Thesis (Ph. D.)--Case Western Reserve University, 2008. / [School of Medicine] Department of Neurosciences. Includes bibliographical references.

Thesis (Ph. D.)--University of Hong Kong, 1997. / Includes bibliographical references (leaf 155-192).

Thesis (M.S.)--University of Delaware, 2006. / Principal faculty advisor: David C. Usher, Dept. of Biological Sciences. Includes bibliographical references.

Thesis (Ph. D.)--University of Chicago, Committee on Human Nutrition and Nutritional Biology, March 2001. / Includes bibliographical references. Also available on the Internet.

OBJECTIVE—Absence of stearoyl-CoA desaturase-1 (SCD1) in mice reduces plasma triglycerides and provides protection from obesity and insulin resistance, which would be predicted to be associated with reduced susceptibility to atherosclerosis. The aim of this study was to determine the effect of SCD1 deficiency on atherosclerosis. Methods and RESULTS—Despite an antiatherogenic metabolic profile, SCD1 deficiency increases atherosclerosis in hyperlipidemic low density lipoprotein receptor (LDLR)-deficient mice challenged with a western diet. Lesion area at the aortic root is significantly increased in males and females in two models of SCD1 deficiency. Inflammatory changes are evident in the skin of these mice, including increased intercellular adhesion molecule (ICAM)-1 and ulcerative dermatitis. Increases in ICAM-1 and interleukin-6 are also evident in plasma of SCD1-deficient mice. HDL particles demonstrate changes associated with inflammation, including, decreased plasma apoA-II and apoA-I and paraoxonase-1 and increased plasma serum amyloid A. Lipopolysaccharide-induced inflammatory response and cholesterol efflux are not altered in SCD1-deficient macrophages. In addition, when SCD1 deficiency is limited to bone-marrow derived cells, lesion size is not altered in LDLR-deficient mice. CONCLUSIONS—These studies reinforce the crucial role of chronic inflammation in promoting atherosclerosis, even in the presence of antiatherogenic biochemical and metabolic characteristics. [The original version of this article, along with updated information and services is located on the World Wide Web at: http://atvb.ahajournals.org/cgi/content/full/29/3/341] [UBC users: please click on the UBC eLink icon at the bottom of this record]

Thesis (M.Sc.) - University of Queensland, 2005. / Includes bibliography.

Thesis (Ph. D.)--Oregon State University, 2007. / Printout. Includes bibliographical references (leaves 67-74). Also available on the World Wide Web.

No description available.

Thesis (Ph. D.)Open University. BLDSC no. DXN036583.

Apolipophorin-III (apoLp-III) is known to influence the haemocyte-mediated induction of antimicrobial peptides in Galleria mellonella and yeast phagocytosis, bind to Gram-negative and Gram positive bacteria and limit the activation of the haemocytes and the prophenoloxidase system by bacterial surface antigens. The effects of apoLp-III on haemocyte adhesion to glass slides and to bacteria were herein examined. ApoLp-III bound to haemocytes limiting the adhesion of both granular cells and plasmatocytes to glass and the contact of the plasmatocytes with Bacillus subtilis. The percentage of granular cells with bacteria was increased by the protein. However, the total number of bacteria adhering to haemocytes in vitro declined in the presence of apoLp-III. Bacterial removal from the haemolymph in vivo by the haemocytes was slowed by the protein. / The adhesion of both the granular cells and plasmatocytes to slides was decreased by inhibiting protein tyrosine kinase and increased by inhibiting protein kinase A (PKA) and protein kinase C (PKC) activity. The latter was confirmed with haemocytes inhibited by the general PKC inhibitor H-7 using phorbol-3-myfstate (PMA) which, by activating PKC, diminished the adhesion of both haemocyte types. Limiting the formation of PKC activation by diacylglycerides which is produced by phosholipase C (PLC), using PLC inhibitor also increased haemocyte attachment. Although binding of B. subtilis to haemocytes decreased PKC activity, the effect of apoLp-III on PKC was inconclusive.