RÉSUMÉ
Introduction: The domestic cat (Felis catus) is one of the most common pets. Worldwide, approximately one in five adults are sensitive to cat allergens. The major cat allergen is the secretoglobulin Fel d 1, which is primarily produced in the salivary and sebaceous glands. Chickens produce IgY antibodies, which are similar in structure to mammalian IgG. When chickens are exposed to Fel d 1, anti-Fel d 1-specific IgY (AFD1) is produced and is naturally concentrated in egg yolk. The aim of this study was to evaluate the tolerability, effects on growth and food consumption, and potential adverse effects of a chicken egg product ingredient containing AFD1 in kittens. Methods: This was a blinded, controlled study. Twenty-seven (27) eight-week old kittens were randomly assigned to three feeding groups containing 0 ppm AFD1 (Group 0), 8 ppm AFD1 (Group 1), and 16 ppm AFD1 (Group 2) for 84 days. Veterinary exams and bloodwork were performed on Day 42 and Day 84, and body weight and body condition score (BCS) were monitored weekly. Results: Throughout the study, there were no signs of nutritional deficiency or adverse clinical events in any of the subjects. Administration of a chicken egg product ingredient containing AFD1 in the diet (whether in coating or combination of coating and top dress) had no significant effect on body weight nor food consumption, and all subjects maintained a healthy Body Condition Score (BCS) throughout the study. Moreover, there were no biologically significant differences in the mean clinical chemistry and hematology parameters. Discussion: This study demonstrated that a diet formulated to contain up to 16 ppm AFD1, included in the coating and the top-dress of dry kitten food, was well tolerated, promoted adequate growth, and exhibited no adverse effects.
Sujet(s)
Maladies des chats , Maladies des chiens , Vieillissement , Animaux , Encéphale , Chats , Chiens , Besoins nutritifsRÉSUMÉ
Arabidopsis thaliana CARBOXYL-TERMINAL DOMAIN (CTD) PHOSPHATASE-LIKE 1 (CPL1) regulates plant transcriptional responses to diverse stress signals. Unlike typical CTD phosphatases, CPL1 contains two double-stranded (ds) RNA binding motifs (dsRBMs) at its C-terminus. Some dsRBMs can bind to dsRNA and/or other proteins, but the function of the CPL1 dsRBMs has remained obscure. Here, we report identification of REGULATOR OF CBF GENE EXPRESSION 3 (RCF3) as a CPL1-interacting protein. RCF3 co-purified with tandem-affinity-tagged CPL1 from cultured Arabidopsis cells and contains multiple K-homology (KH) domains, which were predicted to be important for binding to single-stranded DNA/RNA. Yeast two-hybrid, luciferase complementation imaging, and bimolecular fluorescence complementation analyses established that CPL1 and RCF3 strongly associate in vivo, an interaction mediated by the dsRBM1 of CPL1 and the KH3/KH4 domains of RCF3. Mapping of functional regions of CPL1 indicated that CPL1 in vivo function requires the dsRBM1, catalytic activity, and nuclear targeting of CPL1. Gene expression profiles of rcf3 and cpl1 mutants were similar during iron deficiency, but were distinct during the cold response. These results suggest that tethering CPL1 to RCF3 via dsRBM1 is part of the mechanism that confers specificity to CPL1-mediated transcriptional regulation.
Sujet(s)
Protéines d'Arabidopsis/métabolisme , Arabidopsis/physiologie , Phosphoprotein Phosphatases/métabolisme , Motifs et domaines d'intéraction protéique , Protéines de liaison à l'ARN/métabolisme , Transduction du signal , Stress physiologique , Facteurs de transcription/métabolisme , Séquence d'acides aminés , Protéines d'Arabidopsis/composition chimique , Protéines d'Arabidopsis/génétique , Sites de fixation , Domaine catalytique , Régulation de l'expression des gènes végétaux , Données de séquences moléculaires , Signaux de localisation nucléaire , Pression osmotique , Fragments peptidiques/composition chimique , Phosphoprotein Phosphatases/composition chimique , Phosphoprotein Phosphatases/génétique , Liaison aux protéines , Protéines de liaison à l'ARN/composition chimique , Protéines de liaison à l'ARN/génétique , Alignement de séquences , Facteurs de transcription/composition chimique , Facteurs de transcription/génétiqueRÉSUMÉ
OBJECTIVE: To evaluate the outcome of urinary bladder marsupialization in male goats. STUDY DESIGN: Prospective, experimental study. ANIMALS: Six healthy mixed-breed male goats. METHODS: After experimentally induced urethral obstruction, 6 male goats had urinary bladder marsupialization. Renal ultrasonography, complete blood count, and serum biochemical analysis were evaluated preoperatively (day 0), at 7 postoperative days, and then at 30-day intervals until 180 days. Stomal diameter was recorded immediately postoperatively and at each postoperative interval. Necropsy examination was performed on day 180 or when stomal stricture or death occurred. RESULTS: Stomal stricture occurred in 1 goat at 120 days. Another goat was found dead at 150 days; severe, suppurative cystitis was identified on necropsy. All goats had mild urine scald dermatitis. Serum biochemical values remained within normal limits, but significant decreases in white blood cell count, serum creatinine concentration, and stomal diameter occurred. At necropsy, all bladders were tubular in shape. Histological evidence of chronic suppurative cystitis and chronic, mild lymphoplasmacytic pyelitis occurred in all goats. Bacterial culture of renal tissue yielded growth in 3 goats, and bladder mucosal swabs yielded bacterial growth in all goats. CONCLUSIONS: Although clinical signs of ascending urinary tract infection were not observed in goats with patent stomata, urinary bladder marsupialization may result in ascending urinary tract inflammation or infection. CLINICAL RELEVANCE: Based on our results, urinary bladder marsupialization should be recommended with caution as the primary method for management of urinary tract obstruction in clinical cases.