Customized tissue engineering for ear reconstruction.

Tissue engineering (TE) of cartilage for reconstructive surgery has proven to be a promising option for obtaining tissue for 3D structures that results in minimal donor site morbidity. Technological advances in this area are important since many defects can only be treated with customized implants. Most TE strategies rely on the use of resorbable 3D scaffolds to guide the growing tissue, with each tissue requiring a specific scaffold that has precisely defined properties depending on the physiological environment. Rapid prototyping (RP) technologies allow the fabrication of scaffolds of various geometric complexities from a variety of materials and as composites, while even allowing the inner architecture of the object to be varied in a defined manner at any given location. Scaffolds can be manufactured using RP techniques directly from computer aided design (CAD) data sources, e.g. via an STL file. The combination of TE and RP serves as the basis for the production of customized implants, for example the cartilage ear framework, and provides new perspectives for autologous ear reconstruction.

Binding properties of the cerebral alpha4beta2 nicotinic acetylcholine receptor ligand 2-[18F]fluoro-A-85380 to plasma proteins.

INTRODUCTION: To determine the availability of nicotinic acetylcholine receptors in different human brain regions using the positron emission tomography (PET) radioligand 2-[18F]fluoro-A-85380 (2-[18F]FA) and invasive approaches for quantification, it is important to correct the arterial input function as well for plasma protein binding (PPB) of the radioligand as for radiolabeled metabolites accumulating in blood. This study deals with some aspects of PPB of 2-[18F]FA. METHODS: Patients with different neurological disorders (n=72), such as Parkinson's disease, Alzheimer's disease and multiple sclerosis, and a group of healthy volunteers (n=15) subjected for PET imaging were analyzed for their PPB level of 2-[18F]FA using ultrafiltration. Protein gel electrophoresis of plasma samples was performed to identify the binding protein of 2-[18F]FA. The dependency of PPB on time and on free ligand concentration was analyzed to obtain the binding parameters Bmax and Kd. RESULTS: Albumin was identified to be the binding protein of 2-[18F]FA. PPB of 2-[18F]FA was low at 17+/-4% and did not show significant differences between the groups of patients. Corresponding to this, a narrow range of plasma albumin of 0.62+/-0.05 mM was observed. Bmax was determined as twice the albumin concentration, which indicates two binding sites for 2-[18F]FA on the protein. No time dependence of the PPB could be observed. By relating PPB to Bmax, an average Kd value of 6.0+/-1.5 mM was obtained. CONCLUSION: This study shows the dependency of PPB of 2-[18F]FA on human albumin plasma concentration. An equation utilizing Bmax and Kd to easily estimate PPB is presented.