bluuebunny/crossref_metadata_2025_split huggingface dataset:
Air filtration units in homes with cats: can they reduce personal exposure to cat allergen?
Authors: Gore R. B. , Bishop S. , Durrell B. , Curbishley L. , Woodcock A. , Custovic A. 
Published: June 2003

SummaryBackground Domestic air filtration units have previously been shown to cause a dramatic fall in airborne pet allergen levels in homes with pets. Clinical trials of air filtration units, however, have failed to reveal a significant beneficial effect. Personal pet allergen exposure during air filtration unit use has never been measured.Objective To determine the effect of air filtration on inhaled cat allergen exposure in homes with cats.Methods Nasal air samplers were worn to measure personal cat allergen exposure. The study was carried out in five homes with cats on 4 separate days examining four experimental conditions (cat absent or present, air filtration off or on). The two operators collected four baseline samples and two 15‐min samples/h over three consecutive hours. Cat allergen‐bearing particles were detected by immunoblotting and allergen concentrations measured by amplified enzyme‐linked immunosorbent assay (ELISA).Results There was a significant reduction in the quantity of the inhaled Fel d 1 when the air cleaner was used with the cat in the room. Fel d 1 halo counts (detransformed means) were 29.3 at baseline, 11.8 after 1 h, 10.0 after 2 h and 14.1 after 3 h, with no change on control days (P = 1.00). With the cat elsewhere in the house, a marginal, but statistically significant reduction was observed only after 3 h with the use of air cleaner (Fel d 1 halo count: baseline 12.4; 3 h 5.5; P = 0.01).Conclusions The use of air filtration units appears to result in a much smaller reduction of inhaled cat allergen exposure than suggested by previous studies using standard air samplers. Cat removal remains the best advice to cat‐allergic patients who experience symptoms upon exposure.
Identification of Cucumisin (Cuc m 1), a subtilisin‐like endopeptidase, as the major allergen of melon fruit
Authors: Cuesta‐Herranz J. , Pastor C. , Figueredo E. , Vidarte L. , De Las Heras M. , Durán C. , Fernández‐Caldas E. , De Miguel J. , Vivanco F. 
Published: June 2003

SummaryBackground Allergenic components in melon extracts have not been described in spite of the fact that melon (Cucumis melo) is a frequent allergy‐eliciting fruit. The aim of this study was to evaluate allergenic components in melon extract and to report the identification of cucumisin as a major melon allergen.Materials and methods Sera from 35 patients allergic to melon were selected on the basis of clinical symptoms, skin prick tests and oral challenge test. Allergenic components were detected by sodium dodecyl sulphate polyacrylamide gel electrophoresis and immunoblotting. Molecular characterization of IgE‐binding bands was performed by N‐terminal amino acid sequencing.Results More than 10 IgE‐binding bands, between 10 and 80 kDa, were identified in melon extract. Out of them, four IgE‐binding bands were major allergens: 14 kDa, 36 kDa, 54 kDa and 67 kDa. These major allergens, except 14 kDa band, showed the same N‐terminal sequence: T‐T‐R‐S‐W‐D‐F‐L. Research conducted with protein databases identified this N‐terminal sequence as cucumisin, an alkaline serine protease, which shares structural homology with microbial subtilisin. The molecular mass of the identified bands corresponds with different molecular forms of cucumisin produced during the processing or degradation of the enzyme: 67 kDa native cucumisin, 54 kDa mature cucumisin and 36 kDa NH2‐terminal cucumisin fragment.Conclusion Cucumisin (Cuc m 1) and several N‐terminal cucumisin fragments are the major allergens of melon. The ubiquitous distribution of this protein family (cucumisin‐like proteases) in many plant species and its high structural similarity suggest its potential role as a new panallergen in plant foods.
Inhibitory effects of interferon‐γ on the heterologous desensitization of β‐adrenoceptors by transforming growth factor‐β1 in tracheal smooth muscle
Authors: Ishikawa T. , Kume H. , Kondo M. , Ito Y. , Yamaki K. , Shimokata K. 
Published: June 2003

