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- Abel, S. (1)
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- Cavalleri, J. M. V. (1)
- Cehak, A. (1)
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- Levy, M. (1)
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Krägeloh, T.; Cavalleri, J. M. V.; Ziegler, J.; Sander, J.; Terhardt, M.; Breves, G.; Cehak, A. Identification of hypoglycin A binding adsorbents as potential preventive measures in co-grazers of atypical myopathy affected horses Equine Vet J 50, 220-227, (2018) DOI: 10.1111/evj.12723
BackgroundIntestinal absorption of hypoglycin A
(HGA) and its metabolism are considered major prerequisites for atypical
myopathy (AM). The increasing incidence and the high mortality rate of
AM urgently necessitate new therapeutic and/or preventative
approaches.ObjectivesTo identify a substance for oral administration
capable of binding HGA in the intestinal lumen and effectively reducing
the intestinal absorption of the toxin.Study designExperimental in vitro
study.MethodsSubstances commonly used in equine practice (activated
charcoal composition, di‐tri‐octahedral smectite, mineral oil and
activated charcoal) were tested for their binding capacity for HGA using
an in vitro incubation method. The substance most effective in binding
HGA was subsequently tested for its potential to reduce intestinal HGA
absorption. Jejunal tissues of 6 horses were incubated in Ussing
chambers to determine mucosal uptake, tissue accumulation, and serosal
release of HGA in the presence and absence of the target substance.
Potential intestinal metabolism in methylenecyclopropyl acetic acid
(MCPA)‐conjugates was investigated by analysing their concentrations in
samples from the Ussing chambers.ResultsActivated charcoal composition
and activated charcoal were identified as potent HGA binding substances
with dose and pH dependent binding capacity. There was no evidence of
intestinal HGA metabolism.Main limitationsBinding capacity of adsorbents
was tested in vitro using aqueous solutions, and in vivo factors such
as transit time and composition of intestinal content, may affect
adsorption capacity after oral administration.ConclusionsFor the first
time, this study identifies substances capable of reducing HGA
intestinal absorption. This might have major implications as a
preventive measure in cograzers of AM affected horses but also in horses
at an early stage of intoxication.
Abel, S.; Savchenko, T.; Levy, M. Genome-wide comparative analysis of the <em>IQD</em> gene families in <em>Arabidopsis thaliana</em> and Oryza sativa BMC Evolutionary Biology 5, 72 (1-25), (2005)
We identified and analyzed 33 and 29 IQD1-like genes in Arabidopsis thaliana and Oryza sativa, respectively. The encoded IQD proteins contain a plant-specific domain of 67 conserved amino acid residues, referred to as the IQ67 domain, which is characterized by a unique and repetitive arrangement of three different calmodulin recruitment motifs, known as the IQ, 1-5-10, and 1-8-14 motifs. We demonstrated calmodulin binding for IQD20, the smallest IQD protein in Arabidopsis, which consists of a C-terminal IQ67 domain and a short N-terminal extension. A striking feature of IQD proteins is the high isoelectric point (~10.3) and frequency of serine residues (~11%). We compared the Arabidopsis and rice IQD gene families in terms of gene structure, chromosome location, predicted protein properties and motifs, phylogenetic relationships, and evolutionary history. The existence of an IQD-like gene in bryophytes suggests that IQD proteins are an ancient family of calmodulin-binding proteins and arose during the early evolution of land plants. Comparative phylogenetic analyses indicate that the major IQD gene lineages originated before the monocot-eudicot divergence. The extant IQD loci in Arabidopsis primarily resulted from segmental duplication and reflect preferential retention of paralogous genes, which is characteristic for proteins with regulatory functions. Interaction of IQD1 and IQD20 with calmodulin and the presence of predicted calmodulin binding sites in all IQD family members suggest that IQD proteins are a new class of calmodulin targets. The basic isoelectric point of IQD proteins and their frequently predicted nuclear localization suggest that IQD proteins link calcium signaling pathways to the regulation of gene expression. Our comparative genomics analysis of IQD genes and encoded proteins in two model plant species provides the first step towards the functional dissection of this emerging family of putative calmodulin targets.