Learning histology – dental and medical students' study strategies

PurposeHistology, the science of cells and tissues at the microscopic level, is an integral component of most dental and medical curricula and is often taught using both traditional and novel computer‐based didactic approaches. The purpose of this study was to analyse the strategies used by dental and medical students when studying this very visual and challenging subject.MethodsData were collected from 75 dental and 143 medical students, who had almost identical histology learning resources at their disposal.ResultsWhen compared with their medical counterparts, dental students view histology as a more difficult subject and as less relevant for their future career. Whereas dental students, who are required to attend class unlike medical students, made more use of in‐classroom learning opportunities, they did not take as much advantage of out‐of‐classroom resources. In addition, dental students reported a significantly higher tendency than medical students to work together, rather than to study alone.DiscussionSmall differences in the dental versus the medical learning environment associate with several observed differences in learning strategies that are adopted by dental and medical students.ConclusionsThese differences should be considered when teaching the subject of histology to dental or to medical students.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/111121/1/eje12104.pd

Mechanism of the Very Efficient Quenching of Tryptophan Fluorescence in Human γD- and γS-Crystallins: The γ-Crystallin Fold May Have Evolved To Protect Tryptophan Residues from Ultraviolet Photodamage†

Proteins exposed to UV radiation are subject to irreversible photodamage through covalent modification of tryptophans (Trps) and other UV-absorbing amino acids. Crystallins, the major protein components of the vertebrate eye lens that maintain lens transparency, are exposed to ambient UV radiation throughout life. The duplicated β-sheet Greek key domains of β- and γ-crystallins in humans and all other vertebrates each have two conserved buried Trps. Experiments and computation showed that the fluorescence of these Trps in human γD-crystallin is very efficiently quenched in the native state by electrostatically enabled electron transfer to a backbone amide [Chen et al. (2006) Biochemistry 45, 11552−11563]. This dispersal of the excited state energy would be expected to minimize protein damage from covalent scission of the excited Trp ring. We report here both experiments and computation showing that the same fast electron transfer mechanism is operating in a different crystallin, human γS-crystallin. Examination of solved structures of other crystallins reveals that the Trp conformation, as well as favorably oriented bound waters, and the proximity of the backbone carbonyl oxygen of the n − 3 residues before the quenched Trps (residue n), are conserved in most crystallins. These results indicate that fast charge transfer quenching is an evolved property of this protein fold, probably protecting it from UV-induced photodamage. This UV resistance may have contributed to the selection of the Greek key fold as the major lens protein in all vertebrates.National Eye Institute (Grant EY 015834

Architecture and regulation of a GDNF-GFRα1 synaptic adhesion assembly

Abstract Glial-cell line derived neurotrophic factor (GDNF) bound to its co-receptor GFRα1 stimulates the RET receptor tyrosine kinase, promoting neuronal survival and neuroprotection. The GDNF-GFRα1 complex also supports synaptic cell adhesion independently of RET. Here, we describe the structure of a decameric GDNF-GFRα1 assembly determined by crystallography and electron microscopy, revealing two GFRα1 pentamers bridged by five GDNF dimers. We reconsitituted the assembly between adhering liposomes and used cryo-electron tomography to visualize how the complex fulfils its membrane adhesion function. The GFRα1:GFRα1 pentameric interface was further validated both in vitro by native PAGE and in cellulo by cell-clustering and dendritic spine assays. Finally, we provide biochemical and cell-based evidence that RET and heparan sulfate cooperate to prevent assembly of the adhesion complex by competing for the adhesion interface. Our results provide a mechanistic framework to understand GDNF-driven cell adhesion, its relationship to trophic signalling, and the central role played by GFRα1