Prominent collagen type VI expression in juvenile angiofibromas.

The extracellular matrix component collagen type VI demonstrates potent growth-stimulatory effects and has been associated with aggressive tumour growth. Although, juvenile angiofibromas (JAs) often exhibit an aggressive growth pattern, the collagen type VI expression of this fibrovascular tumour has not been addressed so far. RT-PCR, Western blot analysis and immunohistochemistry were used in this study to analyse collagen type VI, type VI collagen receptor subunits (integrin alpha1, alpha2, alpha10, alpha11 and beta1) and the type VI collagen receptor NG2 in JAs (N = 15) and nasal mucosa (NM, N = 8) samples. The mRNA expression of all three collagen type VI chains was found to be up-regulated significantly (P < 10(-3)-10(-5), adjusted) in JAs compared to NM tissues. The Western blot analysis proved highly prominent collagen-type VI expression in JAs. The ApoTome technique revealed strong collagen-type VI signals in tumour endothelium. NG2 (P < 10(-3), adjusted) and alpha11-integrin (P = 0.04, adjusted) showed a significantly higher mRNA expression levels in JAs than in NM samples. NG2, alpha1-, alpha2- and beta1-intergin were located to tumour vessels, and additional stromal signals were observed for NG2 and alpha1-integrin in JAs. This study demonstrates a prominent collagen-type VI expression in JAs. The collagen-type VI may exert an important growth stimulus in this tumour.

Arabidopsis INOSITOL TRANSPORTER2 mediates H+ symport of different inositol epimers and derivatives across the plasma membrane.

Of the four genes of the Arabidopsis (Arabidopsis thaliana) INOSITOL TRANSPORTER family (AtINT family) so far only AtINT4 has been described. Here we present the characterization of AtINT2 and AtINT3. cDNA sequencing revealed that the AtINT3 gene is incorrectly spliced and encodes a truncated protein of only 182 amino acids with four transmembrane helices. In contrast, AtINT2 codes for a functional transporter. AtINT2 localization in the plasma membrane was demonstrated by transient expression of an AtINT2-GREEN FLUORESCENT PROTEIN fusion in Arabidopsis and tobacco (Nicotiana tabacum) epidermis cells and in Arabidopsis protoplasts. Its functional and kinetic properties were determined by expression in yeast (Saccharomyces cerevisiae) cells and Xenopus laevis oocytes. Expression of AtINT2 in a Deltaitr1 (inositol uptake)/Deltaino1 (inositol biosynthesis) double mutant of bakers' yeast complemented the deficiency of this mutant to grow on low concentrations of myoinositol. In oocytes, AtINT2 mediated the symport of H(+) and several inositol epimers, such as myoinositol, scylloinositol, d-chiroinositol, and mucoinositol. The preference for individual epimers differed from that found for AtINT4. Moreover, AtINT2 has a lower affinity for myoinositol (K(m) = 0.7-1.0 mm) than AtINT4 (K(m) = 0.24 mm), and the K(m) is slightly voltage dependent, which was not observed for AtINT4. Organ and tissue specificity of AtINT2 expression was analyzed in AtINT2 promoter/reporter gene plants and showed weak expression in the anther tapetum, the vasculature, and the leaf mesophyll. A T-DNA insertion line (Atint2.1) and an Atint2.1/Atint4.2 double mutant were analyzed under different growth conditions. The physiological roles of AtINT2 are discussed.

Laminin expression in juvenile angiofibroma indicates vessel's early developmental stage.

CONCLUSION: This study confirms the wide range of vascular architecture in juvenile angiofibromas. Proof of laminin alpha2 expression in tumour vessels is suggested to indicate presence of vessels of early developmental stage in juvenile angiofibromas, supporting the concept that plexus remnants of the first branchial arch artery contribute to the vascular tumour component. OBJECTIVES: Laminins, one of the major components of vascular wall basement membranes, have been implicated in tumour growth and have been shown to have developmentally regulated expression patterns. The goal of this study was to analyse the expression of laminins in juvenile angiofibromas. MATERIALS AND METHODS: A detailed analysis of the laminin isoform expression was performed by immunofluorescence staining for laminin chains alpha1, alpha2, alpha3, alpha4, alpha5, beta1, beta2, beta3, gamma1, gamma2, and gamma3 on cryosections of 10 juvenile angiofibromas and inferior nasal turbinate tissue for control. RESULTS: Vascular staining of the different laminin chains revealed areas of differential vessel density in juvenile angiofibromas and irregularities in vessel size, configuration and architecture. Similar to vessels in nasal turbinates, laminins alpha4, alpha5, beta1, beta2 and gamma1 were found to be expressed in juvenile angiofibroma vessels. In contrast to vessels of nasal turbinates, staining for alpha2 and alpha3 chains was only detected in vessels of juvenile angiofibromas.

Arabidopsis INOSITOL TRANSPORTER4 mediates high-affinity H+ symport of myoinositol across the plasma membrane.

Four genes of the Arabidopsis (Arabidopsis thaliana) monosaccharide transporter-like superfamily share significant homology with transporter genes previously identified in the common ice plant (Mesembryanthemum crystallinum), a model system for studies on salt tolerance of higher plants. These ice plant transporters had been discussed as tonoplast proteins catalyzing the inositol-dependent efflux of Na(+) ions from vacuoles. The subcellular localization and the physiological role of the homologous proteins in the glycophyte Arabidopsis were unclear. Here we describe Arabidopsis INOSITOL TRANSPORTER4 (AtINT4), the first member of this subgroup of Arabidopsis monosaccharide transporter-like transporters. Functional analyses of the protein in yeast (Saccharomyces cerevisiae) and Xenopus laevis oocytes characterize this protein as a highly specific H(+) symporter for myoinositol. These activities and analyses of the subcellular localization of an AtINT4 fusion protein in Arabidopsis and tobacco (Nicotiana tabacum) reveal that AtINT4 is located in the plasma membrane. AtINT4 promoter-reporter gene plants demonstrate that AtINT4 is strongly expressed in Arabidopsis pollen and phloem companion cells. The potential physiological role of AtINT4 is discussed.