SummaryBackground Transforming growth factor‐β1 (TGF‐β1) is generally considered to play an important role in the pathogenesis of chronic inflammation and fibrosis.Objective and methods This study was designed to determine mechanisms of reduced responsiveness of guinea‐pig tracheal smooth muscle to β‐adrenoceptor agonists by TGF‐β1, using isometric tension records and tissue cAMP measurement. Moreover, we examined the involvement of the signal transduction processes of TGF‐β superfamily in the desensitization of β‐adrenoceptors.Results After exposure to 0.2–2000 pm TGF‐β1 for 4–8 h, the inhibitory effects of 1 µm isoprenaline (ISO) and 10 µm forskolin on 1 µm MCh‐induced contraction were markedly reduced in a concentration‐dependent fashion. The desensitization by TGF‐β1 was greater against ISO than for forskolin. The values of EC75 for the curves for ISO after exposure to the normal bathing solution and TGF‐β1 were 0.039 ± 0.02 and 0.38 ± 0.28 µm, respectively. The values of EC50 for the curves for forskolin under these conditions were 0.50 ± 0.12 and 0.89 ± 0.21 µm, respectively. On the other hand, the inhibitory effects of phosphodiesterase inhibitors such as theophylline and rolipram were not attenuated after exposure to TGF‐β1. Concentration–inhibition curve for ISO was shifted to the right after exposure to 2000 pm TGF‐β1 for 8 h more than that curve for forskolin. In contrast, the curve for theophylline was not shifted to the right by TGF‐β1. When the tissues were incubated with TGF‐β1 in the presence of IFN‐γ, an intracellular antagonist of TGF‐β signalling, IFN‐γ inhibited the reduced response to ISO and forskolin after exposure to TGF‐β1 in a concentration‐dependent fashion. After exposure to TGF‐β1, the effects of cAMP accumulation of ISO was significantly reduced, however, neither forskolin‐nor theophylline‐induced cAMP accumulation was affected. IFN‐γ had no significant effect on cAMP accumulation either to ISO or forskolin.Conclusions Impairment of the β‐adrenoceptors/adenylyl cyclase pathway are involved in heterologous desensitization of β‐adrenoceptors induced by TGF‐β1 in airway smooth muscle. IFN‐γ functionally suppresses this phenomenon via cAMP‐independent processes. Phosphodiesterase is still intact under this condition.
Effects of mediator antagonism on mannitol and adenosine monophosphate challenges
Authors: Currie G. P. , Haggart K. , Lee D. K. C. , Fowler S. J. , Wilson A. M. , Brannan J. D. , Anderson S. D. , Lipworth B. J. 
Published: June 2003

SummaryBackground Airway hyper‐responsiveness (AHR) to indirect stimuli is a useful non‐invasive surrogate inflammatory marker in the evaluation of asthma, while histamine and cysteinyl leukotrienes are important inflammatory mediators.Objective To evaluate AHR to indirect bronchoconstrictor stimuli and time taken to recover following single doses of montelukast 10 mg and desloratadine 5 mg in combination, montelukast 10 mg alone and placebo.Methods Fifteen mild‐to‐moderate persistent asthmatics completed a randomized, double‐blind, cross‐over study. Patients received encapsulated montelukast 10 mg/desloratadine 5 mg combination, montelukast 10 mg alone and placebo, 10–14 h prior to challenge on two separate occasions. The mannitol threshold dose, AMP threshold concentration and recovery times after challenge were measured along with lung function.Results Compared to placebo, montelukast/desloratadine conferred improvements (P < 0.05) in adenosine monophosphate (AMP) threshold concentration and mannitol threshold dose: a 3.2‐fold (95% CI 2.2–4.6) and 2.4‐fold (95% CI 1.7–3.3) difference, respectively, while compared to montelukast this amounted to a 2.0‐fold (95% CI 1.2–3.4) and 1.5‐fold (95% CI 1.1–2.4) improvement, respectively. Montelukast was not significantly different from placebo. Both montelukast/desloratadine and montelukast compared to placebo, shortened recovery following both challenges (P < 0.05): a 27‐min (95% CI 17–37) and 29‐min (95% CI 20–36) reduction, respectively, for AMP, and a 27‐min (95% CI 17–37) and 26‐min (95% CI 17–35) reduction, respectively for mannitol.Conclusion The dissociated effects of single doses of montelukast alone but not montelukast/desloratadine combination on AHR and recovery time, highlights the relative roles of histamine in initiating the bronchoconstrictor response and cysteinyl leukotrienes in sustaining it. Similar improvements in AHR and recovery time were observed following both indirect bronchoconstrictor stimuli.
Montelukast as an adjuvant to mainstay therapies in patients with seasonal allergic rhinitis
Authors: Topuz B. , Öǧmen G. G. 
Published: June 2003

