Revolving around two members of a high school synchronized naiant team and their relationship with a petite, singular girl, Celine Sciamma's seductive first feature film, Water Lilies, unveils its reminiscent fever-dream in the Parisian suburb of Cergy. At the late New Directors/New Films Festival in NY, Sciamma's puerile enigma was an inarguable highlight among some very strong competition.
It's after a demonstration of Anne and Floriane's submerged coordination, in a locker room, that Fran�ois (Warren Jacquin) encounters a completely nude Anne (Louise Blachere). Anne's frumpish body doesn't excite Fran�ois, but the teenage girl is left exhilarated by the exhibitionistic thrill in any event. Outside the school, Floriane (Adele Haenel), the naiant team's siren, agrees to allow the skinny, nymph-like Marie (an astounding Pauline Acquart) into the consortium area side by side time they practice, in exchange for a forthcoming favor.
The favour asked is to be a lookout of sorts for Floriane as she runs off with Fran�ois. The beauty's inability to go all the way with Fran�ois becomes a point of intrigue both for herself and Marie, who begins harboring a romance for Floriane. Meanwhile, Anne daydreams of Fran�ois deflowering her, going as far as to stand naked, eyes shut, in the locker room for the lean stud to discover her again. As Marie's toying with Floriane becomes a mutual affair, the stress between her and the insufferable histrionics of Anne's crush tighten like a vice, especially when Fran�ois makes a house visit to Anne.
Things get preferably randy, only the enticement of Sciamma's film is considerably proper. At a club, the fumblings of an initial kiss between Floriane and Marie fluidly mutates into Floriane terpsichore with an older
Saturday 30 August 2008
Water Lilies
Sunday 10 August 2008
Iron Metabolism Research Yields New Tool In Diagnosing Anemia Of Chronic Disease
�University of Utah School of Medicine researchers let developed a new tool that facilitates diagnosis of anemia related to chronic illness, as well as diseases of iron overload. The results of a study particularisation the young tool ar published in the August 2008 take of the journal Cell Metabolism, a publication of Cell Press.
Iron balance in the body is regulated by the interaction between a liver-produced hormone called hepcidin and the iron transporting receptor ferroportin. Hepcidin binds to ferroportin resulting in reduced export of iron out of cells. An overindulgence of hepcidin in the blood can result in anemia and a deficiency of hepcidin causes a build-up of iron that is damaging to body organs.
Since both anemia and iron surcharge have versatile causes, it is often difficult to distinguish among those causes. "It is hard to diagnose the anemia of chronic disease," said senior author Jerry Kaplan, Ph.D., University of Utah professor of pathology and assistant vice president of the United States for enquiry at the University of Utah Health Sciences. "Having an assay for hepcidin would make it a great deal easier and it would also help in diagnosis iron overload diseases."
Identification of the Hepcidin-Binding Domain
In the study, Kaplan and researchers from the University of Utah and University of California, Los Angeles report that they have identified the hepcidin-binding domain (HBD), the specific site where hepcidin binds to ferroportin. By placing a synthetic version of that binding site on agarose beads, the researchers developed a rapid, sensitive test, called the HBD assay, for measuring the concentration of active hepcidin in the blood.
The ability to observe and touchstone hepcidin has important implications for the diagnosis of anemias and iron clog disorders related to hepcidin. Anemia is a want of the oxygen-carrying molecules inside bolshie blood cells which commode be caused by smoothing iron deficiency, vitamin B12 or folate deficiency, or chronic illnesses. Anemia of chronic disease, or anemia of inflammation, is a shape of anemia that is thought to be related to abnormally high levels of hepcidin.
The most vulgar human upset of fe overload is hereditary bronzed diabetes, which leads to abnormal accumulation of iron in the liver, heart, skin, and other organs. Some types of hereditary hemochromatosis are associated with inappropriately low levels of hepcidin in the blood.
The HBD assay developed by Kaplan and his colleagues detects biologically active hepcidin. This assay commode readily notice variations in hepcidin levels in the blood due to mutations in genes that are known to affect hepcidin levels, as well as mutations in other genes involved in iron metamorphosis. It can also measure hepcidin assiduity in response to rubor. This novel test would allow doctors to severalise anemias and diseases of iron metabolism that arise from abnormalities in hepcidin from those that accept other causes.
Hepcidin was low reported for its purpose in the body's defense Department against bacterial and fungal infections. Current scientific evidence, however, suggests that hepcidin's primary use in the body is to shape iron balance.
Kaplan and his colleagues establish that even very minor changes to the composing of the HBD had significant personal effects on the ability of the binding site to bind hepcidin. They besides discovered that hepcidin's ability to bandage to the HBD decreases at temperatures below the normal human body temperature of 37�C due to structural changes in the hepcidin molecule at depress temperatures. This change in structure besides affected the ability of hepcidin to bind to bacteria. This raised questions about the effect of low temperatures on smoothing iron metabolism and antibacterial activity.
