Ultralow-density nanostructured metal foams: combustion synthesis, morphology, and composition.

The synthesis of low-density, nanoporous materials has been an active area of study in chemistry and materials science dating back to the initial synthesis of aerogels. These materials, however, are most often limited to metal oxides, e.g., silica and alumina, and organic aerogels, e.g., resorcinol/formaldehyde, or carbon aerogels, produced from the pyrolysis of organic aerogels. The ability to form monolithic metallic nanocellular porous materials is difficult and sometimes elusive using conventional methodology. Here we report a relatively simple method to access unprecedented ultralow-density, nanostructured, monolithic, transition-metal foams, utilizing self-propagating combustion synthesis of novel transition-metal complexes containing high nitrogen energetic ligands. During the investigation of the decomposition behavior of the high-nitrogen transition metal complexes, it was discovered that nanostructured metal monolithic foams were formed in a post flame-front dynamic assembly having remarkably low densities down to 0.011 g cm(-3) and extremely high surface areas as high as 270 m(2) g(-1). We have produced monolithic nanoporous metal foams via this method of iron, cobalt, copper, and silver metals. We expect to be able to apply this to many other metals and to be able to tailor the resulting structure significantly.

Remarkable spectator ligand effect on the rate constant of ligand substitution of (aqua)ruthenium(II) complexes.

The influence of two different di(1-pyrazolyl)alkane ligands on the rate constant of aqua ligand substitution of ruthenium(II) complexes with the formula [Ru(H2O)(L2)(tpmm)]2+ (L2 = di(1-pyrazolyl)methane (DPMet) or 2,2-di(1-pyrazolyl)propane (DPPro)) was investigated. A 9.4 x 10(5)-fold increase in the rate constant of ligand substitution at pH = 6.86 was observed when DPMet was replaced with DPPro. This remarkable increase was unexpected, considering that these bidentate ligands appear quite similar. To help lend insight into this dramatic spectator ligand effect, the activation parameters for the ligand substitution reactions were determined, and single-crystal X-ray data were collected on the structurally analogous (chloro)ruthenium(II) complexes, [Ru(Cl)(L2)(tpmm)]+. These results are discussed in the context of a heteroscorpionate effect exerted by the DPPro ligand.

Redox chemistry of morpholine-based Os(VI)-hydrazido complexes: trans-[Os(VI)(tpy)(Cl)2(NN(CH2)4O)](2+).

The oxidations of benzyl alcohol, PPh3, and the sulfides (SEt2 and SPh2) (Ph = phenyl and Et = ethyl) by the Os(VI)-hydrazido complex trans-[Os(VI)(tpy)(Cl)2(NN(CH2)4O)](2+) (tpy = 2,2':6',2' '-terpyridine and O(CH2)4N(-) = morpholide) have been investigated in CH3CN solution by UV-visible monitoring and product analysis by gas chromatography-mass spectrometry. For benzyl alcohol and the sulfides, the rate law for the formation of the Os(V)-hydrazido complex, trans-[Os(V)(tpy)(Cl)2(NN(CH2)4O)](+), is first order in both trans-[Os(VI)(tpy)(Cl)2(NN(CH2)4O)](2+) and reductant, with k(benzyl) (25.0 +/- 0.1 degrees C, CH3CN) = (1.80 +/- 0.07) x 10(-4) M(-1) s(-1), k(SEt2) = (1.33 +/- 0.02) x 10(-1) M(-1) s(-1), and k(SPh2) = (1.12 +/- 0.05) x 10(-1) M(-1) s(-1). Reduction of trans-[Os(VI)(tpy)(Cl)2(NN(CH2)4O)](2+) by PPh3 is rapid and accompanied by isomerization and solvolysis to give the Os(IV)-hydrazido product, cis-[Os(IV)(tpy)(NCCH3)2(NN(CH2)4O)](2+), and OPPh3. This reaction presumably occurs by net double Cl-atom transfer to PPh3 to give Cl2PPh3 that subsequently undergoes hydrolysis by trace H2O to give the final product, OPPh3. In the X-ray crystal structure of the Os(IV)-hydrazido complex, the Os-N-N angle of 130.9(5) degrees and the Os-N bond length of 1.971(7) A are consistent with an Os-N double bond.

