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  • MEDLINE/PubMed (NLM)  (400)
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  • 1
    Article
    Article
    Language: English
    In: Clinical Chemistry, 02/01/2014, Vol.60(2), pp.424-424
    Description: We appreciate the interest in our recently published CALIPER (Canadian Laboratory Initiative for Pediatric Reference Intervals)1 manuscripts and are delighted to see that the publications are stimulating further discussion in the field. Overall, the authors of these letters have raised several important questions, but they appear to have overlooked some important points when reviewing the published studies. They also fail to acknowledge the numerous limitations inherent in interpretation of cortisol as addressed in our published articles: namely, that circadian rhythms in infants differ from those of adults, that the stress of phlebotomy can alter cortisol concentrations, and that we examined a single time point in each individual within a large population of children rather than multiple time points in a small number of individuals. That being said, in our population, the reference intervals did not differ significantly between morning and afternoon. We did not seek to answer in our studies whether the influence of circadian rhythms could be observed within individuals, but rather, whether such a change could be observed across the population. Of course, our population is ethnically diverse and is representative of a healthy population in Ontario, Canada. Therefore, we believe that our conclusions are not altered by points raised in these letters. We agree that performing sequential sampling for cortisol measurement at multiple time points over 3–5 days would be ideal to assess the diurnal variation for cortisol. However, such a determination was well beyond the scope of the recently published CALIPER studies, which established reference value distributions in a large, healthy population of children. We would like to respond first to the question raised by Rovnaghi et al. (1) regarding the differences in age partitions between the CALIPER immunoassay study published in Clinical Chemistry (2) and the HPLC-MS/MS study published in Clinical Biochemistry (3 …
    Keywords: Medicine;
    ISSN: 0009-9147
    E-ISSN: 1530-8561
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  • 2
    Language: English
    In: Clinical chemistry, October 2013, Vol.59(10), pp.1538-9
    Description: In a recent issue of Science , Lacetera, Macis, and Slonim summarize new information regarding the impact that economic rewards have on the blood supply and safety (1). For many years, the WHO has taken the stance that economic incentives decrease the safety of the blood supply. In support of the WHO position, the establishment of an all-volunteer blood supply led to a dramatic decrease in the incidence of posttransfusion hepatitis C. The authors submit, however, that the position of the WHO is based on studies that failed to control for several confounding variables (percentage of first-time donors, location of donation, and use of prisoners). Recent randomized field surveys reviewed by the authors found that economic incentives increase …
    Keywords: Guidelines As Topic ; Blood Donors -- Ethics ; Reimbursement, Incentive -- Ethics
    ISSN: 00099147
    E-ISSN: 1530-8561
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  • 3
    Article
    Article
    Language: English
    In: International Journal of Pharmaceutics, 02/22/2007, Vol.331(1), pp.1-10
    Description: To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.ijpharm.2006.10.021 Byline: Jorg Kreuter Keywords: Nanoparticles; Historical development Abstract: The historical development of nanoparticles starting with Paul Ehrlich and then first attempts by Ursula Scheffel and colleagues and the extensive work by the group of Professor Peter Speiser at the ETH Zurich in the late 1960s and early 1970s are described from a personal point of view. Special attention is given to the years between 1970 and the early 1980s. Further developments resulting from this work are also followed, and focus is placed on especially interesting improvements such as nanoparticles for the delivery of drugs across the blood-brain barrier (BBB) and PEGylated nanoparticles with a prolonged blood circulation time. Author Affiliation: Institut fur Pharmazeutische Technologie, Biozentrum, J.W. Goethe-Universitat, D-60439 Frankfurt, Germany Article History: Received 4 October 2006; Accepted 10 October 2006
    Keywords: Nanotechnology ; Nanoparticles;
    ISSN: 03785173
    E-ISSN: 18733476
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  • 4
    Language: English
    In: International Journal of Pharmaceutics, 2007, Vol.341(1), pp.207-214
    Description: Human serum albumin (HSA) nanoparticles represent promising drug carrier systems. Binding of cytostatics to HSA nanoparticles may diminish their toxicity, optimise their body distribution and/or may overcome multidrug resistance. In the present study, doxorubicin-loaded HSA nanoparticle preparations were prepared. Doxorubicin was loaded to the HSA nanoparticles either by adsorption to the nanoparticles’ surfaces or by incorporation into the particle matrix. Both loading strategies resulted in HSA nanoparticles of a size range between 150 nm and 500 nm with a loading efficiency of 70–95%. The influence on cell viability of the resulting nanoparticles was investigated in two different neuroblastoma cell lines. The anti-cancer effects of the drug-loaded nanoparticles were increased in comparison to doxorubicin solution. Based on these result a standard protocol for the preparation of doxorubicin-loaded HSA nanoparticles for further antitumoural studies was established.
