Download (.pdf) Study of 3D cell morphology and effect on light scattering distribution
Andrew E. Ekpenyong, Junhua Ding, Li V. Yang, Nancy R. Leffler, and Jun Q. Lu East Carolina Univ. (USA) R. Scott Brock Virginia Commonwealth Univ. (USA) Xin-Hua Hu East Carolina Univ. (USA). Published in Proc. SPIE, Vol. 7367, 73671J (2009); doi:10.1117/12.831510
We have acquired and reconstructed the 3D structures of B16F10 mouse melanoma cells to study morphology changes in... more
We have acquired and reconstructed the 3D structures of B16F10 mouse melanoma cells to study morphology changes in response to gene variations. The 3D structure can be imported into a parallel FDTD code to model light scattering distribution and determine morphological parameters such as volumes of cytoplasm, nucleus and mitochondria. We found that the measured parameters agree with the light scatter data obtained with a flow cytometer, showing significant differences between the genetically modified and the unmodified melanoma cells.
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The angiogenic inhibitor long pentraxin PTX3 forms an asymmetric octamer with two binding sites for FGF2.
by David Briggs
I did a bit of the SAXS analysis. Hence waaay down author list.
The inflammation-associated long pentraxin PTX3 plays key roles in innate immunity, female fertility and vascular... more The inflammation-associated long pentraxin PTX3 plays key roles in innate immunity, female fertility and vascular biology; e.g. it inhibits fibroblast growth factor 2 (FGF2)-mediated angiogenesis. PTX3 is composed of multiple protomers, each comprised of distinct N- and C-terminal domains, however, it is not known how these are organized or contribute to its functional properties. Here, biophysical analyses reveal that PTX3 is composed of eight identical protomers, associated through disulfide bonds, forming an elongated, and asymmetric, molecule with two differently sized domains interconnected by a stalk. The N-terminal region of the protomer provides the main structural determinant underlying this quaternary organization, supporting formation of a disulfide-linked tetramer and a dimer of dimers (a non-covalent tetramer) giving rise to the asymmetry of the molecule. Furthermore, the PTX3 octamer is shown to contain two FGF2 binding sites, where it is the tetramers that act as the functional units in ligand recognition. Thus, these studies provide a unifying model of the PTX3 oligomer explaining both its quaternary organization and how this is required for its anti-angiogenic function.