Redox-induced terpyridyl substitution in the Os(VI)-hydrazido complex, trans-[Os(VI)(tpy)(Cl)(2)(NN(CH(2))(4)O)](2+).

Reaction between the Os(VI)-hydrazido complex, trans-[Os(VI)(tpy)(Cl)(2)(NN(CH(2))(4)O)](2+) (tpy = 2,2':6',2"-terpyridine and O(CH(2))(4)N(-) = morpholide), and a series of N- or O-bases gives as products the substituted Os(VI)-hydrazido complexes, trans-[Os(VI)(4'-RNtpy)(Cl)(2)(NN(CH(2))(4)O)](2+) or trans-[Os(VI)(4'-ROtpy)(Cl)(2)(NN(CH(2))(4)O)](2+) (RN(-) = anilide (PhNH(-)); S,S-diphenyl sulfilimide (Ph(2)S=N(-)); benzophenone imide (Ph(2)C=N(-)); piperidide ((CH(2))(5)N(-)); morpholide (O(CH(2))(4)N(-)); ethylamide (EtNH(-)); diethylamide (Et(2)N(-)); and tert-butylamide (t-BuNH(-)) and RO(-) = tert-butoxide (t-BuO(-)) and acetate (MeCO(2)(-)). The rate law for the formation of the morpholide-substituted complex is first order in trans-[Os(VI)(tpy)(Cl)(2)(NN(CH(2))(4)O)](2+) and second order in morpholine with k(morp)(25 degrees C, CH(3)CN) = (2.15 +/- 0.04) x 10(6) M(-)(2) s(-)(1). Possible mechanisms are proposed for substitution at the 4'-position of the tpy ligand by the added nucleophiles. The key features of the suggested mechanisms are the extraordinary electron withdrawing effect of Os(VI) on tpy and the ability of the metal to undergo intramolecular Os(VI) to Os(IV) electron transfer. These substituted Os(VI)-hydrazido complexes can be electrochemically reduced to the corresponding Os(V), Os(IV), and Os(III) forms. The Os-N bond length of 1.778(4) A and Os-N-N angle of 172.5(4) degrees in trans-[Os(VI)(4'-O(CH(2))(4)Ntpy)(Cl)(2)(NN(CH(2))(4)O)](2+) are consistent with sp-hybridization of the alpha-nitrogen of the hydrazido ligand and an Os-N triple bond. The extensive ring substitution chemistry implied for the Os(VI)-hydrazido complexes is discussed.

Formation and Reactivity of the Osmium(IV)-Cyanoimido Complex [Os(IV) (bpy)(Cl)3 (NCN)](-).

Oxo-like reactivity exists for a new series of osmium complexes such as [Os(IV) (bpy)(Cl)3 (NCN)](-) (bpy=2,2'-bipyridine, see structure) containing the cyanoimido ligand. This ligand is formed directly at the metal center by the reaction of Os(VI) -nitrido precursors with tetraethylammonium cyanide. In the cyanoimido complexes there is an extensive electron-transfer chemistry at the metal center and an extensive functional-group chemistry based on the ligand.

Association of SPARC (osteonectin, BM-40) with extracellular and intracellular components of the ciliated surface ectoderm of Xenopus embryos.