    Keywords: Nanoparticles ; Doxorubicin ; Human Serum Albumin (HSA) ; Physicochemical Characterisation ; Cell Viability ; Pharmacy, Therapeutics, & Pharmacology
    ISSN: 0378-5173
    E-ISSN: 1873-3476
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  • 5
    Language: English
    In: Die Pharmazie, July 2013, Vol.68(7), pp.549-54
    Description: Lysosomal storage disorders like mucopolysaccharidosis (MPS) VI are rare diseases with a lack of well-suited treatments. Even though an enzyme replacement therapy (ERT) of recombinant arylsulfatase B (ASB) is available for MPS VI, the administration cannot positively affect the neurologic manifestations such as spinal cord compression. Since nanoparticles (NP) have shown to be effective drug carriers, the feasibility of arylsulfatase B adsorption onto poly(butyl cyanoacrylate) (PBCA) nanoparticles was investigated in this study. In order to advance the ERT of ASB, the adsorption of the latter on the surface of PBCA NP as well as in vitro release in serum was investigated. With alteration of parameters like temperature, incubation time, pH, and enzyme amount, the adsorption process revealed to be stable with a maximum capacity of 67 microg/mg NP at a pH of 6.3. In vitro release experiments demonstrated that the adsorption is stable for at least 60 minutes in human blood serum, indicating that the ASB-loaded PBCA nanoparticles represent a promising candidate for ERT of MPS VI.
    Keywords: Enzyme Replacement Therapy ; Mucopolysaccharidosis VI -- Drug Therapy ; N-Acetylgalactosamine-4-Sulfatase -- Therapeutic Use
    ISSN: 0031-7144
    Source: MEDLINE/PubMed (U.S. National Library of Medicine)
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  • 6
    Language: English
    In: Journal of Controlled Release, 28 September 2015, Vol.214, pp.76-84
    Description: Highly aggressive cancer types such as pancreatic cancer possess a mortality rate of up to 80% within the first 6 months after diagnosis. To reduce this high mortality rate, more sensitive diagnostic tools allowing an early stage medical imaging of even very small tumours are needed. For this purpose, magnetic, biodegradable nanoparticles prepared using recombinant human serum albumin (rHSA) and incorporated iron oxide (maghemite, -Fe O ) nanoparticles were developed. Galectin-1 has been chosen as target receptor as this protein is upregulated in pancreatic cancer and its precursor lesions but not in healthy pancreatic tissue nor in pancreatitis. Tissue plasminogen activator derived peptides (t-PA-ligands), that have a high affinity to galectin-1 have been chosen as target moieties and were covalently attached onto the nanoparticle surface. Improved targeting and imaging properties were shown in mice using single photon emission computed tomography–computer tomography (SPECT–CT), a handheld gamma camera, and magnetic resonance imaging (MRI).
    Keywords: Rhsa Nanoparticles ; Maghemite ; T-PA-Ligands to Galectins ; T-Papeptide1lac ; Single Photon Emission Computed Tomography–Computer Tomography (Spect–CT) ; Handheld Gamma Camera ; Magnetic Resonance Imaging (Mri) ; Pharmacy, Therapeutics, & Pharmacology
    ISSN: 0168-3659
    E-ISSN: 1873-4995
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  • 7
    Language: English
    In: Die Pharmazie, July 2014, Vol.69(7), pp.518-24
    Description: Arylsulfatase A (ASA) deficiency is the cause of metachromatic leucodystrophy (MLD), a lysosomal storage disease associated with severe neurological disorders. Poly(butyl cyanoacrylate) (PBCA) nanoparticles overcoated with polysorbate 80 enabled the delivery of several drugs across the blood-brain barrier to the brain suggesting that these nanoparticles also may transport ASA across this barrier. The objective of this research, therefore, was to evaluate the feasibility of loading ASA onto PBCA nanoparticles. A stable ASA-loaded PBCA nanoparticle formulation was developed that could be easily freeze-dried and stored over a period of more than 8 weeks. The maximum loading capacity for this enzyme was -59 microg per 1 mg of PBCA. In the presence of 3% sucrose as a lyoprotector the activity of freeze-dried ASA was found to be 100% recoverable.
