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Goldman, A. I. (1967). A Causal Theory of Knowing. The Journal of Philosophy, 64(12), 357–372.
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Crosby, M. B., Svenson, J. L., Zhang, J., Nicol, C. J., Gonzalez, F. J., & Gilkeson, G. S. (2005). Peroxisome proliferation-activated receptor (PPAR)gamma is not necessary for synthetic PPARgamma agonist inhibition of inducible nitric-oxide synthase and nitric oxide. J Pharmacol Exp Ther, 312(1), 69–76.
Abstract: Peroxisome proliferation-activated receptor (PPAR)gamma agonists inhibit inducible nitric-oxide synthase (iNOS), tumor necrosis factor-alpha, and interleukin-6. Because of these effects, synthetic PPARgamma agonists, including thiazolidinediones, are being studied for their impact on inflammatory disease. The anti-inflammatory concentrations of synthetic PPARgamma agonists range from 10 to 50 microM, whereas their binding affinity for PPARgamma is in the nanomolar range. The specificity of synthetic PPARgamma agonists for PPARgamma at the concentrations necessary for anti-inflammatory effects is thus in question. We report that PPARgamma is not necessary for the inhibition of iNOS by synthetic PPARgamma agonists. RAW 264.7 macrophages possess little PPARgamma, yet lipopolysaccharide (LPS)/interferon (IFN)gamma-induced iNOS was inhibited by synthetic PPARgamma agonists at 20 microM. Endogenous PPARgamma was inhibited by the transfection of a dominant-negative PPARgamma construct into murine mesangial cells. In the transfected cells, synthetic PPARgamma agonists inhibited iNOS production at 10 microM, similar to nontransfected cells. Using cells from PPARgamma Cre/lox conditional knockout mice, baseline and LPS/IFNgamma-induced nitric oxide levels were higher in macrophages lacking PPARgamma versus controls. However, synthetic PPARgamma agonists inhibited iNOS at 10 microM in the PPARgamma-deficient cells, similar to macrophages from wild-type mice. These results indicate that PPARgamma is not necessary for inhibition of iNOS expression by synthetic PPARgamma agonists at concentrations over 10 microM. Intrinsic PPARgamma function, in the absence of synthetic agonists, however, may play a role in inflammatory modulation.
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Wilhelm, W. E., & Anderson, J. H. (1971). Vahlkampfia lobospinosa (Craig. 1912) Craig. 1913: rediscovery of a coprozoic ameba. J Parasitol, 57(6), 1378–1379.
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Walker, M. L., & Becklund, W. W. (1971). Occurrence of a cattle eyeworm, Thelazia gulosa (Nematoda: Thelaziidae), in an imported giraffe in California and T. lacrymalis in a native horse in Maryland. J Parasitol, 57(6), 1362–1363.
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Malek, E. A. (1971). The life cycle of Gastrodiscus aegyptiacus (Cobbold, 1876) Looss, 1896 (Trematoda: Paramphistomatidae: Gastrodiscinae). J Parasitol, 57(5), 975–979.
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Hoogstraal, H., & Mitchell, R. M. (1971). Haemaphysalis (Alloceraea) aponommoides Warburton (Ixodoidea: Ixodidae), description of immature stages, hosts, distribution, and ecology in India, Nepal, Sikkim, and China. J Parasitol, 57(3), 635–645.
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Hoogstraal, H., Dhanda, V., & Bhat, H. R. (1970). Haemaphysalis (Kaiseriana) davisi sp. n. (Ixodoidea: Ixodidae), a parasite of domestic and wild mammals in Northeastern India, Sikkim, and Burma. J Parasitol, 56(3), 588–595.
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Dierenfeld, E. S. (1994). Vitamin E in exotics: effects, evaluation and ecology. J Nutr, 124(12 Suppl), 2579s–2581s.