SPARC (Secreted Protein, Acidic, Rich in Cysteine) was detected by immunohistochemistry in the sensorial layer of the bilayered embryonic epidermis of Xenopus laevis during neurulation, when a subset of the sensorial cells are selected to differentiate into ciliated cell precursors. After the ciliated cells had intercalated into the outer layer and had undergone ciliogenesis, intense SPARC immunostaining was associated with the cilia and remained associated with the cilia throughout their persistence on the epidermis. Circumferential SPARC immunostaining was also detected at the interface between surface epithelial cells. Animal cap explants indicated that the embryonic activation of SPARC expression in the dorsal ectoderm does not require signaling from factors secreted by the underlying mesoderm. Immunoelectron microscopy revealed that SPARC is intimately associated with the 9 + 2 microtubule arrays of cilia. Our data indicate that SPARC plays a role in the development and function of the surface ciliated epidermis of Xenopus embryos. We propose that the counter-adhesive activity of SPARC facilitates the intercalation of ciliary cell precursors to the surface epithelial layer, where its Ca(2+)-binding abilities promote cell-cell adhesion. Based on its association with ciliary microtubule arrays, we also propose that intracellular SPARC may play a role in regulating ciliary beat frequency and polarity.

Mechanism and molecular-electronic structure correlations in a novel series of osmium(V) hydrazido complexes.

Reaction between the Os(VI) nitrido (OsVI identical to N+) complexes [OsVI(L3)(Cl)2(N)]+ (L3 is 2,2':6',2"-terpyridine (tpy) or tris(1-pyrazolyl)methane (tpm)) and secondary amines (HN(CH2)4O = morpholine, HN(CH2)4CH2 = piperidine, and HN(C2H5)2 = diethylamine) gives Os(V)-hydrazido complexes, [OsV(L3)(Cl)2(NNR2)]+ (NR2 = morpholide, piperidide, or diethylamide). They can be chemically or electrochemically oxidized to Os(VI) or reduced to Os(IV) and Os(III). The Os-N bond lengths and Os-N-N angles in the structures of these complexes are used to rationalize the bonding between the dianionic hydrazido ligand and Os. The rate law for formation of the Os(V) hydrazido complexes with morpholine as the base is first order in [OsVI(L3)(Cl)2(N)]+ and second order in HN(CH2)4O with ktpy(25 degrees C, CH3CN) = (581 +/- 12) M-2 s-1 and ktpm(25 degrees C, CH3CN) = 2683 +/- 40 M-2 s-1. The proposed mechanism involves initial nucleophilic attack of the secondary amine on the Os(VI) nitrido group to give a protonated Os(IV)-hydrazido intermediate. It is subsequently deprotonated and then oxidized by OsVI identical to N+ to Os(V). The extensive redox chemistry for these complexes can be explained by invoking a generalized bonding model. It can also be used to assign absorption bands that appear in the electronic from the visible-near-infrared spectra including a series of d pi-->d pi interconfigurational bands at low energy.

Mechanistic control of product selectivity. Reactions between cis-/trans cis-/trans-[OsVI(tpy)(Cl)2(N)]+ and triphenylphosphine sulfide.

Reactions between the Os(VI)-nitrido complexes cis- and trans-[Os(VI)(tpy)(Cl)2(N)]+ (tpy is 2,2':6',2"-terpyridine) and triphenylphosphine sulfide, SPPh3, give the corresponding Os(IV)-phosphoraniminato, [Os(IV)(tpy)(Cl)2(NPPh3)]+, and Os(II)-thionitrosyl, [Os(II)(tpy)(Cl)2(NS)]+, complexes as products. The Os-N bond length and Os-N-P angle in cis-[Os(IV)(tpy)(Cl)2(NPPh3)](PF6) are 2.077(6) A and 138.4(4) degrees. The rate law for formation of cis- and trans-[Os(IV)(tpy)(Cl)2(NPPh3)]+ is first order in both [Os(VI)(tpy)(Cl)2(N)]+ and SPPh3 with ktrans(25 degrees C, CH3CN) = 24.6 +/- 0.6 M(-1) s(-1) and kcis(25 degrees C, CH3CN) = 0.84 +/- 0.09 M(-1) s(-1). As found earlier for [Os(II)(tpm)(Cl)2(NS)]+, both cis- and trans-[Os(II)(tpy)(Cl)2(NS)]+ react with PPh3 to give [Os(IV)(tpy)(Cl)2(NPPh3)]+ and SPPh3. For both complexes, the reaction is first order in each reagent with ktrans(25 degrees C, CH3CN) = (6.79 +/- 0.08) x 10(2) M(-1) s(-1) and kcis(25 degrees C, CH3CN) = (2.30 +/- 0.07) x 10(2) M(-1) s(-1). The fact that both reactions occur rules out mechanisms involving S atom transfer. These results can be explained by invoking a common intermediate, [Os(IV)(tpy)(Cl)2(NSPPh3)]+, which undergoes further reaction with PPh3 to give [Os(IV)(tpy)(Cl)2(NPPh3)]+ and SPPh3 or with [Os(VI)(tpy)(Cl)2(N)]+ to give [Os(IV)(tpy)(Cl)2(NPPh3)]+ and [Os(II)(tpy)(Cl)2(NS)]+.

