12 research outputs found
Correlations between body weight, visceral fat, parameters of glucose homeostasis and lipid profile.
<p>Significant correlations are shown in bold with *, ** and *** indicating a P-value of <.05, <.01 and <.001 respectively, n = 12 per group.</p
Effects of diet and gender on spatial and non-spatial escape strategies during the MWM test.
<p>(A) Orientation of entry point and escape platform on trial days 1–4. Arrows indicate location of entry point. (B) Distribution of search strategies in aspartame-fed mice compared to controls on trial days 1–4. As the acquisition training advanced, control C57BL/6J mice exhibited progressive behavioral changes from random chaining, thigmotaxis and floating into predominantly spatial strategies such as direct swim and direct search. Mice in the aspartame group exhibited less spatial strategies and more non-spatial behavior throughout the trials.</p
Results from a probe trial intended to measure spatial memory.
<p>Percentage of time spent searching in the former location of the platform (Target Quad) in (A) males and (B) females, compared to time spent in the adjacent quads. Aspartame-fed males showed a reduction in the number of times they crossed over former location of the platform (C: Platform Crossings and (E: Annulus Crossing Index), n = 12 per group, * P<0.05, ** P<0.01, *** P<0.001. There was no significance in the reduction of platform crossings and Annulus Crossing Index in females. Actual overlapping swim paths of the control (G,I) and aspartame-fed mice (H,J). Swim paths illustrate less intense swimming in the location of the platform by aspartame-fed mice, compared to controls.</p
Effect of aspartame consumption on weight gain, adiposity, glucose homeostasis and lipid profile.
<p>BW, Body Weight; RW, Relative weight.</p><p>Data presented are means ± SEM, n = 12 per group. P-value <.05 and < 0.01 based on t-test comparisons of diet groups within sexes are indicated by * and **; and comparison of sexes by § and §§ respectively.</p
Aspartame consumption reduces insulin sensitivity of male C57BL/6J mice during a random-fed insulin tolerance test.
<p>Values are mean±SEM of (A) male glucose levels and (B) female glucose levels, n = 18 per group, *** P<0.001 compared to controls.</p
Effect of aspartame consumption on spatial learning in C57BL/6J mice: gender-specific differences.
<p>Acquisition curves of escape latency in male (A) and female (B) aspartame-fed and control diet mice. Percentage time spent in target quad in male (C) and female (D) mice. Mean Distance to goal in male (E) and female (F) mice. Each group consisted of 12 mice; * P<0.05, ** P<0.01, *** P<0.001.</p
Summary of correlation analysis between body characteristics and spatial memory variables in the MWM test.
<p>Significant correlations are shown in bold with *, ** and *** indicating a P-value of ≤.05, ≤.01 and ≤.001 respectively, n = 12 per group</p
Effects of aspartame consumption on non-cognitive behavior.