Abstract: The pathophysiology and lesions associated with vitamin E deficiency are similar between domestic and exotic species, and circulating plasma concentrations are also similar between comparable groups. However, many ecological variables must be considered for the most relevant comparisons. Tissue values of vitamin E, apart from plasma, are unknown for most exotics. Dietary vitamin E requirements of exotic species and domestics appear to differ; based on natural foodstuff analyses and clinical observations, between 50 and 200 mg vitamin E/kg DM are necessary to prevent vitamin E deficiency, 5- to 10-fold higher than current livestock recommendations.
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Tang, A. C., Reeb, B. C., Romeo, R. D., & McEwen, B. S. (2003). Modification of Social Memory, Hypothalamic-Pituitary-Adrenal Axis, and Brain Asymmetry by Neonatal Novelty Exposure. The Journal of Neuroscience, 23(23), 8254–8260.
Abstract: Although corticosterone (a stress hormone) is known to influence social behavior and memory processes, little has been explored concerning its modulatory role in social recognition. In rats, social recognition memory for conspecifics typically lasts <2 hr when evaluated using a habituation paradigm. Using neonatal novelty exposure, a brief and transient early life stimulation method known to produce long-lasting changes in the hypothalamic-pituitary-adrenal axis, we found that social recognition memory was prolonged to at least 24 hr during adulthood. This prolonged social memory was paralleled by a reduction in the basal blood concentration of corticosterone. The same neonatal stimulation also resulted in a functional asymmetry expressed as a greater right-turn preference in a novel environment. Rats that preferred to turn right showed better social recognition memory. These inter-related changes in basal blood corticosterone concentration, turning asymmetry, and social recognition memory suggest that stress hormones and brain asymmetry are likely candidates for modulating social memory. Furthermore, given that neonatal stimulation has been shown to improve learning and memory performance primarily under aversive learning situations, the neonatal novelty exposure-induced enhancement in social recognition broadens the impact of early life stimulation to include the social domain.
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Hieshima, K., Kawasaki, Y., Hanamoto, H., Nakayama, T., Nagakubo, D., Kanamaru, A., et al. (2004). CC Chemokine Ligands 25 and 28 Play Essential Roles in Intestinal Extravasation of IgA Antibody-Secreting Cells. The Journal of Immunology, 173(6), 3668–3675.
Abstract: CCL25 (also known as thymus-expressed chemokine) and CCL28 (also known as mucosae-associated epithelial chemokine) play important roles in mucosal immunity by recruiting IgA Ab-secreting cells (ASCs) into mucosal lamina propria. However, their exact roles in vivo still remain to be defined. In this study, we first demonstrated in mice that IgA ASCs in small intestine expressed CCR9, CCR10, and CXCR4 on the cell surface and migrated to their respective ligands CCL25, CCL28, and CXCL12 (also known as stromal cell-derived factor 1), whereas IgA ASCs in colon mainly expressed CCR10 and CXCR4 and migrated to CCL28 and CXCL12. Reciprocally, the epithelial cells of small intestine were immunologically positive for CCL25 and CCL28, whereas those of colon were positive for CCL28 and CXCL12. Furthermore, the venular endothelial cells in small intestine were positive for CCL25 and CCL28, whereas those in colon were positive for CCL28, suggesting their direct roles in extravasation of IgA ASCs. Consistently, in mice orally immunized with cholera toxin (CT), anti-CCL25 suppressed homing of CT-specific IgA ASCs into small intestine, whereas anti-CCL28 suppressed homing of CT-specific IgA ASCs into both small intestine and colon. Reciprocally, CT-specific ASCs and IgA titers in the blood were increased in mice treated with anti-CCL25 or anti-CCL28. Anti-CXCL12 had no such effects. Finally, both CCL25 and CCL28 were capable of enhancing α4 integrin-dependent adhesion of IgA ASCs to mucosal addressin cell adhesion molecule-1 and VCAM-1. Collectively, CCL25 and CCL28 play essential roles in intestinal homing of IgA ASCs primarily by mediating their extravasation into intestinal lamina propria.
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