Multiple assembly strategies for silica aerogel-fiber combinations – a review

Silica aerogels have a unique structure that makes them promising materials for variable applications. However, they are brittle due to weak inter-particle necks, and also expensive. Combining aerogel with fibers can not only enhance the mechanical/insulation properties, but also reduce dust release, and ease practical application. The majority of review articles in this field have been on the aerogel/textile systems' application or on textile impregnation in silica sol utilizing the sol–gel technique, with a few papers also addressing the use of aerogel as filler. This review for the first time highlights all strategies to assemble silica aerogel with textile materials. For sol–gel approaches, the fibers can be impregnated in a silica precursor sol to form the aerogel in situ between the fibers, but the sol itself can also be spun into aerogel fibers. Other strategies employ pre-formed silica aerogel, mixed in polymer or solvent matrices/slurries, to form aerogel injected blankets, aerogel-filled material coated fibers, and aerogel-filled composite fibers. Aerogel particles-filled textile packages have also been proposed. The emerging activities on simulations of aerogel-fiber combinations are reviewed. The advantages/disadvantages of various approaches are evaluated, and the current market situation and an outlook for the future of the field are summarized

Identification of increased amounts of eppin protein complex components in sperm cells of diabetic and obese individuals by difference gel electrophoresis

Metabolic disorders like diabetes mellitus and obesity may compromise the fertility of men and women. To unveil disease-associated proteomic changes potentially affecting male fertility, the proteomes of sperm cells from type-1-diabetic, type-2-diabetic, non-diabetic obese and clinically healthy individuals were comparatively analyzed by differ-ence gel electrophoresis (DIGE). The adaptation of a general protein extraction proce-dure to the solubilization of proteins from sperm cells allowed for the resolution of 3,187 fluorescent spots in the DIGE image of the master gel, which contained the entirety of solubilized sperm proteins. Comparison of the pathological and reference proteomes by applying an average abundance ratio setting of 1.6 and a p≤0.05 criterion resulted in the identification of 79 fluorescent spots containing proteins that were present at significantly changed levels in the sperm cells. Biometric evaluation of the fluorescence data followed by mass spectrometric protein identification revealed altered levels of 12, 71 and 13 pro-tein species in the proteomes of the type-1-diabetic, type-2-diabetic and non-diabetic obese patients, respectively, with considerably enhanced levels of the same set of one molecular form of semenogelin-1, one form of clusterin and two forms of lactotransferrin in each group of pathological samples. Remarkably,galactosidase-1-like protein was the only protein that was detected at decreased levels in all three pathological situations. The former three proteins are part of the eppin (epididymal proteinase inhibitor) protein complex (EPC), which is thought to fulfill fertilization-related functions, such as ejaculate sperm protection, motility regulation and gain of competence for acrosome reaction, while the putative role of the latter protein to function as a glycosyl hydrolase during sperm maturation remains to be explored at the protein/enzyme level. The strikingly similar differences detected in the three groups of pathological sperm proteomes reflect a disease-associated enhanced formation of predominantly proteolytically modified forms of the EPC components, possibly as a response to enduring hyperglycemia and enhanced oxidative stress

Pharmacokinetics and cellular uptake of imatinib and its main metabolite CGP74588

Despite the remarkable clinical response rates to imatinib in the treatment of bcr-abl leukemic patients, pharmacokinetic data on this relatively novel substance are needed to improve our understanding of the emergence of resistance, the interindividual variations of clinical response and the clinical and biologic relevance of its main metabolite N-desmethyl-imatinib. We present here pharmacokinetic data obtained with a newly designed HPLC approach in 97 patients with chronic myeloid leukemia or acute lymphatic leukemia (ALL) under treatment with imatinib that allowed us to calculate the AUC (39.5 μg·h/ml for an oral dose of 400 mg daily), the t1/2 (18.2 h) and the peak concentration (1.92 μ/ml for an oral dose of 400 mg daily) of imatinib in plasma. In a subgroup of patients, the same parameters were analyzed for N-desmethyl-imatinib. We also provide data on the imatinib concentration in the cerebrospinal fluid (CSF) of ALL patients and demonstrate that oral administration of imatinib resulted only in a marginal flux across the blood-brain barrier. Finally, in an in vitro setting, we determined cellular concentrations of imatinib in HL-60 cells and showed an over-proportional uptake both in RPMI medium and in human plasma. Using an arithmetical approach combining all parameters obtained in imatinib-treated patients, we finally provide a conclusive approximation of basic pharmacokinetic data for both imatinib and its main metabolite N-desmethyl-imatinib