SummaryBackground Drug selection for optimal treatment of allergic rhinitis may be difficult and involve many diverse factors.Objective To evaluate montelukast, in the treatment of patients with seasonal allergic rhinitis, as an adjuvant to mainstay therapies, i.e., antihistamines and corticosteroids.Methods The study was a prospective, three‐phased (per lasted 2 weeks) clinical trial. In phase I, patients were separated into two groups, based on the predominating symptoms: (1) runners (patients with moderate to severe sneezing/itchy, watery nose/itchy, watery eyes), and (2) blockers (patients with moderate to severe nasal congestion). The runners received antihistamine loratidine 10 mg daily, and the blockers received intranasal corticosteroid mometasone furoate 200 µg. In phase II, if patients were dissatisfied with the initial treatment, they were assigned to receive another study drug additionally. In phase III, for the patients unsatisfied with the treatment of loratidine plus mometasone furoate, montelukast 10 mg once daily was added.Results Of the 169 patients who entered phase I, 150 could be evaluated for treatment efficacy and safety. There were 108 runners and 42 blockers. Physicians' and patients' assessments indicated that in phase I 58 runners (60.0% of 50 runners) and 36 blockers (33.3% of six blockers) were satisfied with their therapy. In phase II, 30 runners (27.7%) and two blockers (4.7%) were satisfied with the addition of other study drug. Totally 62.6% of patients were satisfied at the end of phase I, and 84.0% at the end of phase II. Sixteen patients (66.6% of 24 patients) were satisfied with the addition of montelukast to the previous two drugs (in total, 10.6% of patients). Fourteen patients (12.2%) treated with loratadine, and three patients (0.3%) treated with mometasone, reported side‐effect.Conclusion The results of this trial indicate that 10% of patients with seasonal allergic rhinitis may be treated with the supplement of montelukast to mainstay therapy.
Suppression of fructokinase encoded by LeFRK2 in tomato stem inhibits growth and causes wilting of young leaves
Authors: German Marcelo A. , Dai Nir , Matsevitz Tanya , Hanael Rana , Petreikov Marina , Bernstein Nirit , Ioffe Marina , Shahak Yosepha , A. Schaffer Arthur ,   David Granot
Published: June 2003

