Hsp70/Hsp90 Organising Protein (Hop): Beyond Interactions with Chaperones and Prion Proteins - The Networking of Chaperones by Co-chaperones - page 75

Table 3.1 (continued)

Condition Hop status a Model system Cellular function b Proposed biological

mechanism b

Reference

Development S? Neural stem cell culture Self-renewal and

proliferation

Inhibition reduced neurosphere
formation; self-renewal and
proliferation

Lopes et al. ( 2012 )

KD Murine ESC culture Pluripotency Blocked embryoid body

formation

Longshaw et al. ( 2009 )

KO Mouse model Embryonic

development

Embryonic lethal (E10.5) Beraldo et al. ( 2013 )

UP, S, I Developing versus mature retinal

tissues (rat)

Cell proliferation and
death

Retinal development indepen-
dent of PrP C

Arruda-Carvalho et al.
( 2007 )

Memory I (antibodies);

UP

Intra-hippocampal infusion Reduced performance Short term and long term

memory inhibited

Coitinho et al. ( 2007 )

ND (but involves PrP C binding
site)

OE (Peptide
230-245)

Peptide 230-245 from Hop
(including PrP C binding site)

Enhanced
performance

PrP C dependent activa-
tion of signalling pathways,
endocytosis

Neuronal
function

Lopes et al. ( 2005 );
Lima et al. ( 2007 );
Roffe et al. ( 2010 );
Caetano et al. ( 2008 )
a KD knockdown by RNA interference, S secreted or extracellular Hop, KO gene knockout, OE Hop overexpressed (recombinant form), UP Hop upregulated
(endogenous form), CO Hop in complex with Hsp90 and Hsp70, I pharmacological inhibition, MUT mutated
b ND not determined

S? Mouse model and in vitro cell lines Neuroprotection,

neurite formation