Activation of SPARC expression in reactive stroma associated with human epithelial ovarian cancer.

OBJECTIVE: SPARC (secreted protein, acidic, rich in cysteine) is a calcium-binding counteradhesive glycoprotein that has the potential to play an important role in promoting tumor progression and invasiveness. SPARC has been reported to be markedly down-regulated in ovarian carcinomas relative to the normal surface epithelium and has been suggested to act as a tumor suppressor in ovarian cancer. To more precisely define potential changes in SPARC expression associated with malignant transformation of the ovary, we compared the distribution of SPARC mRNA and protein expression in patient specimens of malignant and nonmalignant ovaries. METHOD: SPARC mRNA and protein expression was examined in 24 human invasive ovarian cancers, 5 tumors of low malignant potential (LMP), and 8 nonmalignant ovaries by in situ hybridization and immunohistochemistry. RESULTS: In nonmalignant ovaries, SPARC mRNA expression was restricted to thecal and granulosa cells of vessiculated follicles. Cytoplasmic SPARC immunoreactivity was observed in these compartments, whereas variable SPARC immunostaining was observed in normal surface epithelial cells. In contrast, high-level expression of SPARC mRNA and protein was detected in stroma of ovaries containing malignant tumor cells, particularly at the tumor-stromal interface of the invading tumors. Lower levels and a more diffuse pattern of SPARC mRNA expression were associated with LMP specimens. SPARC mRNA was not expressed by ovarian adenocarcinoma or by surface epithelial cells. Consistent with the in situ hybridization data, SPARC immunoreactivity was found throughout the reactive stroma of specimens containing ovarian carcinoma. However, despite the lack of detectable SPARC mRNA, SPARC immunoreactivity was consistently observed within the cytoplasm of cancer cells. CONCLUSION: The pattern of SPARC expression shown in this study indicates that SPARC is up-regulated in reactive stroma associated with invasive ovarian cancer. Moreover, these results raise the possibility that SPARC secreted from the stroma is internalized by ovarian cancer cells and may exert important intracellular effects upon these cells.

A calcium-binding motif in SPARC/osteonectin inhibits chordomesoderm cell migration during Xenopus laevis gastrulation: evidence of counter-adhesive activity in vivo.