SummaryFructokinases catalyze the key step of fructose phosphorylation in plants. LeFRK2, the major fructokinase‐encoding gene in tomato plants, is abundantly expressed in roots, stems, and fruits. To analyze the role of LeFRK2 in plant development, we analyzed transgenic tomato plants with sense and antisense expression of StFRK, the potato homolog of LeFRK2. Increased fructokinase activity had no effect. However, plants in which LeFRK2 was specifically suppressed, either via antisense suppression or via co‐suppression, exhibited growth inhibition and wilting of young leaves at daytime. Grafting experiments indicated that a stem interstock of antisense plants was sufficient to inhibit growth and cause leaf wilting. Stem secondary xylem exhibited particular suppression of LeFRK2 and the area of active xylem, estimated by eosin uptake, was significantly smaller in antisense stem compared to that of wild‐type plants. These results suggest that LeFRK2 might be required for proper development of xylem that affected growth and wilting.
The GA octodinucleotide repeat binding factor BBR participates in the transcriptional regulation of the homeobox gene Bkn3
Authors: Santi Luca , Wang Yamei , Stile Maria Rosaria , Berendzen Kenneth , Wanke Dierk , Roig Cristina , Pozzi Carlo , Müller Kai , Müller Judith , Rohde Wolfgang , Salamini Francesco 
Published: June 2003

SummaryIn the dominant mutant Hooded (K), the barley gene BKn3 is overexpressed as a result of a duplication of 305 bp in intron IV. When fused to a cauliflower mosaic virus 35S minimal promoter, the 305 bp element activates gene expression in tobacco, as does a 655 bp BKn3 promoter sequence. Both DNA fragments contain a (GA)8 repeat (GA/TC)8. A one‐hybrid screen using the 305 bp element as the DNA target led to the cloning of the barley b recombinant (BBR) protein, which binds specifically to the (GA/TC)8 repeat. BBR is nuclear targeted and is a characterized nuclear localization signal (NLS) sequence, a DNA‐binding domain extended up to 90 aa at the C‐terminus and a putative N‐terminal activation domain. The corresponding gene has no introns and is ubiquitously expressed in barley tissues. In co‐transfection experiments, BBR activates (GA/TC)8‐containing promoters, and its overexpression in tobacco leads to a pronounced leaf shape modification. BBR has properties of a GAGA‐binding factor, but the corresponding gene has no sequence homology to Trl and Psq of Drosophila, which encode functionally analogous proteins. In Arabidopsis, (GA/TC)8 repeats occur particularly within 1500 bp upstream of gene start codons included in some homeodomain genes of different classes. The data presented suggest that expression of the barley BKn3 is regulated, at least in part, by the binding of the transcription factor BBR to GA/TC repeats.
Protein interaction analysis of SCF ubiquitin E3 ligase subunits from Arabidopsis
Authors: Risseeuw Eddy P. , Daskalchuk Timothy E. , Banks Travis W. , Liu Enwu , Cotelesage Julian , Hellmann Hanjo , Estelle Mark , Somers David E. , Crosby William L. 
Published: June 2003

SummaryUbiquitin E3 ligases are a diverse family of protein complexes that mediate the ubiquitination and subsequent proteolytic turnover of proteins in a highly specific manner. Among the several classes of ubiquitin E3 ligases, the Skp1‐Cullin‐F‐box (SCF) class is generally comprised of three ‘core’ subunits: Skp1 and Cullin, plus at least one F‐box protein (FBP) subunit that imparts specificity for the ubiquitination of selected target proteins. Recent genetic and biochemical evidence in Arabidopsis thaliana suggests that post‐translational turnover of proteins mediated by SCF complexes is important for the regulation of diverse developmental and environmental response pathways. In this report, we extend upon a previous annotation of the Arabidopsis Skp1‐like (ASK) and FBP gene families to include the Cullin family of proteins. Analysis of the protein interaction profiles involving the products of all three gene families suggests a functional distinction between ASK proteins in that selected members of the protein family interact generally while others interact more specifically with members of the F‐box protein family. Analysis of the interaction of Cullins with FBPs indicates that CUL1 and CUL2, but not CUL3A, persist as components of selected SCF complexes, suggesting some degree of functional specialization for these proteins. Yeast two‐hybrid analyses also revealed binary protein interactions between selected members of the FBP family in Arabidopsis. These and related results are discussed in terms of their implications for subunit composition, stoichiometry and functional diversity of SCF complexes in Arabidopsis.
The Arabidopsis thaliana CUTA gene encodes an evolutionarily conserved copper binding chloroplast protein
Authors: Burkhead Jason L. , Abdel‐Ghany Salah E. , Morrill Jonathan M. , Pilon‐Smits Elizabeth A. H. , Pilon Marinus 
Published: June 2003

