A novel RUNX1 mutation in familial platelet disorder with propensity to develop myeloid malignanciesWe describe a Japanese family with familial platelet disorder with propensity to develop myeloid malignancies (FPD/MM). Among the three affected individuals, two members developed myeloid malignancies. Sequence studies demonstrate that all affected individuals of the pedigree display a heterozygous single nucleotide deletion in exon 8 of the RUNX1 gene. Haematologica. 2008 Jan; 93:(1)155-156.

No abstract

Phytochemical examination of Convallaria majalis (Liliaceae) whole plants yielded 15 steroidal glycosides (1–15), including nine new compounds (4–6, 10–15) with a lycotetrose unit. The structures of the new compounds were determined using two-dimensional Nuclear magnetic resonance (NMR) analyses and chemical methods. The isolated compounds were evaluated for cytotoxicity against HL-60 human promyelocytic leukemia cells, A549 human lung adenocarcinoma cells, and HSC-4 and HSC-2 human oral squamous cell carcinoma cell lines. Of these, (25S)-spirost-5-en-3β-yl O-β-d-glucopyranosyl-(1→2)-O-[β-d-xylopyranosyl-(1→3)]-O-β-d-glucopyranosyl-(1→4)-β-d-galactopyranoside (1) exhibited cytotoxic activity against HL-60, A549, HSC-4, and HSC-2 cells with IC50 values ranging from 0.96 to 3.15 μM. The corresponding furostanol glycoside of 1, (25S)-26-[(β-d-glucopyranosyl)oxy]-22α-hydroxyfurost-5-en-3β-yl O-β-d-glucopyranosyl-(1→2)-O-[β-d-xylopyranosyl-(1→3)]-O-β-d-glucopyranosyl-(1→4)-β-d-galactopyranoside (8), was cytotoxic to the adherent cell lines of A549, HSC-4, and HSC-2 cells with IC50 values of 2.97, 11.04, and 8.25 μM, respectively. The spirostanol lycotetroside (1) caused necrotic cell death in A549 cells in a dose-dependent manner. Alternatively, the furostanol lycotetroside (8) induced apoptotic cell death in A549 cells in a time-dependent manner, as was evident by morphological observations and flow cytometry analyses.

Edited by Veli-Pekka LehtoKeywords: Collagen Synthetic collagen Collagen-related peptide Blood platelet Glycoprotein VI a b s t r a c t Novel synthetic collagen fibers, poly(PHG) made by polycondensation of Pro-Hyp-Gly, spontaneously assume polymeric structure with molecular weights greater than 10 5 . Its application for biomaterials has been explored, but that for a platelet agonist has not been investigated. Poly(PHG)-induced platelet aggregation independently of thromboxane A 2 and integrin a2b1. Poly(PHG)-induced tyrosine phosphorylation of glycoprotein VI (GPVI)-related molecules and failed to activate GPVI/ FcRc-deficient platelets. Binding of GPVI to poly(PHG) was confirmed by a surface plasmon resonance spectroscopy, suggesting that poly(PHG) activates platelets through GPVI. Poly(PHG) is an useful research tool to investigate GPVI-mediated signals and a substitute for collagen in platelet functional assays.