Structure and variability in human tongue muscle anatomy.

The human tongue has a complex architecture, consistent with its complex roles in eating, speaking and breathing. Tongue muscle architecture has been depicted in drawings and photographs, but not quantified volumetrically. This paper aims to fill that gap by measuring the muscle architecture of the tongue for 14 people captured in high-resolution 3D MRI volumes. The results show the structure, relationships and variability among the muscles, as well as the effects of age, gender and weight on muscle volume. Since the tongue consists of partially interdigitated muscles, we consider the muscle volumes in two ways. The functional muscle volume encompasses the region of the tongue served by the muscle. The structural volume halves the volume of the muscle in regions where it interdigitates with other muscles. Results show similarity of scaling across subjects, and speculate on functional effects of the anatomical structure.

Pro-thrombotic state induced by post-translational modification of fibrinogen by reactive nitrogen species.

Formation of nitric oxide-derived oxidants has been linked to development of atherosclerosis and associated thrombotic complications. Although systemic levels of protein nitrotyrosine predict risk for coronary artery disease, neither specific proteins targeted for modification nor functional consequences that might contribute to disease pathogenesis have been defined. Here we report a selective increase in circulating levels of nitrated fibrinogen in patients with coronary artery disease. Exposure of fibrinogen to nitrating oxidants, including those produced by the myeloperoxidase-hydrogen peroxide-nitrite system, significantly accelerates clot formation and factor XIII cross-linking, whereas exposure of fibrinogen to non-nitrating oxidants decelerates clot formation. Clots formed with fibrinogen exposed to nitrating oxidants are composed of large bundles made from twisted thin fibrin fibers with increased permeation and a decrease in storage modulus G' value, suggesting that these clots could be easily deformed by mechanical stresses. In contrast, clots formed with fibrinogen exposed to non-nitrating oxidants showed decreased permeation with normal architecture. Fibrinogen modified by exposure to physiologic nitration systems demonstrated no difference in the rate of plasmin-induced clot lysis, platelet aggregation, or binding. Thus, increased levels of fibrinogen nitration may lead to a pro-thrombotic state via acceleration in formation of fibrin clots. The present results may account, in part, for the association between nitrative stress and risk for coronary artery disease.