SummaryThe Arabidopsis thaliana CUTA gene encodes a 182‐amino‐acid‐long putative precursor of a chloroplast protein with high sequence similarity to evolutionarily conserved prokaryotic proteins implicated in copper tolerance. Northern analysis indicates that AtCUTA mRNA is expressed in all major tissue types. Analysis of cDNA clones and RT‐PCR with total mRNA revealed alternative splicing of AtCUTA by retention of an intron. The intron‐containing mRNA encodes a truncated 156‐amino‐acid protein as a result of stop codons in the included intron. The sequence of AtCutAp encoded by the fully spliced transcript suggests that the precursor consists of three domains: an N‐terminal chloroplast transit sequence of 70 residues, followed by a domain with prokaryotic signal‐sequence‐like characteristics and finally the most conserved C‐terminal domain. The N‐terminal chloroplast transit sequence was functional to route a passenger protein into isolated pea chloroplasts with possible sorting to the envelope. Chloroplast localization was confirmed by Western blot analysis of isolated and fractionated chloroplasts. Recombinant AtCutA protein was expressed in Escherichia coli without the N‐terminal 70‐amino‐acid chloroplast transit sequence. This recombinant AtCutAp was routed to the bacterial periplasm of E. coli. Purified recombinant AtCutAp is tetrameric and selectively binds Cu(II) ions with an affinity comparable to that reported for mammalian prion proteins.
A pea antisense gene for the chloroplast stromal processing peptidase yields seedling lethals in Arabidopsis: survivors show defective GFP import in vivo
Authors: Zhong Rong , Wan Jiangxin , Jin Rongguan , Lamppa Gayle 
Published: June 2003

SummaryThe stromal processing peptidase (SPP) of chloroplasts is a metalloendopeptidase that cleaves in vitro a broad range of precursor substrates. Here, we have investigated SPP's role in vivo. Two pea cDNA antisense constructs encoding either full‐length SPP (AS4.0) or its N‐terminal half (AS2.2) are introduced into Arabidopsis, which contains one gene for SPP that codes for one isoform. Our analyses show that AS4.0 produces a strong mutant phenotype, with a large percentage of the plants dying as seedling lethals. Surviving plants exhibited slower shoot and root growth, and grossly aberrant leaf morphology. Green and white sectoring, and purple pigmentation was observed. In cells where chloroplasts could be identified, they were fewer in number by at least 40%, thylakoids were not fully developed, and starch granules accumulated. The phenotype produced by AS2.2 was less severe. Using green fluorescent protein (GFP) fused to a transit peptide as a reporter, we examined import into chloroplasts in vivo. In the Arabidopsis antisense lines, GFP was located primarily in the cytosol, indicating that an early step in the import pathway was impeded. In a tobacco AS14 line expressing AS2.2, GFP was located in the cytosol, on the envelope, and in the stroma. The three patterns were observed in different cells, suggesting that the import capacity of individual cells was not the same. Our in vivo studies demonstrate that SPP is essential for chloroplast biogenesis and plant survival. SPP does not act independently in the stroma, but its activity influences earlier steps in the import pathway.
Monitoring expression profiles of Arabidopsis gene expression during rehydration process after dehydration using ca. 7000 full‐length cDNA microarray
Authors: Oono Youko , Seki Motoaki , Nanjo Tokihiko , Narusaka Mari , Fujita Miki , Satoh Rie , Satou Masakazu , Sakurai Tetsuya , Ishida Junko , Akiyama Kenji , Iida Kei , Maruyama Kyonoshin , Satoh Shinobu , Yamaguchi‐Shinozaki Kazuko , Shinozaki Kazuo 
Published: June 2003

