scholarly journals Biocompatibility and Toxicity of Poly(vinyl alcohol)/N,O-Carboxymethyl Chitosan Scaffold

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Tunku Kamarul ◽  
G. Krishnamurithy ◽  
Noman D. Salih ◽  
Nurul Syuhada Ibrahim ◽  
Hanumantha Rao Balaji Raghavendran ◽  
...  
Keyword(s):  
Total Protein ◽  
Protein A ◽  
Blood Parameters ◽  
Tissue Response ◽  
Poly Vinyl Alcohol ◽  
Inert Material ◽  
Inflammatory Infiltration ◽  
Histology And Immunohistochemistry ◽  
Toxic Tissue

The in vivo biocompatibility and toxicity of PVA/NOCC scaffold were tested by comparing them with those of a biocompatible inert material HAM in a rat model. On Day 5, changes in the blood parameters of the PVA/NOCC-implanted rats were significantly higher than those of the control. The levels of potassium, creatinine, total protein, A/G, hemoglobulin, erythrocytes, WBC, and platelets were not significantly altered in the HAM-implanted rats, when compared with those in the control. On Day 10, an increase in potassium, urea, and GGT levels and a decrease in ALP, platelet, and eosinophil levels were noted in the PVA/NOCC-implanted rats, when compared with control. These changes were almost similar to those noted in the HAM-implanted rats, except for the unaltered potassium and increased neutrophil levels. On Day 15, the total protein, A/G, lymphocyte, monocyte, and eosinophil levels remained unaltered in the PVA/NOCC-implanted rats, whereas urea, A/G, WBC, lymphocyte, and monocyte levels remained unchanged in the HAM-implanted rats. Histology and immunohistochemistry analyses revealed inflammatory infiltration in the PVA/NOCC-implanted rats, but not in the HAM-implanted rats. Although a low toxic tissue response was observed in the PVA/NOCC-implanted rats, further studies are necessary to justify the use of this material in tissue engineering applications.

scholarly journals In Vivo Investigation of Soft Tissue Response of Novel Silver/Poly(Vinyl Alcohol)/ Graphene and Silver/Poly(Vinyl Alcohol)/Chitosan/Graphene Hydrogels Aimed for Medical Applications – The First Experience

2018 ◽  
Vol 68 (3) ◽  
pp. 321-339 ◽  
Author(s):  
Tijana Lužajić Božinovski ◽  
Danica Marković ◽  
Vera Todorović ◽  
Bogomir Prokić Bolka ◽  
Ivan Milošević ◽  
...  
Keyword(s):  
Soft Tissue ◽  
Vinyl Alcohol ◽  
Subcutaneous Tissue ◽  
Tissue Response ◽  
Surrounding Tissue ◽  
Poly Vinyl Alcohol ◽  
Medical Applications ◽  
Capsule Thickness ◽  
Soft Tissue Response

Abstract In this paper, we have shown for the fi rst time the soft tissue response of novel silver/ poly(vinyl alcohol)/graphene (Ag/PVA/Gr) and silver/poly(vinyl alcohol)/chitosan/ graphene (Ag/PVA/CHI/Gr) nanocomposite hydrogels aimed for medical applications. These novel hydrogels were produced by in situ electrochemical synthesis of silver nanoparticles in the polymer matrices as described in our previously published works. Both Ag/PVA/Gr and Ag/PVA/CHI/Gr, as well as controls Ag/PVA, Ag/PVA/CHI and commercial Suprasorb©hydrogel discs, were implanted in the subcutaneous tissue of rats. Implants with the surrounding tissue were dissected after post-implantation on days 7, 15, 30 and 60, and then processed for histological examination. The tissue irritation index (TIrI) score, according to ISO 10993-6, 2007, as well as the number of leukocytes in the peri-implant zone and connective tissue capsule thickness were examined. The results show that each TIrI score, the leukocyte number around the implanted materials and capsule thickness gradually decreased during the observation period. At the endpoint of follow-up, the Ag/PVA/CHI/Gr implant was surrounded with a thinner capsule, while both the TIrI score and the number of leukocytes of the peri-implant zone were greater compared to the Ag/PVA/Gr implant. Despite the observed differences, we can conclude that our in vivo experiment suggested that both novel hydrogels were biocompatible and suitable for medical use.