Secreted protein, acidic, rich in cysteine (SPARC) is a Ca2+-binding, counter-adhesive, extracellular glycoprotein associated with major morphogenic events and tissue remodeling in vertebrates. In Xenopus laevis embryos, SPARC is expressed first by dorsal mesoderm cells at the end of gastrulation and undergoes complex, rapid changes in its pattern of expression during early organogenesis. Another study has reported that precocious expression of SPARC by injection of native protein into the blastocoele cavity of pregastrula embryos leads to a concentration-dependent reduction in anterior development. Thus, normal development requires that the timing, spatial distribution, and/or levels of SPARC be regulated precisely. In a previous study, we demonstrated that injection of a synthetic peptide corresponding to the C-terminal, Ca2+-binding, EF-hand domain of SPARC (peptide 4.2) mimicked the effects of native SPARC. In the present investigation, peptide 4.2 was used to examine the cellular and molecular bases of the phenotypes generated by the aberrant presence of SPARC. Exposure of late blastula embryos to LiCl also generated a concentration-dependent reduction in anterior development; therefore, injections of LiCl were carried out in parallel to highlight the unique effects of peptide 4.2 on early development. At concentrations that caused a similar loss in anterior development (60-100 ng peptide 4.2 or 0.25-0.4 microg LiCl), LiCl had a greater inhibitory effect on the initial rate of chordomesoderm cell involution, in comparison with peptide 4.2. However, as gastrulation progressed, peptide 4.2 had a greater inhibitory effect on prospective head mesoderm migration than that seen in the presence of LiCl. Moreover, peptide 4.2 and LiCl had distinct influences on the expression pattern of dorso-anterior markers at the neural and tail-bud stages of development. Scanning electron microscopy showed that peptide 4.2 inhibited spreading of migrating cells at the leading edge of the involuting chordomesoderm. While still in close proximity to the blastocoele roof, many of the cells appeared rounded and lacked lamellipodia and filopodia extended in the direction of migration. In contrast, LiCl had no effect on the spreading or shape of involuting cells. These data are the first evidence of a counter-adhesive activity for peptide 4.2 in vivo, an activity demonstrated for both native SPARC and peptide 4.2 in vitro.

Regulation of SPARC expression during early Xenopus development: evolutionary divergence and conservation of DNA regulatory elements between amphibians and mammals.

SPARC (Secreted Protein, Acidic, Rich in Cysteine/osteonectin/BM-40) is a highly conserved metal-binding extracellular matrix (ECM) glycoprotein which is first expressed by Xenopus embryos during late gastrulation/early neurulation (stage 12/13), by presumptive notochord and somitic cells. When animal cap explants of stage 9 embryos were cultured in vitro, SPARC expression was not detected until sibling embryos reached late neurula stage (stage 19). Addition of activin, a potent dorsal mesoderm inducer, to animal caps resulted in SPARC being expressed by the time sibling embryos reached stage 16. While basic fibroblast growth factor (bFGF), a ventral mesoderm inducer, had modest effects on SPARC mRNA expression, the combination of both activin and bFGF was synergistic. The appearance, however, of SPARC transcripts 11 h after the addition of activin and bFGF, indicates that unknown intermediates were likely to be involved in activating SPARC expression. In order to identify the potential intermediate regulatory factors which may activate and control SPARC expression, we examined the genomic organization of the 5' end of the Xenopus SPARC gene. No significant homology to the equivalent region that is highly conserved in the mouse, bovine and human SPARC genes was observed. Thus, while mammalian SPARC promoters lack TATA or CAAT boxes, the Xenopus gene contains a consensus TATA box. Moreover, promoter-proximal GGA-box repeats necessary for high level expression of mammalian SPARC are absent in Xenopus. When reporter constructs containing the 5' flanking region of the Xenopus gene were microinjected into two-cell embryos, 868 bp of 5' flanking DNA was sufficient to mimic the temporal and tissue-specific pattern of SPARC expression observed in whole embryos. While a bovine SPARC promoter reporter construct containing 740 bp of the 5' flanking DNA was expressed at a significant level in Xenopus embryos, significant differences in the cell-type expression of the reporter genes were obtained between the bovine and Xenopus constructs. The data indicate that zygotic activation of SPARC mRNA is mediated by regulatory factors acting downstream of major mesoderm induction events. The high DNA sequence conservation at the 5' end of mammalian SPARC genes is not conserved in Xenopus. These differences led to differences in their ability to direct tissue-specific gene expression in early Xenopus embryos.