Indications for the Nonexistence of Three-Neutron Resonances near the Physical Region

The pending question of the existence of three-neutron resonances near the physical energy region is reconsidered. Finite rank neutron-neutron forces are used in Faddeev equations, which are analytically continued into the unphysical energy sheet below the positive real energy axis. The trajectories of the three-neutron S-matrix poles in the states of total angular momenta and parity J^\pi=1/2 +- and J^\pi= 3/2 +- are traced out as a function of artificial enhancement factors of the neutron-neutron forces. The final positions of the S-matrix poles removing the artificial factors are found in all cases to be far away from the positive real energy axis, which provides a strong indication for the nonexistence of nearby three-neutron resonances. The pole trajectories close to the threshold E=0 are also predicted out of auxiliary generated three-neutron bound state energies using the Pad\'e method and agree very well with the directly calculated ones.Comment: 20 pages, 7 Postscript figures, fig.1 is corrected, uses relax.st

Syndecan-1 and FGF-2, but Not FGF Receptor-1, Share a Common Transport Route and Co-Localize with Heparanase in the Nuclei of Mesenchymal Tumor Cells

Syndecan-1 forms complexes with growth factors and their cognate receptors in the cell membrane. We have previously reported a tubulin-mediated translocation of syndecan-1 to the nucleus. The transport route and functional significance of nuclear syndecan-1 is still incompletely understood. Here we investigate the sub-cellular distribution of syndecan-1, FGF-2, FGFR-1 and heparanase in malignant mesenchymal tumor cells, and explore the possibility of their coordinated translocation to the nucleus. To elucidate a structural requirement for this nuclear transport, we have transfected cells with a syndecan-1/EGFP construct or with a short truncated version containing only the tubulin binding RMKKK sequence. The sub-cellular distribution of the EGFP fusion proteins was monitored by fluorescence microscopy. Our data indicate that syndecan-1, FGF-2 and heparanase co-localize in the nucleus, whereas FGFR-1 is enriched mainly in the perinuclear area. Overexpression of syndecan-1 results in increased nuclear accumulation of FGF-2, demonstrating the functional importance of syndecan-1 for this nuclear transport. Interestingly, exogenously added FGF-2 does not follow the route taken by endogenous FGF-2. Furthermore, we prove that the RMKKK sequence of syndecan-1 is necessary and sufficient for nuclear translocation, acting as a nuclear localization signal, and the Arginine residue is vital for this localization. We conclude that syndecan-1 and FGF-2, but not FGFR-1 share a common transport route and co-localize with heparanase in the nucleus, and this transport is mediated by the RMKKK motif in syndecan-1. Our study opens a new perspective in the proteoglycan field and provides more evidence of nuclear interactions of syndecan-1

Heparan Sulfate Acts as a Bone Morphogenetic Protein Coreceptor by Facilitating Ligand-induced Receptor Hetero-oligomerization

Cell surface heparan sulfate (HS) potentiates the activities of various growth factors. Here we show that HS stimulates bone morphogenetic protein (BMP) activity by enhancing recruitment of type II receptor subunits to BMP-type I receptor complexes, suggesting a view of HS as a catalyst of the formation of signaling complexes