scholarly journals Characterization of the SARS-CoV-2 coronavirus X4-like accessory protein

2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Olanrewaju Ayodeji Durojaye ◽  
Nkwachukwu Oziamara Okoro ◽  
Arome Solomon Odiba
Keyword(s):  
Rapid Development ◽  
Protein A ◽  
The Novel ◽  
Quality Model ◽  
A Value ◽  
Model Protein ◽  
Novel Coronavirus ◽  
Global Threat

Abstract Background The novel coronavirus SARS-CoV-2 is currently a global threat to health and economies. Therapeutics and vaccines are in rapid development; however, none of these therapeutics are considered as absolute cure, and the potential to mutate makes it necessary to find therapeutics that target a highly conserved regions of the viral structure. Results In this study, we characterized an essential but poorly understood coronavirus accessory X4 protein, a core and stable component of the SARS-CoV family. Sequence analysis shows a conserved ~ 90% identity between the SARS-CoV-2 and previously characterized X4 protein in the database. QMEAN Z score of the model protein shows a value of around 0.5, within the acceptable range 0–1. A MolProbity score of 2.96 was obtained for the model protein and indicates a good quality model. The model has Ramachandran values of φ = − 57o and ψ = − 47o for α-helices and values of φ = − 130o and ψ = + 140o for twisted sheets. Conclusions The protein data obtained from this study provides robust information for further in vitro and in vivo experiment, targeted at devising therapeutics against the virus. Phylogenetic analysis further supports previous evidence that the SARS-CoV-2 is positioned with the SL-CoVZC45, BtRs-BetaCoV/YN2018B and the RS4231 Bat SARS-like corona viruses.

In vivo behavior of trimethylene carbonate and ε-caprolactone-based (co)polymer networks: Degradation and tissue response

2010 ◽  
Vol 95A (3) ◽  
pp. 940-949 ◽  
Author(s):  
Erhan Bat ◽  
Josée A. Plantinga ◽  
Martin C. Harmsen ◽  
Marja J. A. van Luyn ◽  
Jan Feijen ◽  
...  
Keyword(s):  
Polymer Networks ◽  
Tissue Response ◽  
Trimethylene Carbonate

scholarly journals The Yeast Recombinational Repair Protein Rad59 Interacts With Rad52 and Stimulates Single-Strand Annealing

Genetics ◽  
2001 ◽  
Vol 159 (2) ◽  
pp. 515-525 ◽  
Author(s):  
Allison P Davis ◽  
Lorraine S Symington
Keyword(s):  
Protein A ◽  
Single Strand ◽  
Physical Interaction ◽  
Dna Double Strand Breaks ◽  
Single Stranded Dna ◽  
Single Strand Annealing ◽  
Strand Annealing ◽  
Recombination Pathway

Abstract The yeast RAD52 gene is essential for homology-dependent repair of DNA double-strand breaks. In vitro, Rad52 binds to single- and double-stranded DNA and promotes annealing of complementary single-stranded DNA. Genetic studies indicate that the Rad52 and Rad59 proteins act in the same recombination pathway either as a complex or through overlapping functions. Here we demonstrate physical interaction between Rad52 and Rad59 using the yeast two-hybrid system and co-immunoprecipitation from yeast extracts. Purified Rad59 efficiently anneals complementary oligonucleotides and is able to overcome the inhibition to annealing imposed by replication protein A (RPA). Although Rad59 has strand-annealing activity by itself in vitro, this activity is insufficient to promote strand annealing in vivo in the absence of Rad52. The rfa1-D288Y allele partially suppresses the in vivo strand-annealing defect of rad52 mutants, but this is independent of RAD59. These results suggest that in vivo Rad59 is unable to compete with RPA for single-stranded DNA and therefore is unable to promote single-strand annealing. Instead, Rad59 appears to augment the activity of Rad52 in strand annealing.