    Keywords: Cerebroside-Sulfatase -- Therapeutic Use ; Enbucrilate -- Chemistry ; Enzyme Replacement Therapy -- Methods
    ISSN: 0031-7144
    Source: MEDLINE/PubMed (U.S. National Library of Medicine)
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  • 8
    Language: English
    In: Biochimica et biophysica acta, 12 January 2001, Vol.1544(1-2), pp.177-88
    Description: Protamine is a cationic peptide with a molecular mass of approx. 4000 Da that is able to condense DNA. In the present study it was used to complex antisense oligonucleotides (ODNs) and to form solid particles with initial diameters of 90-150 nm. The reaction was very rapid and occurred by simple mixing of diluted solutions of the polycation with the oligonucleotide. The aggregation was dependent on the oligonucleotide chain length and the protamine/ODN mass ratio. Particle formation required a minimal chain length of nine nucleotides and a mass ratio of 0.5:1. The particle surface charge and the number of particles depended on the mass ratio. With increasing amounts of the peptide, the number of particles and the zeta potential increased. Both negatively and positively charged particles improved the stability of oligonucleotides against DNase I digestion. Above a mass ratio of 2.5:1 no degradation was found. The uptake of unbound rhodamine-labelled ODNs and its complexes with protamine was determined with Vero cells under in vitro cell culture conditions at 37 degrees C and 4 degrees C. At 37 degrees C the cellular uptake increased with increasing mass ratio. The internalized oligonucleotides were localized in the cytoplasm and in the nucleus of the cells. When Vero cells were treated with these samples at 4 degrees C for 4 h, no fluorescence could be detected inside the cells. Therefore, our data indicate an energy dependent endocytotic uptake mechanism. In contrast, spermine and spermidine, which are also known condensation agents, did not aggregate with oligonucleotides into nanoparticles under the same conditions.
    Keywords: Oligonucleotides, Antisense -- Chemical Synthesis ; Organophosphorus Compounds -- Chemical Synthesis ; Thionucleotides -- Chemical Synthesis
    ISSN: 0006-3002
    Source: MEDLINE/PubMed (U.S. National Library of Medicine)
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  • 9
    Language: English
    In: Pharmaceutical research, July 1996, Vol.13(7), pp.1055-8
    Description: The organ distribution of radiolabeled poly (methyl methacrylate) (PMMA) nanoparticles coated with plasma proteins and serum complement in rats was studied in order to determine the effect of serum complement on the particle phagocytosis by the organs of the reticulo-endothelial system (RES). PMMA-nanoparticles were coated overnight with plasma proteins or serum complement, and injected into Wistar rats. The body distribution of nanoparticles was measured by means of scintillation counting of organ samples. In addition, proteins adsorbed to the particle surface were inactivated by heat treatment prior to injection, and the particle's distribution was measured as described above. Whereas uncoated nanoparticles (control group) were mainly taken up by the Kupffer cells in the liver, incubation of the particles in plasma for 12 h followed by heat inactivation reduced the particle concentrations in the liver to merely 22% after 30 min. After 120 min, liver concentrations were still lower than the control group, and almost 30% of the administered dose of the heat-inactivated particle group was present in non-RES organs and tissues. Particles with non-inactivated complement were accumulated in the lung at concentrations of 29% after 30 min, which increased to 71% after 120 min, whereas those coated with inactivated complement reached lung concentrations above 70% already after 30 min. Particles coated with plasma components are able to avoid uptake by the RES, especially after heat inactivation of the plasma components adsorbed. Adsorption and heat inactivation of complement proteins alone, however, does not have the same result as coating with plasma proteins followed by heat inactivation. Therefore, it is concluded that plasma components other than complement proteins take part in the process of RES activation and phagocytosis of injected nanoparticles.
    Keywords: Complement System Proteins -- Chemistry ; Mononuclear Phagocyte System -- Drug Effects ; Polymethacrylic Acids -- Pharmacology
    ISSN: 0724-8741
    E-ISSN: 1573904X
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  • 10
    In: Bone Marrow Transplantation, 2017
    Keywords: Allografts–Blood ; Bone Marrow Transplantation–Blood ; Donor Selection–Therapy ; Female–Therapy ; HLA Antigens–Therapy ; Humans–Therapy ; Isoantibodies–Therapy ; Leukemia, Myelogenous, Chronic, BCR-Abl Positive–Therapy ; Middle Aged–Therapy ; Tissue Donors–Therapy ; HLA Antigens ; Isoantibodies;
    ISSN: 0268-3369
    E-ISSN: 1476-5365
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