Short-term memory formation and long-term memory consolidation are enhanced by cellular prion association to stress-inducible protein 1

Disease-associated Mutations in the Prion Protein Impair Laminin-induced Process Outgrowth and Survival

“…In the last decade a diverse range of functions has been attributed to the native PrP C protein, such as neuroprotection against cellular and systemic insults, neuritogenesis, neuronal plasticity and excitability, and memory formation and consolidation (21)(22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33). Noteworthy, PrP C mutations associated to CJD, fatal familial insomnia, and Gerstmann-Straussler-Scheinker disease decrease or abolish the anti-bax function in primary human neurons and breast cancer cell lines promoting programmed cell death (34).…”

Prion protein interaction with stress-inducible protein 1 enhances neuronal protein synthesis via mTOR

“…In particular, PrP C binding to the astrocyte-secreted stress-inducible protein 1 (STI1) (15) induces neuronal survival, neuritogenesis, and memory formation and consolidation (16,17 Fig. 1A) did not present any response to STI1, whereas protein synthesis induced by BDNF was equivalent in both cell types, indicating that STI1 signaling is dependent on PrP C and that PrP C -null cells can respond with increased protein synthesis to other neurotrophic stimuli (Fig.…”

Prion potency in stem cells biology

“…STI1 specifically binds to PrP and leads to a significant number of biological effects such as neuritogenesis and neuroprotection 56,57 through α7 nicotinic acetylcholine receptor activity, 58 and astrocyte development, 54 and also alters in vivo processes such as short-term memory formation and longterm memory consolidation. 59 We found that STI1 positively modulates the self-renewal of NSC in a PrP-dependent manner and this effect can be disrupted with STI1 antibodies. The mechanism by which STI1 enhances self-renewal requires the induction of cell proliferation, without apparent involvement of cell protection 56 ( Fig.…”