Imidazolidinyl urea activates mast cells via MRGPRX2 to induce non-histaminergic allergy

2021 ◽  
Author(s):  
Jiapan Gao ◽  
Delu Che ◽  
Xueshan Du ◽  
Yi Zheng ◽  
Huiling Jing ◽  
...  
Keyword(s):  
Contact Dermatitis ◽  
Mast Cells ◽  
Pharmaceutical Products ◽  
Drug Induced ◽  
Inflammatory Infiltration ◽  
Local Inflammatory Response ◽  
Allergic Contact ◽  
G Protein Coupled

Abstract Imidazolidinyl urea (IU) is used as an antimicrobial preservative in cosmetic and pharmaceutical products. IU induces allergic contact dermatitis, however, the mechanism has not yet been elucidated. Mas-related G protein-coupled receptor-X2 (MRGPRX2) triggers drug-induced pseudo-allergic reactions. The aims of this study were to determine whether IU activated mast cells through MRGPRX2 to further trigger contact dermatitis. Wild-type (WT) and KitW-sh/HNihrJaeBsmJNju (MUT) mice were treated with IU to observe its effects on local inflammation and mast cells degranulation in vivo. Laboratory of allergic disease 2 cells were used to detect calcium mobilization and release of inflammatory mediators in vitro. WT mice showed a severe local inflammatory response and contact dermatitis, whereas only slight inflammatory infiltration was observed in MUT mice. Thus, MRGPRX2 mediated the IU-induced activation of mast cells. However, histamine, a typical allergen, was not involved in this process. Tryptase expressed by mast cells was the major non-histaminergic inflammatory mediator of contact dermatitis. IU induced anaphylactic reaction via MRGPRX2 and further triggering non-histaminergic contact dermatitis, which explained why antihistamines are clinically ineffective against some chronic dermatitis.

scholarly journals Improvement of biohistological response of facial implant materials by tantalum surface treatment

2019 ◽  
Vol 41 (1) ◽  
Author(s):  
Mohammed Mousa Bakri ◽  
Sung Ho Lee ◽  
Jong Ho Lee
Keyword(s):  
Foreign Body ◽  
Soft Tissue ◽  
Surface Treatment ◽  
Clinical Applications ◽  
Tissue Response ◽  
Bone Surface ◽  
Tissue Thickness ◽  
Implant Materials ◽  
Soft Tissue Thickness

Abstract Background A compact passive oxide layer can grow on tantalum (Ta). It has been reported that this oxide layer can facilitate bone ingrowth in vivo though the development of bone-like apatite, which promotes hard and soft tissue adhesion. Thus, Ta surface treatment on facial implant materials may improve the tissue response, which could result in less fibrotic encapsulation and make the implant more stable on the bone surface. The purposes of this study were to verify whether surface treatment of facial implant materials using Ta can improve the biohistobiological response and to determine the possibility of potential clinical applications. Methods Two different and commonly used implant materials, silicone and expanded polytetrafluoroethylene (ePTFE), were treated via Ta ion implantation using a Ta sputtering gun. Ta-treated samples were compared with untreated samples using in vitro and in vivo evaluations. Osteoblast (MG-63) and fibroblast (NIH3T3) cell viability with the Ta-treated implant material was assessed, and the tissue response was observed by placing the implants over the rat calvarium (n = 48) for two different lengths of time. Foreign body and inflammatory reactions were observed, and soft tissue thickness between the calvarium and the implant as well as the bone response was measured. Results The treatment of facial implant materials using Ta showed a tendency toward increased fibroblast and osteoblast viability, although this result was not statistically significant. During the in vivo study, both Ta-treated and untreated implants showed similar foreign body reactions. However, the Ta-treated implant materials (silicone and ePTFE) showed a tendency toward better histological features: lower soft tissue thickness between the implant and the underlying calvarium as well as an increase in new bone activity. Conclusion Ta surface treatment using ion implantation on silicone and ePTFE facial implant materials showed the possibility of reducing soft tissue intervention between the calvarium and the implant to make the implant more stable on the bone surface. Although no statistically significant improvement was observed, Ta treatment revealed a tendency toward an improved biohistological response of silicone and ePTFE facial implants. Conclusively, tantalum treatment is beneficial and has the potential for clinical applications.

