A dusty torus around the luminous young star LkHa 101

A star forms when a cloud of dust and gas collapses. It is generally believed that this collapse first produces a flattened rotating disk, through which matter is fed onto the embryonic star at the center of the disk. When the temperature and density at the center of the star pass a critical threshold, thermonuclear fusion begins. The remaining disk, which can still contain up to 0.3 times the mass of the star, is then sculpted and eventually dissipated by the radiation and wind from the newborn star. Unfortunately this picture of the structure and evolution of the disk remains speculative because of the lack of morphological data of sufficient resolution and uncertainties regarding the underlying physical processes. Here we present resolved images of a young star, LkHa 101 in which the structure of the inner accretion disk is resolved. We find that the disk is almost face-on, with a central gap (or cavity) and a hot inner edge. The cavity is bigger than previous theoretical predictions, and we infer that the position of the inner edge is probably determined by sublimation of dust grains by direct stellar radiation, rather than by disk reprocessing or the viscous heating processes as usually assumed.Comment: 7 pages, 1 figure. Appears in Nature, 22 Feb, 2001 (Vol 409

Mechanical Strain Stabilizes Reconstituted Collagen Fibrils against Enzymatic Degradation by Mammalian Collagenase Matrix Metalloproteinase 8 (MMP-8)

Collagen, a triple-helical, self-organizing protein, is the predominant structural protein in mammals. It is found in bone, ligament, tendon, cartilage, intervertebral disc, skin, blood vessel, and cornea. We have recently postulated that fibrillar collagens (and their complementary enzymes) comprise the basis of a smart structural system which appears to support the retention of molecules in fibrils which are under tensile mechanical strain. The theory suggests that the mechanisms which drive the preferential accumulation of collagen in loaded tissue operate at the molecular level and are not solely cell-driven. The concept reduces control of matrix morphology to an interaction between molecules and the most relevant, physical, and persistent signal: mechanical strain.The investigation was carried out in an environmentally-controlled microbioreactor in which reconstituted type I collagen micronetworks were gently strained between micropipettes. The strained micronetworks were exposed to active matrix metalloproteinase 8 (MMP-8) and relative degradation rates for loaded and unloaded fibrils were tracked simultaneously using label-free differential interference contrast (DIC) imaging. It was found that applied tensile mechanical strain significantly increased degradation time of loaded fibrils compared to unloaded, paired controls. In many cases, strained fibrils were detectable long after unstrained fibrils were degraded.In this investigation we demonstrate for the first time that applied mechanical strain preferentially preserves collagen fibrils in the presence of a physiologically-important mammalian enzyme: MMP-8. These results have the potential to contribute to our understanding of many collagen matrix phenomena including development, adaptation, remodeling and disease. Additionally, tissue engineering could benefit from the ability to sculpt desired structures from physiologically compatible and mutable collagen