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Mesencephalic Astrocyte-derived Neurotrophic Factor (MANF) forms an evultionarily conserved distinct family of growth factors together with the Cerebral Dopamine Neurotrophic Factor (CDNF) (Lindholm and Saarma, 2010). MANF and also CDNF can repair dopamine neurons in different toxin-induced lesion models in vivo in rats (Voutilainen et al, 2009). MANF can protect neurons also in rat models of stroke (Airavaara et al, 2009). MANF also protects cardiac myocytes in myocardial infarction (Glembotski et al, 2012).

However, the mechanisms of the protective actions of MANF, including it's receptor, remain to be discovered. It is however known, that MANF is localized in the ER and is part of the unfolded protein (UPR) response cascade and is secreted upon ER-stress in vitro, also binding the ER chaperone GRP78 (Glembotski et al., 2012, Lindholm and Saarma, 2010, <ref>PMID:18561914</ref>, ~~Mizobouchi et al., 2007~~).

However, the mechanisms of the protective actions of MANF, including it's receptor, remain to be discovered. It is however known, that MANF is localized in the ER and is part of the unfolded protein (UPR) response cascade and is secreted upon ER-stress in vitro, also binding the ER chaperone GRP78 (Glembotski et al., 2012, Lindholm and Saarma, 2010, <ref>PMID:18561914</ref>, <ref>PMID:17507765</ref>).

In 2009 the crystal structure of MANF was solved by Parkash et al (Parkash et al, 2009), giving important insights into the function of MANF. The further content of this page is directed to dissecting the structure/function relation of the MANF protein.

Sandbox Reserved 938: Difference between revisions

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 Mesencephalic Astrocyte-derived Neurotrophic Factor (MANF) forms an evultionarily conserved distinct family of growth factors together with the Cerebral Dopamine Neurotrophic Factor (CDNF) (Lindholm and Saarma, 2010). MANF and also CDNF can repair dopamine neurons in different toxin-induced lesion models in vivo in rats (Voutilainen et al, 2009). MANF can protect neurons also in rat models of stroke (Airavaara et al, 2009). MANF also protects cardiac myocytes in myocardial infarction (Glembotski et al, 2012).
-However, the mechanisms of the protective actions of MANF, including it's receptor, remain to be discovered. It is however known, that MANF is localized in the ER and is part of the unfolded protein (UPR) response cascade and is secreted upon ER-stress in vitro, also binding the ER chaperone GRP78 (Glembotski et al., 2012, Lindholm and Saarma, 2010, <ref>PMID:18561914</ref>, Mizobouchi et al., 2007).
+However, the mechanisms of the protective actions of MANF, including it's receptor, remain to be discovered. It is however known, that MANF is localized in the ER and is part of the unfolded protein (UPR) response cascade and is secreted upon ER-stress in vitro, also binding the ER chaperone GRP78 (Glembotski et al., 2012, Lindholm and Saarma, 2010, <ref>PMID:18561914</ref>, <ref>PMID:17507765</ref>).
 In 2009 the crystal structure of MANF was solved by Parkash et al (Parkash et al, 2009), giving important insights into the function of MANF. The further content of this page is directed to dissecting the structure/function relation of the MANF protein.