Concealed Neuroanatomy in Michelangelo's Separation of Light From Darkness in the Sistine Chapel
ABSTRACT Michelangelo Buonarroti (1475-1564) was a master anatomist as well as an artistic genius. He dissected cadavers numerous times and developed a profound understanding of human anatomy. From 1508 to 1512, Michelangelo painted the ceiling of the Sistine Chapel in Rome. His Sistine Chapel frescoes are considered one of the monumental achievements of Renaissance art. In the winter of 1511, Michelangelo entered the final stages of the Sistine Chapel project and painted 4 frescoes along the longitudinal apex of the vault, which completed a series of 9 central panels depicting scenes from the Book of Genesis. It is reported that Michelangelo concealed an image of the brain in the first of these last 4 panels, namely, the Creation of Adam. Here we present evidence that he concealed another neuronanatomic structure in the final panel of this series, the Separation of Light From Darkness, specifically a ventral view of the brainstem. The Separation of Light From Darkness is an important panel in the Sistine Chapel iconography because it depicts the beginning of Creation and is located directly above the altar. We propose that Michelangelo, a deeply religious man and an accomplished anatomist, intended to enhance the meaning of this iconographically critical panel and possibly document his anatomic accomplishments by concealing this sophisticated neuroanatomic rendering within the image of God.
SourceAvailable from: Hunkoog Jho12/2014; 34(8):755-765. DOI:10.14697/jkase.2014.34.8.0755
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Article: Lactoferrin, all roads lead to Rome.[Show abstract] [Hide abstract]
ABSTRACT: Lactoferrin is an iron-binding cationic glycoprotein that is constitutively synthesized by exocrine glands and by neutrophils. Its biosynthesis can be markedly increased during infection and inflammation. This multifunctional protein also acts as a major player in host defense in bodily fluids while it simultaneously protects the human mucosa. Several functions of lactoferrin are dependent on its ability to avidly bind two ferric ions in two characteristic binding sites while other biological activities do not require this property and they are mediated by other parts of the protein. In particular, the highly basic N-terminal regions of human and bovine lactoferrin seem to play an important role in the antimicrobial and immuno-regulatory properties of the protein, which can be emulated to some extent by using synthetic peptide derivatives that resemble this region. From the 1960s onward, when the protein was first purified from milk, the number of scientific publications concerning itsBioMetals 08/2014; DOI:10.1007/s10534-014-9787-7 · 2.69 Impact Factor