Chevron bunionectomy fixation: In vitro stability assessment of plate-and-screw system compared with kirschner wire

1995 ◽  
Vol 34 (3) ◽  
pp. 266-272 ◽  
Author(s):  
Robert K. Buckenberger ◽  
Flair D. Goldman
Materials ◽  
2021 ◽  
Vol 14 (23) ◽  
pp. 7130
Author(s):  
Ruth Gong Li ◽  
Kim Lindland ◽  
Tina Bjørnlund Bønsdorff ◽  
Sara Westrøm ◽  
Roy Hartvig Larsen

Lead-212 is recognized as a promising radionuclide for targeted alpha therapy for tumors. Many studies of 212Pb-labeling of various biomolecules through bifunctional chelators have been conducted. Another approach to exploiting the cytotoxic effect is coupling the radionuclide to a microparticle acting as a carrier vehicle, which could be used for treating disseminated cancers in body cavities. Calcium carbonate may represent a suitable material, as it is biocompatible, biodegradable, and easy to synthesize. In this work, we explored 212Pb-labeling of various CaCO3 microparticles and developed a protocol that can be straightforwardly implemented by clinicians. Vaterite microparticles stabilized by pamidronate were effective as 212Pb carriers; labeling yields of ≥98% were achieved, and 212Pb was strongly retained by the particles in an in vitro stability assessment. Moreover, the amounts of 212Pb reaching the kidneys, liver, spleen, and skeleton of mice following intraperitoneal (i.p.) administration were very low compared to i.p. injection of unbound 212Pb2+, indicating that CaCO3-bound 212Pb exhibited stability when administered intraperitoneally. Therapeutic efficacy was observed in a model of i.p. ovarian cancer for all the tested doses, ranging from 63 to 430 kBq per mouse. Lead-212-labeled CaCO3 microparticles represent a promising candidate for treating intracavitary cancers.


1977 ◽  
Vol 16 (04) ◽  
pp. 157-162 ◽  
Author(s):  
C. Schümichen ◽  
B. Mackenbrock ◽  
G. Hoffmann

SummaryThe bone-seeking 99mTc-Sn-pyrophosphate compound (compound A) was diluted both in vitro and in vivo and proved to be unstable both in vitro and in vivo. However, stability was much better in vivo than in vitro and thus the in vitro stability of compound A after dilution in various mediums could be followed up by a consecutive evaluation of the in vivo distribution in the rat. After dilution in neutral normal saline compound A is metastable and after a short half-life it is transformed into the other 99mTc-Sn-pyrophosphate compound A is metastable and after a short half-life in bone but in the kidneys. After dilution in normal saline of low pH and in buffering solutions the stability of compound A is increased. In human plasma compound A is relatively stable but not in plasma water. When compound B is formed in a buffering solution, uptake in the kidneys and excretion in urine is lowered and blood concentration increased.It is assumed that the association of protons to compound A will increase its stability at low concentrations while that to compound B will lead to a strong protein bond in plasma. It is concluded that compound A will not be stable in vivo because of a lack of stability in the extravascular space, and that the protein bond in plasma will be a measure of its in vivo stability.


1997 ◽  
Vol 36 (02) ◽  
pp. 71-75 ◽  
Author(s):  
S. Glatz ◽  
S. N. Reske ◽  
K. G. Grillenberger

Summary Aim: One therapeutic approach to rheumatoid arthritis and other inflammatory arthropathies besides surgical removal of inflamed synovium is radiation synovectomy using beta-emitting radionuclides to destroy the affected synovial tissue. Up to now the major problem associated with the use of labeled particles or colloids has been considerable leakage of radionuclides from the injected joint coupled with high radiation doses to liver and other non target organs. In this study we compared 188Re labeled hydroxyapatite particles and 188Re rhenium sulfur colloid for their potential use in radiation synovectomy. Methods: To this end we varied the labeling conditions (concentrations, pH-value, heating procedure) and analyzed the labeling yield, radiochemical purity, and in vitro stability of the resulting radiopharmaceutical. Results: After optimizing labeling conditions we achieved a labeling yield of more than 80% for 188Re hydroxyapatite and more than 90% for the rhenium sulfur colloid. Both of the radiopharmaceuticals can be prepared under aseptic conditions using an autoclav for heating without loss of activity. In vitro stability studies using various challenge solutions (water, normal saline, diluted synovial fluid) showed that 188Re labeled hydroxyapatite particles lost about 80% of their activity within 5 d in synovial fluid. Rhenium sulfur colloid on the other hand proved to be very stable with a remaining activity of more than 93% after 5 d in diluted synovial fluid. Conclusion: These in vitro results suggest that 188Re labeled rhenium sulfur colloid expects to be more suitable for therapeutic use in radiation synovectomy than the labeled hydroxyapatite particles.