<p>Percentage of time spent floating in male (A) and female (B) aspartame-fed and control diet mice. Thigmotaxis in male (C) and female (D) mice, n = 12 per group; * P<0.05, ** P<0.01, *** P<0.001.</p
DataSheet_1_The immunoglobulin A isotype of the Arabian camel (Camelus dromedarius) preserves the dualistic structure of unconventional single-domain and canonical heavy chains.docx
IntroductionThe evolution of adaptive immunity in Camelidae resulted in the concurrent expression of classic heterotetrameric and unconventional homodimeric heavy chain-only IgG antibodies. Heavy chain-only IgG bears a single variable domain and lacks the constant heavy (CH) γ1 domain required for pairing with the light chain. It has not been reported whether this distinctive feature of IgG is also observed in the IgA isotype. MethodsGene-specific primers were used to generate an IgA heavy chain cDNA library derived from RNA extracted from the dromedary’s third eyelid where isolated lymphoid follicles and plasma cells abound at inductive and effector sites, respectively. ResultsMajority of the cDNA clones revealed hallmarks of heavy chain-only antibodies, i.e. camelid-specific amino acid substitutions in framework region 1 and 2, broad length distribution of complementarity determining region 3, and the absence of the CHα1 domain. In a few clones, however, the cDNA of the canonical IgA heavy chain was amplified which included the CHα1 domain, analogous to CHγ1 domain in IgG1 subclass. Moreover, we noticed a short, proline-rich hinge, and, at the N-terminal end of the CHα3 domain, a unique, camelid-specific pentapeptide of undetermined function, designated as the inter-α region. Immunoblots using rabbit anti-camel IgA antibodies raised against CHα2 and CHα3 domains as well as the inter-α region revealed the expression of a ~52 kDa and a ~60 kDa IgA species, corresponding to unconventional and canonical IgA heavy chain, respectively, in the third eyelid, trachea, small and large intestine. In contrast, the leporine anti-CHα1 antibody detected canonical, but not unconventional IgA heavy chain, in all the examined tissues, milk, and serum, in addition to another hitherto unexplored species of ~45 kDa in milk and serum. Immunohistology using anti-CHα domain antibodies confirmed the expression of both variants of IgA heavy chains in plasma cells in the third eyelid’s lacrimal gland, conjunctiva, tracheal and intestinal mucosa. ConclusionWe found that in the dromedary, the IgA isotype has expanded the immunoglobulin repertoire by co-expressing unconventional and canonical IgA heavy chains, comparable to the IgG class, thus underscoring the crucial role of heavy chain-only antibodies not only in circulation but also at the mucosal frontiers.</p
Image_1_The immunoglobulin A isotype of the Arabian camel (Camelus dromedarius) preserves the dualistic structure of unconventional single-domain and canonical heavy chains.tiff
IntroductionThe evolution of adaptive immunity in Camelidae resulted in the concurrent expression of classic heterotetrameric and unconventional homodimeric heavy chain-only IgG antibodies. Heavy chain-only IgG bears a single variable domain and lacks the constant heavy (CH) γ1 domain required for pairing with the light chain. It has not been reported whether this distinctive feature of IgG is also observed in the IgA isotype. MethodsGene-specific primers were used to generate an IgA heavy chain cDNA library derived from RNA extracted from the dromedary’s third eyelid where isolated lymphoid follicles and plasma cells abound at inductive and effector sites, respectively. ResultsMajority of the cDNA clones revealed hallmarks of heavy chain-only antibodies, i.e. camelid-specific amino acid substitutions in framework region 1 and 2, broad length distribution of complementarity determining region 3, and the absence of the CHα1 domain. In a few clones, however, the cDNA of the canonical IgA heavy chain was amplified which included the CHα1 domain, analogous to CHγ1 domain in IgG1 subclass. Moreover, we noticed a short, proline-rich hinge, and, at the N-terminal end of the CHα3 domain, a unique, camelid-specific pentapeptide of undetermined function, designated as the inter-α region. Immunoblots using rabbit anti-camel IgA antibodies raised against CHα2 and CHα3 domains as well as the inter-α region revealed the expression of a ~52 kDa and a ~60 kDa IgA species, corresponding to unconventional and canonical IgA heavy chain, respectively, in the third eyelid, trachea, small and large intestine. In contrast, the leporine anti-CHα1 antibody detected canonical, but not unconventional IgA heavy chain, in all the examined tissues, milk, and serum, in addition to another hitherto unexplored species of ~45 kDa in milk and serum. Immunohistology using anti-CHα domain antibodies confirmed the expression of both variants of IgA heavy chains in plasma cells in the third eyelid’s lacrimal gland, conjunctiva, tracheal and intestinal mucosa. ConclusionWe found that in the dromedary, the IgA isotype has expanded the immunoglobulin repertoire by co-expressing unconventional and canonical IgA heavy chains, comparable to the IgG class, thus underscoring the crucial role of heavy chain-only antibodies not only in circulation but also at the mucosal frontiers.</p