SummaryPlants respond and adapt to drought stress in order to survive under stress conditions. Several genes that respond to drought at the transcriptional level have been described, but there are few reports on genes involved in the recovery from dehydration. Analysis of rehydration‐inducible genes should help not only to understand the molecular mechanisms of stress responses in higher plants, but also to improve the stress tolerance of crops by gene manipulation. We used a full‐length cDNA microarray containing ca. 7000 Arabidopsis full‐length cDNAs and identified 152 rehydration‐inducible genes. Venn diagram analysis showed relationship of the rehydration‐inducible genes to proline‐inducible and water‐treatment‐inducible genes. Among the 152 rehydration‐inducible genes, 58 genes contained the ACTCAT sequence involved in proline‐ and hypoosmolarity‐inducible gene expression in their promoter regions, suggesting that ACTCAT sequence is a major cis‐acting element involved in rehydration‐inducible gene expression, and that some novel cis‐acting elements are involved in rehydration‐inducible gene expression. Functional analysis of rehydration‐inducible and rehydration‐repressed genes revealed their functions not only in the release from a stressed status but also in the recovery of growth in plants.
Emerging role of calprotectin in gastroenterology
Authors: POULLIS ANDREW , FOSTER RUSSELL , MENDALL MICHAEL A , FAGERHOL MAGNE K 
Published: June 2003

Abstract  Calprotectin is a calcium and zinc binding protein of the S100 family derived predominantly from neutrophils and monocytes. It is detectable in body fluids and tissue samples and is emerging as a valuable marker in the diagnosis, and the monitoring and determining of the prognosis of commonly encountered gastroenterological conditions. Fecal calprotectin, in particular, has for a long time been regarded as a promising marker of gastrointestinal pathology and has now been established as a routine test in Norway and at several centers in the UK.© 2003 Blackwell Publishing Asia Pty Ltd
Alteration of aquaporin mRNA expression after small bowel resection in the rat residual ileum and colon
Authors: TSUJIKAWA TOMOYUKI , ITOH AKIHIKO , FUKUNAGA TETSUYA , SATOH JIN , YASUOKA TAKASHI , FUJIYAMA YOSHIHIDE 
Published: June 2003

AbstractBackground: Diarrhea occurring after small bowel resection gradually improves due to intestinal adaptation. It is known that several water channels, termed aquaporins (AQP), are expressed in the gastrointestinal tract and facilitate water transport. However, the changes of AQP after bowel resection remain unclear. In the present paper, the alterations in AQP mRNA expression were investigated after a massive small bowel resection in the rat residual ileum and colon.Methods: The 6‐week‐old male Sprague–Dawley rats (n = 15) underwent an 80% distal small bowel resection. The residual ileum and colon were dissected on postoperative day 1, 3, 5 or 7 (n= 3 on each day). Total RNA was purified from each mucosa, and the expressions of AQP and sodium‐dependent glucose transporter (SGLT1) mRNA were analyzed by northern blot. The plasma vasoactive intestinal polypeptide (VIP) concentrations on the preoperative day and postoperative day 1 were assayed.Results: In the residual small intestine, the expression of AQP‐1 and AQP‐3 mRNA increased significantly on postoperative day 1. The AQP‐7 mRNA increased on postoperative day 3, but the AQP‐4 mRNA did not change after the bowel resection. The SGLT1 mRNA gradually decreased after the bowel resection. In the colon, the expression of AQP‐3 increased on postoperative day 1 and 7, but AQP‐4 mRNA did not change after surgery. The AQP‐8 mRNA levels increased slightly on postoperative day 7. Plasma VIP concentration did not change between preoperative day and postoperative day 1.Conclusions: These results indicate that several AQP, except for AQP‐4, were up‐regulated after a massive small bowel resection, and that AQP might play important roles during adaptation.© 2003 Blackwell Publishing Asia Pty Ltd