Other PrP Interacting Molecules

GFAP expressed in Escherichia coli, suggesting tiiat Pli 45 and GFAP are indeed the same proteins. 

Pli 45 was found exclusively in brain, whereas Pli 110 is present in several tissues, such as brain, lung, liver, spleen, and pancreas. Pli 110 was shown to be identical to PTP-associated splicing factor (PSF) (Oesch, 

Aplp2 is a member of the APP-like (amyloid precursor protein) family, playing an important role in the pathogenesis of Alzheimer disease (AD). The major component of the senile plaques observed in AD is the AP peptide, which is derived from the APP protein (Glenner and Wong, 1984 Masters et al, 1985). PrP and Aplpl are both membrane proteins hence it is likely that they could interact on the cell surface. 

Bcl-2 and Bax act as antiapoptotic and proapoptotic molecules in apoptosis, respectively. Moreover, the ratio of Bax-Bcl-2 heterodimers to homodimers of each protein is important for the regulation of apoptosis (Oltvai and Korsmeyer, 1994 O Dowd et al, 1988 Yang and Korsmeyer, 

An involvement of the PrP -laminin interaction in neuritogene-sis induced by NGF plus laminin in the PC-12 cell line was further suggested (Graner et al, 2000). Neuritogenesis, induced either by laminin or its y-l-derived peptide in primary cultures from rat or either wild-type or PrP null mice hippocampal neurons, might imply that PrP could be the main cellular receptor for the particular y-1 domain located in the carboxy terminus of laminin (Graner et al, 2000). 

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