The taxonomy,genetics, production and uses of the cultivated species ofCucurbita

Hundreds of varieties in the five reco?nized species of this ?enus, all native to the Americas, are the sources of the well known pumpkins and squashes, of which about 150,000 tons, fresh wei?ht, in 481/2 million No. 2 cans, is the annual canned pack alone in the United States. The seeds constitute a potential but so far wholly undeveloped source of valuable oil.     

Aesthetic augmentation of the posterior mandible

The posterior mandible begins just behind the mental nerve and second bicuspid bilaterally, extends to the posterior edge of the ramus, and then runs superiorly to the zygomatic arch. Augmentation of the posterior mandible is possible by use of a synthetic implant that is tailored individually to each patient's specific needs. Implant plant thickness varies from 4 to 8 mm, with an average thickness of 6 mm. Careful preoperative planning is done based on an aesthetic assessment of the amount of highlighting desired, thickness of the soft tissues, and the use of life-size photographs and cephalometric and Panorex x-rays. A pattern is cut, and the implant is carved to fit the patient. Insertion of the material after careful tailoring to the individual patient's own mandibular size and configuration requires a generous posterior lower buccal sulcus incision. Antibiotic irrigation and systemic antibiotics are essential, and careful closure in two layers completes the procedure. One implant in the series extruded in a patient who had had radiation therapy, and one patient required repositioning of the implant. Otherwise, in 22 patients there were no infections or permanent morbidity. The procedure seems to be a realistic and safe one for both the youthful and aging face, as demonstrated in patients in this series, with ages varying from 16 to 40 years.     

Splice variants of mda-7/IL-24 differentially affect survival and induce apoptosis in U2OS cells

Interleukin-24 (mda-7/IL-24) is a cytokine in the IL-10 family that has received a great deal of attention for its properties as a tumor suppressor and as a potential treatment for cancer. In this study, we have identified and characterized five alternatively spliced isoforms of this gene. Several, but not all of these isoforms induce apoptosis in the osteosarcoma cell line U2OS, while none affect the survival of the non-cancerous NOK cell line. One of these isoforms, lacking three exons and encoding the N-terminal end of the mda-7/IL-24 protein sequence, caused levels of apoptosis that were higher than those caused by the full-length mda-7/IL-24 variant. Additionally, we found that the ratio of isoform expression can be modified by the splice factor SRp55. This regulation suggests that alternative splicing of mda-7/IL-24 is under tight control in the cell, and can be modified under various cellular conditions, such as DNA damage. In addition to providing new insights into the function of an important tumor suppressor gene, these findings may also point toward new avenues for cancer treatment.     

Dihydrotetramethylrosamine: a long wavelength, fluorogenic peroxidase substrate evaluated in vitro and in a model phagocyte

Dihydrotetramethylrosamine, a fluorogenic substrate for peroxidase, and its fluorescent oxidation product, tetramethylrosamine chloride, were evaluated. The substrate is colorless and nonfluorescent while the oxidized dye absorbs at 550 nm and emits at 574 nm in both methanol and water. In vitro assays demonstrated that the substrate was oxidized to the fluorophore by horseradish peroxidase in the presence of hydrogen peroxide. In vivo uptake and oxidation of the substrate by Amoeba proteus was characterized by the initial appearance of fluorescent phagocytic vacuoles with subsequent localization in vesicular organelles the size and shape of protozoan mitochondria. Similar staining patterns occurred in cells incubated with substrate, oxidized rosamine or rhodamine 123, a known mitochondrial stain.     

M protein (M1) of influenza virus: antigenic analysis and intracellular localization with monoclonal antibodies.

A panel of 16 monoclonal antibodies recognizing M protein (M1) of influenza virus was generated. Competition analyses resulted in localization of 14 monoclonal antibodies to three antigenic sites. Three monoclonal antibodies localized to site 1B recognized a peptide synthesized to M1 (residues 220 to 236) with enzyme-linked immunosorbent assay titers equivalent to or greater than that seen with purified M1; therefore, site 1B is located near the C terminus of M1. Sites 2 and 3 localize to the N-terminal half of M1. Antigenic variation of M proteins was seen when the monoclonal antibodies were tested against 14 strains of type A influenza viruses. Several monoclonal antibodies showed specific recognition of A/PR/8/34 and A/USSR/90/77 M proteins and little or no reactivity for all other strains tested. Immunofluorescence analysis with the monoclonal antibodies showed migration of M protein to the nucleus during the replicative cycle and demonstrated association of M protein with actin filaments in the cytoplasm. Use of a vaccinia virus recombinant containing the M-protein gene demonstrated migration of M protein to the nucleus in the absence of synthesis of gene products from other influenza virus RNA segments.