Alard JE

Alberto JL Macario

Almanzar G

Amino N

Andrea Pace

Anraku I

Antonella Marino Gammazza

Antonio Palumbo Piccionello

Arnold K

Ayada K

Baekkeskov S

Bajramovic JJ

Ban HS

Barazi HO

Binder RJ

Bini L

Blasi C

Braig K

Brea D

Brocchieri L

Bross P

Brudzynski K

Bukau B

Campanella C

Cappello F

Cassiano C

Castelli M

Castilla C

Chandra D

Chapman E

Chaudhry C

Chen S

Chen W

Chiti F

Clare DK

Claudia Campanella

Cohen-Tervaert JW

Deniz E

Desmetz C

Dieudé M

Drastichova Z

Dubaquie Y

Elst EF

Everly Conway de Macario

Faried A

Fei X

Fenton WA

Ford PJ

Fortuna CG

Francesco Cappello

Frostell A

Gazali A

Ghosh JC

Glaessgen A

Grundtman C

Gupta RS

Gupta S

Guéry JC

Gülden E

Hahn DL

Hamelin C

Hammarström P

Hansen JJ

He Y

Hitotsumatsu T

Hjerpe E

Horwich A

Hoymans VY

Hsu PL

Hwang YJ

Ishida K

Itoh H

Johansson B

Jones DB

Kamishima T

Khalil AA

Kiefer F

Kirchhoff SR

Kobayashi K

Kol A

Kondoh Y

Introduction: 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.
Area covered: 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.
Expert opinion: 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 autoan&#x2;tigen, or induces cytokine formation and inflammation, or favors carcinogen&#x2;esis. 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 inter&#x2;ruption. 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) level

CAPPELLO, Francesco

MARINO GAMMAZZA, Antonella

PALUMBO PICCIONELLO, Antonio

CAMPANELLA, Claudia

PACE, Andrea

Conway de Macario, E

Macario, AJ

Archivio istituzionale della ricerca - Università di Palermo

Hsp60 chaperonopathies and chaperonotherapy: targets and agents.

Crossref

Expert Opinion on Therapeutic Targets

Hsp60 chaperonopathies and chaperonotherapy: targets and agents

https://iris.unipa.it/retrieve/handle/10447/98315/130199/Cappello%20et%20al.%2c%202014.pdf

Hsp60 chaperonopathies and chaperonotherapy: targets and agents.

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Archivio istituzionale della ricerca - Università di Palermo

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