FREE POSITIONS

POST-DOCs
Currently, we are looking for SEVERAL post-docs specialized in mass spectrometry, proteomics, molecular cell biology, protein chemistry, and/or bacteriology
Please contact: gunnar.hansson@medkem.gu.se
see also contact details


We always have the possibility for a project work.
National and international post-docs who can provide their own funding are always welcome to contact us.

PROJECT WORK

(examensarbete, projektarbete, forskarskoleprojekt, sommarforskarskola) from 7.5 to 30 points

The group happily accepts students with suitable background for making these parts of their basic training within our group.
As a student (läkemedelsprogrammet, biomedicinska forskarskolan, läkarlinjen, molekylärbiologi, biokemi, analytisk kemi, civilingenjör, biologi, biomedicinsk analytiker, tandläkare, etc), you are always welcome to do a project work of 5 - 40 weeks in our group.
We are continuously having one or several students doing their project work in our group.
The more precise content of the project will be adjusted to the length (number of points) and current status of the project. There is a possibility to continue in the group (for example as a Ph. D. student) after a successful project work and the main (only) source of recruiting new members.

Contact: gunnar.hansson@medkem.gu.se or by telephone 031-786 3488 for more information.

Examples of projects
 ASSEMBLY AND PROCESSING OF THE GEL-FORMING MUC2 MUCIN IN COLON AND ITS RELATION TO ULCERATIVE COLITIS
Student project description: Student projects include plasmid construction, eukaryotic cell transfection, cell culture, immunoprecipitation, gel electrophoresis, western blotting, fluorescence microscopy.
General project description: The project is studying the structure and function of gel forming mucins (mucus glycoproteins) in the gastrointestinal tract and lungs. Mucins are large, highly glycosylated molecules having typical mucin domains, where the oligosaccharides are linked via N-acetylgalactosamine to the amino acids threonine and serine. Mucins are forming the gel-like properties of mucus. The major mucin of the gastrointestinal tract is called MUC2 and is produced by the intestinal goblet cells. The MUC2 mucin has properties that is different from other mucins, in that it can form 'insoluble' mucus gels. The apoprotein of this mucin has two central mucin domains and cysteine-rich domains at both the N- and C-terminal ends. The primary translational product is 600 kDa in mass and is quickly dimerized in the endoplasmic reticulum of the cell. The addition of O-glycans starts when the dimer enters the Golgi apparatus and when fully glycosylated the mass will increase to about 5 million Da. The MUC2 mucin is forming polymers by trimerization in the N-terminus in the TGN and secretory vesicles. The MUC5AC mucin is formed in the lungs and has similar structural features as MUC2, except that it is normally not becoming insoluble. The formation and assembly of the MUC2 and MUC5AC mucin is studied in cell culture using the expression of truncated recombinant forms of these mucins. This project is in the forefront of molecular cell biology and function of the secretory system involving the regulated secretory pathway. The different expression plasmids also include GFP sequences (green fluorescent protein) allowing study by fluorescence confocal microscopy. Student projects include plasmid construction, eukaryotic cell transfection, metabolic labeling, immunoprecipitation, gel electrophoresis, fluorescence microscopy. A better understanding of mucins and their assembly causing altered properties will be very important for several types of diseases in the gastrointestinal and respiratory tracts and give the possibility to develop novel therapies.


OTHER MOLECULES FOUND IN THE MUCUS OF THE LARGE INTESTINE
Student project description: Student projects include plasmid construction, eukaryotic cell transfection, cell culture, immunoprecipitation, gel electrophoresis, western blotting, fluorescence microscopy.
General project description: During our proteomics studies we have found a number of interesting molecules that are suggested to have important roles in the function of the mucus layers of the large instestine. One of these will be studied in more detail.


STRUCTURE, FUNCTION AND SIGNALING OF TRANSMEMBRANE MUCINS
Student project description: The student project include plasmid construction, eukaryotic cell transfection, cell culture, immunoprecipitation, gel electrophoresis, western blotting, fluorescence microscopy.
General project description: The human genome has expanded its repertoire of transmembrane mucins compared to lower animals. Today these include the mucins MUC1, MUC3A, MUC3B, MUC4, MUC12, MUC13, MUC16, and MUC17. These molecules have a large extracellular mucin domain often projecting several micrometers from the apical surface of the cell. All of them are cleaved extracellular, but still held together under physiological conditions. Their C-termini are located in the cytoplasm and have been shown to be involved in intracellular signaling for at least MUC1. The project will address the extracellular cleavage, the properties and function of this and potential relation to signaling phenomena elicited by the cytoplasmic tail for one of the above mentioned mucins.


ROLE OF PDZ MEDIATED INTERACTIONS WITH MUCINS AND CFTR
Student project description: The student project includes plasmid construction, eukaryotic cell transfection, cell culture, immunoprecipitation, gel electrophoresis, western blotting, fluorescence microscopy.
General project description: PDZ domains are found in proteins organizing membrane proteins from the cytoplasm by binding specific C-terminal sequences. CFTR, a chloride channel defect in cystic fibrosis, has a PDZ-binding C-terminus. In a search for other proteins that can bind PDZK1, a PDZ protein with four PDZ domains, the MUC3, 12 and 17 mucins were found to bind PDZ domain proteins.


EXPRESSION OF RECOMBINANT MUCINS IN THE LARGE SCALE
Student project description: The student project include plasmid construction, eukaryotic cell transfection, cloning, cell culture, gel electrophoresis, western blotting, ultrafiltration and protein purification. This project is should be specially suitable for a bioengineer student.
General project description: Mucins are large and complex glycoproteins that are difficult to study unless expressed as smaller parts. We have established expression systems for recombinant expression of the extracellular parts of MUC1 as well as the N- and C-termini of the MUC2 and MUC5AC mucins. The mucins are expressed in CHO cells. Additional mucins as well as parts of these will be added to the repertoire. These recombinant proteins will be used as tools in the laboratory, for vaccination trails for breast cancer (MUC1), for crystallization and other structural studies and later developed into therapeutics. The group is directly linked to a Swegene core facility, MPE, for large scale expression of large amounts recombinant proteins. The Muc1 project is part of a EU funded network including laboratories in London and Germany. The glycosylation of the produced recombinant proteins can be manipulated by expression in different cell lines as well as the addition of stably expressing glycosyltransferases. The student will take part in the construction of an expression plasmid, express this in cells, clone these and analyze the secreted recombinant product.