Abstract-Adipose tissue depots originate from distinct precursor cells, are functionally diverse, and modulate disease processes in a depot-specific manner. However, the functional properties of perivascular adipocytes, and their influence on disease of the blood vessel wall, remain to be determined. We show that human coronary perivascular adipocytes exhibit a reduced state of adipocytic differentiation as compared with adipocytes derived from subcutaneous and visceral (perirenal) adipose depots. Secretion of antiinflammatory adiponectin is markedly reduced, whereas that of proinflammatory cytokines interleukin-6, interleukin-8, and monocyte chemoattractant protein-1, is markedly increased in perivascular adipocytes. These depot-specific differences in adipocyte function are demonstrable in both freshly isolated adipose tissues and in vitro-differentiated adipocytes. Murine aortic arch perivascular adipose tissues likewise express lower levels of adipocyte-associated genes as compared with subcutaneous and visceral adipose tissues. Moreover, 2 weeks of high-fat feeding caused further reductions in adipocyte-associated gene expression, while upregulating proinflammatory gene expression, in perivascular adipose tissues. These changes were observed in the absence of macrophage recruitment to the perivascular adipose depot. We conclude that perivascular adipocytes exhibit reduced differentiation and a heightened proinflammatory state, properties that are intrinsic to the adipocytes residing in this depot.

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The cellular cues that guide neuronal growth cones toward their targets are highly conserved in such diverse organisms as insects and vertebrates. Evidence presented here suggests that the molecular mechanisms underlying these events may be equally conserved. This article describes the structure and function of fasciclin II, a glycoprotein expressed on a subset of fasciculating axons in the grasshopper embryo. Antibody perturbation experiments suggest that fasciclin II functions in mediating one form of neuronal recognition: selective fasciculation. Fasciclin II is a member of the immunoglobulin gene superfamily and is homologous in structure and function to the neural cell adhesion molecule N-CAM and to several other vertebrate cell adhesion molecules.