Evolutionary Insight
The hepcidin-binding domain of fish is nearly identical to the human HBD. The researchers looked at hepcidin in fish such as the brown trout from the Middle Provo River, which routinely live in very cold amnionic fluid. Most mammals have only when one hepcidin gene, only fish throw multiple hepcidin genes that encode hepcidin molecules of different lengths. In this study, Kaplan and his colleagues institute that the fish hepcidin which is the same length as human hepcidin was able to bandage to the HBD at temperatures as low as 4�C merely had very little antibacterial activity at both 4�C and 37�C. This discovery provides insight into the evolution of hepcidin among vertebrates. Human hepcidin has both iron and bacteria-related activities, piece fish hepcidin genes evolved to separate these functions.
Due to the similarity of the hepcidin binding land site among vertebrates, the usefulness of the novel HBD assay described in this study is not limited to humanity. "The check can be used to easily step hepcidin in the rakehell of all vertebrates," says Kaplan.
University of Utah Health Sciences
420 Chipeta Way, Ste. 1900
Salt Lake City, UT 84108
United States
http://healthcare.utah.edu/index.cfm
More info
Iron balance in the body is regulated by the interaction between a liver-produced hormone called hepcidin and the iron transporting receptor ferroportin. Hepcidin binds to ferroportin resulting in reduced export of iron out of cells. An overindulgence of hepcidin in the blood can result in anemia and a deficiency of hepcidin causes a build-up of iron that is damaging to body organs.
Since both anemia and iron surcharge have versatile causes, it is often difficult to distinguish among those causes. "It is hard to diagnose the anemia of chronic disease," said senior author Jerry Kaplan, Ph.D., University of Utah professor of pathology and assistant vice president of the United States for enquiry at the University of Utah Health Sciences. "Having an assay for hepcidin would make it a great deal easier and it would also help in diagnosis iron overload diseases."
Identification of the Hepcidin-Binding Domain
In the study, Kaplan and researchers from the University of Utah and University of California, Los Angeles report that they have identified the hepcidin-binding domain (HBD), the specific site where hepcidin binds to ferroportin. By placing a synthetic version of that binding site on agarose beads, the researchers developed a rapid, sensitive test, called the HBD assay, for measuring the concentration of active hepcidin in the blood.
The ability to observe and touchstone hepcidin has important implications for the diagnosis of anemias and iron clog disorders related to hepcidin. Anemia is a want of the oxygen-carrying molecules inside bolshie blood cells which commode be caused by smoothing iron deficiency, vitamin B12 or folate deficiency, or chronic illnesses. Anemia of chronic disease, or anemia of inflammation, is a shape of anemia that is thought to be related to abnormally high levels of hepcidin.
The most vulgar human upset of fe overload is hereditary bronzed diabetes, which leads to abnormal accumulation of iron in the liver, heart, skin, and other organs. Some types of hereditary hemochromatosis are associated with inappropriately low levels of hepcidin in the blood.
The HBD assay developed by Kaplan and his colleagues detects biologically active hepcidin. This assay commode readily notice variations in hepcidin levels in the blood due to mutations in genes that are known to affect hepcidin levels, as well as mutations in other genes involved in iron metamorphosis. It can also measure hepcidin assiduity in response to rubor. This novel test would allow doctors to severalise anemias and diseases of iron metabolism that arise from abnormalities in hepcidin from those that accept other causes.
Hepcidin was low reported for its purpose in the body's defense Department against bacterial and fungal infections. Current scientific evidence, however, suggests that hepcidin's primary use in the body is to shape iron balance.
Kaplan and his colleagues establish that even very minor changes to the composing of the HBD had significant personal effects on the ability of the binding site to bind hepcidin. They besides discovered that hepcidin's ability to bandage to the HBD decreases at temperatures below the normal human body temperature of 37�C due to structural changes in the hepcidin molecule at depress temperatures. This change in structure besides affected the ability of hepcidin to bind to bacteria. This raised questions about the effect of low temperatures on smoothing iron metabolism and antibacterial activity.
Evolutionary Insight
The hepcidin-binding domain of fish is nearly identical to the human HBD. The researchers looked at hepcidin in fish such as the brown trout from the Middle Provo River, which routinely live in very cold amnionic fluid. Most mammals have only when one hepcidin gene, only fish throw multiple hepcidin genes that encode hepcidin molecules of different lengths. In this study, Kaplan and his colleagues institute that the fish hepcidin which is the same length as human hepcidin was able to bandage to the HBD at temperatures as low as 4�C merely had very little antibacterial activity at both 4�C and 37�C. This discovery provides insight into the evolution of hepcidin among vertebrates. Human hepcidin has both iron and bacteria-related activities, piece fish hepcidin genes evolved to separate these functions.
Due to the similarity of the hepcidin binding land site among vertebrates, the usefulness of the novel HBD assay described in this study is not limited to humanity. "The check can be used to easily step hepcidin in the rakehell of all vertebrates," says Kaplan.
University of Utah Health Sciences
420 Chipeta Way, Ste. 1900
Salt Lake City, UT 84108
United States
http://healthcare.utah.edu/index.cfm
More info
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