scholarly journals UV-induced Hyperphosphorylation of Replication Protein A Depends on DNA Replication and Expression of ATM Protein

2001 ◽  
Vol 12 (5) ◽  
pp. 1199-1213 ◽  
Author(s):  
Gregory G. Oakley ◽  
Lisa I. Loberg ◽  
Jiaqin Yao ◽  
Mary A. Risinger ◽  
Remy L. Yunker ◽  
...  
Keyword(s):  
Dna Replication ◽  
Uv Radiation ◽  
Excision Repair ◽  
Genetic Disorder ◽  
Protein A ◽  
Dna Recombination ◽  
Delayed Response ◽  
Replication Intermediates

Exposure to DNA-damaging agents triggers signal transduction pathways that are thought to play a role in maintenance of genomic stability. A key protein in the cellular processes of nucleotide excision repair, DNA recombination, and DNA double-strand break repair is the single-stranded DNA binding protein, RPA. We showed previously that the p34 subunit of RPA becomes hyperphosphorylated as a delayed response (4–8 h) to UV radiation (10–30 J/m2). Here we show that UV-induced RPA-p34 hyperphosphorylation depends on expression of ATM, the product of the gene mutated in the human genetic disorder ataxia telangiectasia (A-T). UV-induced RPA-p34 hyperphosphorylation was not observed in A-T cells, but this response was restored by ATM expression. Furthermore, purified ATM kinase phosphorylates the p34 subunit of RPA complex in vitro at many of the same sites that are phosphorylated in vivo after UV radiation. Induction of this DNA damage response was also dependent on DNA replication; inhibition of DNA replication by aphidicolin prevented induction of RPA-p34 hyperphosphorylation by UV radiation. We postulate that this pathway is triggered by the accumulation of aberrant DNA replication intermediates, resulting from DNA replication fork blockage by UV photoproducts. Further, we suggest that RPA-p34 is hyperphosphorylated as a participant in the recombinational postreplication repair of these replication products. Successful resolution of these replication intermediates reduces the accumulation of chromosomal aberrations that would otherwise occur as a consequence of UV radiation.

Diffusible amyloid oligomers trigger systemic amyloidosis in mice

2008 ◽  
Vol 415 (2) ◽  
pp. 207-215 ◽  
Author(s):  
Sivanesan Senthilkumar ◽  
Edwin Chang ◽  
Rajadas Jayakumar
Keyword(s):  
Protein A ◽  
Mouse Tissue ◽  
Cytokine Induction ◽  
Amyloidogenic Proteins ◽  
Enhancing Factor ◽  
Amyloid Oligomers ◽  
Apparent Relationship ◽  
Amyloid Enhancing Factor ◽  
Local Accumulation

AA (amyloid protein A) amyloidosis in mice is markedly accelerated when the animals are given, in addition to an inflammatory stimulus, an intravenous injection of protein extracted from AA-laden mouse tissue. Previous findings affirm that AA fibrils can enhance the in vivo amyloidogenic process by a nucleation seeding mechanism. Accumulating evidence suggests that globular aggregates rather than fibrils are the toxic entities responsible for cell death. In the present study we report on structural and morphological features of AEF (amyloid-enhancing factor), a compound extracted and partially purified from amyloid-laden spleen. Surprisingly, the chief amyloidogenic material identified in the active AEF was diffusible globular oligomers. This partially purified active extract triggered amyloid deposition in vital organs when injected intravenously into mice. This implies that such a phenomenon could have been inflicted through the nucleation seeding potential of toxic oligomers in association with altered cytokine induction. In the present study we report an apparent relationship between altered cytokine expression and AA accumulation in systemically inflamed tissues. The prevalence of serum AA monomers and proteolytic oligomers in spleen AEF is consistent to suggest that extrahepatic serum AA processing might lead to local accumulation of amyloidogenic proteins at the serum AA production site.

