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Reply to 'Is PRG-1 a new lipid phosphatase?'

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Correspondence to Robert Nitsch.

Supplementary information

Supplementary Fig. 1

(a) Chromatography from the HPLC-analysis of the normalized cpm for PRG-1 in comparison to the point-mutation PRG-1HIS/LYS. HPLC analysis were carried out as described in the Materials and Methods section. The position of 2-monoolein, oleic acid, and 1, 2 diolein were identified by co-injection of authentic standards. In the overall profile of eluted radioactivity, the position of standards are characterized as arrows.

(b) PRG-1 and PRG-1His/Lys overexpression in N1E-115 cells. N1E-115 cells were transfected with a pPRG-1 eGFP and pPRG-1His/Lys eGFP fusion construct. The wild type PRG-1 as well as the point-mutated PRG-1His/Lys are localized in the plasma membrane and in internal membranes.

(c)Attenuation of LPA-induced neurite retraction in PRG-1-expressing cells. GFP-expressing (top) and PRG-1-expressing N1E-115 cells (bottom) were cultured under serum-free conditions and observed by videomicroscopy for 20 min. At 2.5 min 2.5μM LPA was added to the medium (arrow). GFP transfectants show a rapid neurite retraction and cell rounding response, whereas PRG-1 transfectants still maintain their neurite extensions. Application of TRP resulted in neurite retraction in PRG-1-transfected N1Ecells. Note that LPA application did not induced cell lysis even after 17.5 minutes.

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Bräuer, A., Savaskan, N., Kühn, H. et al. Reply to 'Is PRG-1 a new lipid phosphatase?'. Nat Neurosci 7, 789–790 (2004).

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