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. 2012 Aug 20;198(4):561–574. doi: 10.1083/jcb.201111136

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© 2012 Thon et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 3. — TLR9 does not colocalize with known PLT α granule, dense granule, lysosomal, or endosomal markers. Washed human whole-blood PLTs were spun down onto poly-l-lysine–coated glass cover slides, permeabilized with 0.5% Triton X-100 for 5 min, and probed for TLR9. (A) PLTs were colabeled for α granule (fibrinogen, CD62P, PDGF-B, VEGF, CD42a, and CD42b), dense granule (serotonin), lysosome (LAMP-1), or endosome (M6P and syntaxin-13) protein markers using two separate colors. Insets represent magnified regions outlined by the yellow boxes for each image. (B) TLR9 labeling of whole-blood PLTs from patients with Gray PLT and Hermansky–Pudlack syndromes was compared with human normal PLT controls. All samples were examined by wide-field fluorescence microscopy. (C) 2D intensity scatter plot analysis of image overlays reveal that, although TLR9 colocalizes well with PDI, it does not colocalize with either TLR7 or TLR8. These data suggest that TLR9 and PDI may be distributing to a unique intracellular body (T granule) underlying the plasma membrane in resting human PLTs. (insets) Bars, 2 µm.