Current Issue : July - September Volume : 2013 Issue Number : 3 Articles : 5 Articles
The primary focus of national blood programs is the provision of a safe and adequate blood supply. This goal is dependent on\r\nregular voluntary donations and a regulatory infrastructure that establishes and enforces standards for blood safety. Progress in ex\r\nvivo expansion of blood cells from cell sources including peripheral blood, cord blood, induced pluripotent stem cells, and human\r\nembryonic stem cell lines will likely make alternative transfusion products available for clinical use in the near future. Initially,\r\nalloimmunized patients and individuals with rare blood types are most likely to benefit from alternative products. However, in\r\ndeveloped nations voluntary blood donations are projected to be inadequate in the future as blood usage by individuals 60 years\r\nand older increases. In developing nations economic and political challenges may impede progress in attaining self-sufficiency.\r\nUnder these circumstances, ex vivo generated red cells may be needed to supplement the general blood supply....
Since the invention of solid phase synthetic methods by Merrifield in 1963, the\r\nnumber of research groups focusing on peptide synthesis has grown exponentially.\r\nHowever, the original step-by-step synthesis had limitations: the purity of the final product\r\ndecreased with the number of coupling steps. After the development of Boc and Fmoc\r\nprotecting groups, novel amino acid protecting groups and new techniques were introduced\r\nto provide high quality and quantity peptide products. Fragment condensation was a\r\npopular method for peptide production in the 1980s, but unfortunately the rate of\r\nracemization and reaction difficulties proved less than ideal. Kent and co-workers\r\nrevolutionized peptide coupling by introducing the chemoselective reaction of unprotected\r\npeptides, called native chemical ligation. Subsequently, research has focused on the\r\ndevelopment of novel ligating techniques including the famous click reaction, ligation of\r\npeptide hydrazides, and the recently reported -ketoacid-hydroxylamine ligations with 5-\r\noxaproline. Several companies have been formed all over the world to prepare high quality\r\nGood Manufacturing Practice peptide products on a multi-kilogram scale. This review\r\ndescribes the advances in peptide chemistry including the variety of synthetic peptide\r\nmethods currently available and the broad application of peptides in medicinal chemistry....
Although it is generally accepted that blood has never been safer than today, transfusion-associated side \r\neffects, particularly infective, still occur. Unlike screening strategies, pathogen reduction technologies offer a \r\nnew approach to increase blood safety by actively/directly targeting possible, also emerging pathogens or donor \r\nleukocytes. Advanced technologies for cellular blood products like the psoralen-based INTERCEPT BLOOD \r\nSYSTEM or the riboflavin-based Mirasol pathogen reduction technology system have extensively been examined \r\nand are on the way to enter the blood bank routine. However, as with any medical treatment, the transfusion of \r\npathogen reduced blood products is not completely risk-free. Due to possible impairment of the treated blood cells \r\nthe transfusion success is significantly lower as compared to untreated blood products. Long-term side effects \r\nconcerning the photosensitizers and their photoproducts still remain a matter of debate. This paper outlines \r\ncurrent pathogen reduction technologies but also focuses on ethical concerns associated with the employment \r\nof these techniques....
Randomized clinical trials (RCTs) demonstrated the equal efficacy of urinary human chorionic\r\ngonadotropin (uhCG) and recombinant hCG (rhCG) products in in vitro fertilisation (IVF). However,\r\nlimitations inherent with RCTs necessitate the reinforcement of RCT results in real-life. We\r\nretrospectively analyzed pregnancies after treatment with rhCG and uhCG products (n = 391,\r\nand 96, resp.). We found that laboratory-verified pregnancy occurred more frequently in rhCG\r\npatients than in those on uhCG (43% versus 30%, P = 0.02). The association remains significant\r\n(P = 0.002) after its adjustment for clinical characteristics. The prevalence of laboratory-verified\r\npregnancies was higher with GnRH agonist use (P = 0.012) and BMI under 30 kg/m2 (P = 0.053)\r\nwhile decreased the age (P =0.014) and the number of previous failed attempts (P =0.08). Similar\r\n(but not significant) trends were observed with rates of pregnancy filled the 24th week. These\r\nresults reinforce RCTs supporting the notion that rhCG is more efficient as uhCG during IVF....
In the present paper we explored the capacity of yeast Saccharomyces cerevisiae as host for heterologous expression of\r\nhuman Aquaporin-1. Aquaporin-1 cDNA was expressed from a galactose inducible promoter situated on a plasmid with an\r\nadjustable copy number. Human Aquaporin-1 was C-terminally tagged with yeast enhanced GFP for quantification of\r\nfunctional expression, determination of sub-cellular localization, estimation of in vivo folding efficiency and establishment of\r\na purification protocol. Aquaporin-1 was found to constitute 8.5 percent of total membrane protein content after expression\r\nat 15uC in a yeast host over-producing the Gal4p transcriptional activator and growth in amino acid supplemented minimal\r\nmedium. In-gel fluorescence combined with western blotting showed that low accumulation of correctly folded\r\nrecombinant Aquaporin-1 at 30uC was due to in vivo mal-folding. Reduction of the expression temperature to 15uC almost\r\ncompletely prevented Aquaporin-1 mal-folding. Bioimaging of live yeast cells revealed that recombinant Aquaporin-1\r\naccumulated in the yeast plasma membrane. A detergent screen for solubilization revealed that CYMAL-5 was superior in\r\nsolubilizing recombinant Aquaporin-1 and generated a monodisperse protein preparation. A single Ni-affinity\r\nchromatography step was used to obtain almost pure Aquaporin-1. Recombinant Aquaporin-1 produced in S. cerevisiae\r\nwas not N-glycosylated in contrast to the protein found in human erythrocytes....
Loading....