Seed dispersal of wild radishes and its association with within-population spatial distribution.

BACKGROUND: The wild radishes, Raphanus raphanistrum and R. pugioniformis (Brassicaceae) are native to the East Mediterranean region. However, whereas R. raphanistrum is widely distributed worldwide, the endemic R. pugioniformis is limited to specific habitats. In R. raphanistrum the diaspores of the indehiscent fruits comprise glabrous, light, single-seeded segments, whereas the intact fruits of R. pugioniformis are heavy and covered with spiny backward-pointing trichomes. We aimed to investigate whether the structure of the diaspores was directly associated with long- and short-range dispersal in R. raphanistrum and R. pugioniformis, respectively. We further surveyed within-population spatial distributions, to test the hypothesis that short- and long-range dispersal contribute to a patchy vs. uniform distribution patterns of R. pugioniformis and R. raphanistrum, respectively. RESULTS: The results indicated that dispersal by wind and run-off water was substantially lower for diaspores of R. pugioniformis than for those of R. raphanistrum diaspores. Supporting the hypothesis that backward-pointing trichomes promote adherence to soil particles, the displacement on soil surface of R. pugioniformis fruits depended on their orientation relative to wind direction. Furthermore, trichome removal from fruits of R. pugioniformis significantly reduced wind velocity needed to remove fruits that were placed on soils typical of the species' natural habitats. The spatial-distribution survey results indicated a patchy distribution of R. pugioniformis populations as compared with the more uniform arrangement in the studied populations of R. raphanistrum; consistent with the unidirectional vs. homogeneous wind dispersal of the respective diaspores, with respect to wind direction. In addition, R. pugioniformis population sizes changed less between years than those of R. raphanistrum. CONCLUSIONS: Overall, our results indicate that fruit structure is strongly linked to dispersal ability and spatial distribution of the two closely related wild radish species. Whereas R. raphanistrum inhabits homogenous sandy soil habitats, the distribution range of R. pugioniformis includes heterogeneous environments in which growth niches are scarcer. We suggest that the different modes of dispersal have evolved as adaptive traits appropriate to the species' specific habitats.

Intraperitoneal topoisomerase-I inhibitors. Preliminary findings with 9-aminocamptothecin.

The i.p. administration of topoisomerase I (Topo I) inhibitors has a pharmacologic advantage over intravenous application, including preservation of the biologically active lactone form. In our ongoing study, patients have received 9-amino-20(S)-camptothecin (9-AC) i.p. on days 1, 3, 5, 8, 10, and 12, repeated every 4 weeks. The daily dose has been escalated to level IV of 1.5 mg/m2 (9.0 mg/m2 per course), median of 3 cycles, range 1-4, with a reversible Grade 3 neutropenia in one patient. Responses included one CR (resolution of a pleural effusion), two patients without progressive disease (PD), two not evaluable, and two patients too early for evaluation. The area under the curve (AUC)i.p./AUCpl ratio (pharmacologic advantage) ranged from 7.6 to 16.5 on average, and, using nonlinear modeling, the pharmacologic decay data were fit to one- or two-compartmental models. Overall, a 9-AC i.p. application is well tolerated and anticipated to be an active regimen against i.p. malignancies, particularly those known to be sensitive to systemic Topo-I inhibitors.

Identification of a heparin binding peptide on the extracellular domain of the KDR VEGF receptor.

Vascular endothelial growth factor (VEGF), a potent and specific activator of endothelial cells, is expressed as multiple homodimeric forms resulting from alternative RNA splicing. VEGF121 does not bind heparin while the other three isoforms do, and it has been documented that the binding of VEGF165 to its receptor is dependent upon cell surface heparin sulfate proteoglycans. Little is known about the biochemical mechanism that allows for heparin regulation of growth factor binding. For example, it is not clear whether heparin interactions with growth factor or with cell surface receptors or both are essential for VEGF binding to its receptor. In this manuscript we provide results which are consistent with the hypothesis that an interaction between heparin and a site on the KDR receptor subtype is essential for VEGF165 binding. First, we demonstrate that expression of KDR into a CHO cell line deficient in heparan sulfate biosynthesis does not allow VEGF165 binding unless heparin is exogenously added during the binding assay. Secondly, we show that a ten amino acid synthetic peptide, corresponding to a sequence from the extracellular domain of the KDR, both inhibits VEGF165 binding to the receptor and also binds heparin with high avidity. Third, affinity purification of heparin molecules on a KDR-derived peptide affinity column, together with capillary electrophoresis and polyacrylamide electrophoresis analysis, was used to show that the KDR-derived peptide interacts with a specific subset of polysaccharide chains contained in the unfractionated heparin. Taken together, these results are consistent with the hypothesis that interactions between cell surface heparan sulfate proteoglycans and the VEGF receptor contribute to allowing maximal VEGF binding.