Fredrik Lauritzen will give his trial lecture with the title

The influence of physical activity on brain function. Metabolic and health-related aspects

on Thursday 26 April 2012 at 1030, in Auditorium A1.1001, Domus odontologica.

He will defend his PhD thesis with the title

Monocarboxylate transporters in temporal lobe epilepsy

on Thursday 26 April 2012 at 1330, in Auditorium A1.1001, Domus odontologica.

CMBN is pleased to invite you to a guest lecture by Tore Eid, Director, Human Brain Microdialysis Program, Assistant Director, Clinical Chemistry Laboratory, Yale School of Medicine - New Haven Hospital, with the title:

Astrocytic Regulation of Glutamate Homeostasis in Epilepsy

on Friday 27 April 2012 at 12:00 in the Anatomy lunch room, Domus medica.

Tore Eid is a Guest Professor at the CMBN.

Welcome!

Adam Robertson, John Arne Dahl and colleagues at CMBN have published a protocol for identification of the novel 6th DNA base in genomic DNA. The base, 5-hydroxymethylCytosine (5-hmC), was discovered over 30 years ago. At that time, the 5-hmC modification was suggested to be a rare and nonmutagenic DNA damage lesion and therefore was given little attention. In early 2009, 5-hmC was identified again; however, at that time the importance of 5-hmC in epigenetics was realized, as two independent groups began the initial characterization of the 5-hmC modification. Although the function of the 5-hmC modification remains unclear, it has become clear that identifying genomic regions that contain 5-hmC will help to elucidate the function of this base. The protocol described here is based on the procedure developed to isolate 5-hmC–containing DNA in two steps (i) glucosylation of 5-hmC and (ii) the subsequent pull-down of β-glu-5-hmC by JBP1-coated magnetic beads.

Robertson AB, Dahl JA, Ougland R, Klungland A (2012)
Pull-down of 5-hydroxymethylcytosine DNA using JBP1-coated magnetic beads
Nat Protoc, 7 (2), 340-50

Scientists in CIR and CMBN published a paper in Nature Communication that reveals the intermolecular interactions of the FcRn-albumin complex.

Albumin is the most abundant protein in blood where it has a pivotal role as a transporter of fatty acids and drugs. Like IgG, albumin has long serum half-life, protected from degradation by pH-dependent recycling mediated by interaction with the neonatal Fc receptor, FcRn. Although the FcRn interaction with IgG is well characterized at the atomic level, its interaction with albumin is not. Here we present structure-based modelling of the FcRn–albumin complex, supported by binding analysis of site-specific mutants, providing mechanistic evidence for the presence of pH-sensitive ionic networks at the interaction interface. These networks involve conserved histidines in both FcRn and albumin domain III. Histidines also contribute to intramolecular interactions that stabilize the otherwise flexible loops at both the interacting surfaces. These results may guide the development of novel albumin variants with altered serum half-life as carriers of drugs.

Andersen JT, Dalhus B, Cameron J, Daba MB, Plumridge A, Evans L, Brennan SO, Gunnarsen KS, Bjørås M, Sleep D, Sandlie I (2012)
Structure-based mutagenesis reveals the albumin-binding site of the neonatal Fc receptor
Nat Commun, 3, 610
PubMed 22215085

CMBN scientists have contributed to a translational study investigating Slc9a6 knockout mice. The project was lead by Prof. Petter Strømme, Department of Clinical Neurosciences for Children, Ullevål Hospital. Mutations in the corresponding human gene, the solute carrier family 9 isoform 6 on chromosome Xq26.3 encoding sodium–hydrogen exchanger 6, a protein mainly expressed in early and recycling endosomes are known to cause a complex and slowly progressive degenerative human neurological disease. The project is a collaboration between OUS and Steven U. Walkley, Rose F. Kennedy Centre, Albert Einstein College of Medicine, Bronx, NY, USA.

Strømme P, Dobrenis K, Sillitoe RV, Gulinello M, Ali NF, Davidson C, Micsenyi MC, Stephney G, Ellevog L, Klungland A, Walkley SU (2011)
X-linked Angelman-like syndrome caused by Slc9a6 knockout in mice exhibits evidence of endosomal-lysosomal dysfunction
Brain, 134 (Pt 11), 3369-83
PubMed 21964919

Enzymmangel gir sykdom
Forskningsaktuelt, Det medisinske Fakultet, Universitetet i Oslo
5 January 2012

Utstillingen Mind gap handler om hjernen og hjerneforskning. Den åpnet 16. april, og skal stå på Teknisk museum ut 2012. Universitetet i Oslo er hovedsamarbeidspartneren, og utstillingen inngår som en hovedattraksjon i universitetets 200-årsjubileum.

Mind gap's forskere finnes her