scholarly journals The Biological Effects of Combining Metals in a Posterior Spinal Implant: In Vivo Model Development Report of the First Two Cases

2014 ◽  
Vol 2014 ◽  
pp. 1-9 ◽  
Author(s):  
Christine L. Farnsworth ◽  
Peter O. Newton ◽  
Eric Breisch ◽  
Michael T. Rohmiller ◽  
Jung Ryul Kim ◽  
...  
Keyword(s):  
Galvanic Corrosion ◽  
Biological Effects ◽  
Model Development ◽  
Spinal Instrumentation ◽  
Pedicle Screws ◽  
Tissue Response ◽  
In Vivo Model ◽  
Particle Count ◽  
Spinal Implant

Study Design. Combinations of metal implants (stainless steel (SS), titanium (Ti), and cobalt chrome (CC)) were placed in porcine spines. After 12 months, tissue response and implant corrosion were compared between mixed and single metal junctions. Objective. Model development and an attempt to determine any detriment of combining different metals in posterior spinal instrumentation. Methods. Yucatan mini-pigs underwent instrumentation over five unfused lumbar levels. A SS rod and a Ti rod were secured with Ti and SS pedicle screws, SS and Ti crosslinks, SS and CC sublaminar wires, and Ti sublaminar cable. The resulting 4 SS/SS, 3 Ti/Ti, and 11 connections between dissimilar metals per animal were studied after 12 months using radiographs, gross observation, and histology (foreign body reaction (FBR), metal particle count, and inflammation analyzed). Results. Two animals had constructs in place for 12 months with no complications. Histology of tissue over SS/SS connections demonstrated 11.1 ± 7.6 FBR cells, 2.1 ± 1.7 metal particles, and moderate to extensive inflammation. Ti/Ti tissue showed 6.3 ± 3.8 FBR cells, 5.2 ± 6.7 particles, and no to extensive inflammation (83% extensive). Tissue over mixed components had 14.1 ± 12.6 FBR cells and 13.4 ± 27.8 particles. Samples surrounding wires/cables versus other combinations demonstrated FBR (12.4 ± 13.5 versus 12.0 ± 9.6 cells, P = 0.96), particles (19.8 ± 32.6 versus 4.3 ± 12.7, P = 0.24), and inflammation (50% versus 75% extensive, P = 0.12). Conclusions. A nonfusion model was developed to study corrosion and analyze biological responses. Although no statistical differences were found in overlying tissue response to single versus mixed metal combinations, galvanic corrosion between differing metals is not ruled out. This pilot study supports further investigation to answer concerns when mixing metals in spinal constructs.

scholarly journals Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus

2003 ◽  
Vol 31 (3) ◽  
pp. 716-718 ◽  
Author(s):  
N.G. Housden ◽  
S. Harrison ◽  
S.E. Roberts ◽  
J.A. Beckingham ◽  
M. Graille ◽  
...  
Keyword(s):  
Binding Sites ◽  
Protein A ◽  
Cell Wall Protein ◽  
Protein G ◽  
Protein L ◽  
Heavy Chains ◽  
Binding Domains ◽  
Peptostreptococcus Magnus ◽  
Immunoglobulin Binding

Protein L is a multidomain cell-wall protein isolated from Peptostreptococcus magnus. It belongs to a group of proteins that contain repeated domains that are able to bind to Igs without stimulating an immune response, the most characterized of this group being Protein A (Staphylococcus aureus) and Protein G (Streptococcus). Both of these proteins bind predominantly to the interface of CH2-CH3 heavy chains, while Protein L binds exclusively to the VL domain of the κ-chain. The function of these proteins in vivo is not clear but it is thought that they enable the bacteria to evade the host's immune system. Two binding sites for κ-chain on a single Ig-binding domain from Protein L have recently been reported and we give evidence that one site has a 25–55-fold higher affinity for κ-chain than the second site.

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