1994 ◽  
Vol 21 (6) ◽  
pp. 893-895 ◽  
Author(s):  
Miklós Papós ◽  
Jenő Láng ◽  
Mária Rajtár ◽  
László Csernay

1979 ◽  
Vol 57 (6) ◽  
pp. 902-913 ◽  
Author(s):  
Patrick W. K. Lee ◽  
John S. Colter

Studies of the synthesis of viral ribonucleates and polypeptides in cells infected with two RNA−ts mutants of Mengo virus (ts 135 and ts 520) have shown that when ts 135 infected cells are shifted from the permissive (33 °C) to the nonpermissive (39 °C) temperature: (i) the synthesis of all three species of viral RNA (single stranded, replicative form, and replicative intermediate) is inhibited to about the same extent, and (ii) the posttranslational cleavage of structural polypeptide precursors A and B is partially blocked. Investigations of the in vivo and in vitro stability of the viral RNA replicase suggest that the RNA− phentotype reflects a temperature-sensitive defect in the enzyme. The second defect does not appear to result from the inhibition of viral RNA synthesis at 39 °C, since normal cleavage of polypeptides A and B occurs in wt Mengo-infected cells in which viral RNA synthesis is blocked by cordycepin, and at the nonpermissive temperature in ts 520 infected cells. Considered in toto, the evidence suggests that ts 135 is a double mutant.Subviral (53 S) particles have been shown to accumulate in ts 520 (but not ts 135) infected cells when cultures are shifted from 33 to 39 °C. This observation provides supporting evidence for the proposal that this recently discovered particle is an intermediate in the assembly pathway of Mengo virions.


2018 ◽  
Vol 56 (5) ◽  
pp. e121-e124 ◽  
Author(s):  
Pierre Bastin ◽  
Julien Favresse ◽  
Corentin Streel ◽  
Diane Maisin ◽  
Catherine Fillée ◽  
...  
Keyword(s):  

Author(s):  
Jasleen Kaur ◽  
Karim Arroub ◽  
Alexander Drzezga ◽  
Klaus Schomaecker ◽  
Sanjay Mathur

In this work, we describe the synthesis, in-vitro stability, and preliminary biological evaluation of [177Lu]Lu-DOTA-p160 peptide-based radiopharmaceuticals. Our findings highlight that all DOTA-p160-peptide radioconjugates exhibit favorable proteolytic and enzymatic stability...


Author(s):  
N. R. Anderson ◽  
J. Nicholas ◽  
M. R. Holland ◽  
R. Gama

Background: We investigated whether increased protease activity explains the increased in vitro degradation of intact parathyroid hormone (iPTH) observed in serum when compared to EDTA plasma. Methods: Pre-dialysis blood samples for iPTH were taken from 11 patients with chronic renal failure and collected into plain glass tubes, tubes containing 200 KIU/mL aprotinin (a protease inhibitor) and EDTA tubes. All sample aliquots were separated at 20 min, 1 h, 2 h, 4 h, 8 h and 24 h post collection. Results: Over 24 h, iPTH concentrations remained unchanged in EDTA tubes. iPTH concentrations were significantly lower in both plain tubes ( P < 0·01) and aprotinin tubes ( P < 0·001) at 24 h when compared to the baseline sample (20 min). At 24 h, iPTH concentrations in EDTA tubes were higher than in plain tubes ( P < 0·001) and aprotinin tubes ( P < 0·01). The addition of aprotinin to plain tubes significantly reduced the degradation of iPTH ( P < 0·05) at 24 h. Conclusion: Aprotinin significantly reduces the in vitro degradation of iPTH in plain tubes at 24 h from 24·7% to 9·6%. We suggest that increased protease activity contributes to the decline in serum iPTH over time. As this is observed in serum and not plasma it suggests that the increased protease activity may be due to the clotting process.


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