn60) assembles into a tetradecamer that interacts with the co-chaperonin Hsp10 (Cpn10) to assist client polypeptides to fold, but it also has other roles, including participation in pathogenic mechanisms.
  
  
  METHODS
  Hsp60 chaperonopathies are pathological conditions, inherited or acquired, in which the chaperone plays a determinant etiologic-pathogenic role. These diseases justify selection of Hsp60 as a target for developing agents that interfere with its pathogenic effects. We provide information on how to proceed.
  
  
  CONCLUSIONS
  The information available encourages the development of ways to improve Hsp60 activity (positive chaperonotherapy) when deficient or to block it (negative chaperonotherapy) when pathogenic. Many questions are still unanswered and obstacles are obvious. More information is needed to establish when and why autologous Hsp60 becomes a pathogenic autoantigen, or induces cytokine formation and inflammation, or favors carcinogenesis. Clarification of these points will take considerable time. However, analysis of the Hsp60 molecule and a search for active compounds aimed at structural sites that will affect its functioning should continue without interruption. No doubt that some of these compounds will offer therapeutic hopes and will also be instrumental for dissecting structure-function relationships at the biochemical and biological (using animal models and cultured cells) levels.
authors.affiliation: Euro-Mediterranean Institute of Science and Technology (IEMEST) , Palermo , Italy.
authors.forename: Francesco
authors.initials: F
authors.lastname: Cappello
authors.forename: Antonella
authors.initials: A
authors.lastname: Marino Gammazza
authors.forename: Antonio
authors.initials: A
authors.lastname: Palumbo Piccionello
authors.forename: Claudia
authors.initials: C
authors.lastname: Campanella
authors.forename: Andrea
authors.initials: A
authors.lastname: Pace
authors.forename: Everly
authors.initials: E
authors.lastname: Conway de Macario
authors.forename: Alberto J L
authors.initials: AJ
authors.lastname: Macario
mesh_terms: D000818:Animals; D001327:Autoimmune Diseases / Q000378:metabolism; D018834:Chaperonin 60 / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D007249:Inflammation / Q000378:metabolism; D009369:Neoplasms / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D018834:Chaperonin 60