Effect of Metrizamide, a Nonionic Radiographic Contrast Agent, on Human Serum Complement

1984 ◽  
Vol 73 (4) ◽  
pp. 321-329 ◽  
Author(s):  
I. von Zabern ◽  
H. Przyklenk ◽  
R. Nolte ◽  
W. Vogt
Keyword(s):  
Contrast Agent ◽  
Human Serum ◽  
Serum Complement ◽  
Radiographic Contrast

Contrast Nephrotoxicity: A Randomized Controlled Trial of a Nonionic and an Ionic Radiographic Contrast Agent

1989 ◽  
Vol 320 (3) ◽  
pp. 149-153 ◽  
Author(s):  
Steve J. Schwab ◽  
Mark A. Hlatky ◽  
Karen S. Pieper ◽  
Charles J. Davidson ◽  
Kenneth G. Morris ◽  
...  
Keyword(s):  
Randomized Controlled Trial ◽  
Contrast Agent ◽  
Controlled Trial ◽  
Randomized Controlled ◽  
Radiographic Contrast ◽  
Contrast Nephrotoxicity

Effect of Different Sulfonamides on the Human Serum Complement System

1985 ◽  
Vol 76 (3) ◽  
pp. 205-213 ◽  
Author(s):  
I. von Zabern ◽  
R. Nolte ◽  
H. Przyklenk ◽  
W. Vogt
Keyword(s):  
Human Serum ◽  
Complement System ◽  
Serum Complement

Maghemite-human serum albumin hybrid nanoparticles: towards a theranostic system with high MRI r2* relaxivity

2016 ◽  
Vol 4 (21) ◽  
pp. 3801-3814 ◽  
Author(s):  
Rivka Ben Ishay ◽  
Liron L. Israel ◽  
Esthy Levy Eitan ◽  
David M. Partouche ◽  
Jean-Paul Lellouche
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Contrast Agent ◽  
Human Serum ◽  
Hybrid Nanoparticles ◽  
Diagnostic Applications

Magnetic hybrid human serum albumin-based NPs were successfully fabricated, disclosing a powerful T2* contrast agent for dual therapeutic and diagnostic applications.

The mechanisms of activation of normal human serum complement byEscherichia coli strains with K1 surface antigen

2006 ◽  
Vol 51 (6) ◽  
pp. 627-632 ◽  
Author(s):  
G. Bugla-Płoskońska ◽  
A. Cisowska ◽  
K. Karpińska ◽  
S. Jankowski ◽  
W. Doroszkiewicz
Keyword(s):  
Human Serum ◽  
Surface Antigen ◽  
Normal Human Serum ◽  
Serum Complement ◽  
Normal Human ◽  
Byescherichia Coli

scholarly journals Human serum albumin nanoparticles loaded with phthalocyanine dyes for potential use in photodynamic therapy for atherosclerotic plaques

2019 ◽  
Vol 2 (2) ◽  
pp. 279-302 ◽  
Author(s):  
Subhadeep Banerjee ◽  
Jayeeta Sengupta ◽  
Ana Isabel Aljarilla ◽  
Francesca Setaro ◽  
Petri Makinen ◽  
...  
Keyword(s):  
Photodynamic Therapy ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Contrast Agent ◽  
Human Serum ◽  
Zinc Phthalocyanine ◽  
Atherosclerotic Plaques ◽  
Albumin Nanoparticles ◽  
Vulnerable Plaques ◽  
Potential Use

Diseases caused by obstruction or rupture of vulnerable plaques in the arterial walls such as cardiovascular infarction or stroke are the leading cause of death in the world. In the present work, we developed human serum albumin nanoparticles loaded by physisorption with zinc phthalocyanine, TT1, mainly used for industrial application as near-infrared photosensitizer and compared these to HSA NPs loaded with the well-known silicone phthalocyanine (Pc4). The use of NIR light allows for better tissue penetration, while the use of nanoparticles permits high local concentrations. The particles were characterized and tested for toxicity and stability as well as for their potential use as a contrast agent and NIR photosensitizer for photodynamic therapy in cardiovascular disease. We focused on the distribution of the nanoparticles in RAW264.7 macrophage cells and atherosclerotic mice. The nanoparticles had an average size of 120 nm according to dynamic light scattering, good loading capacity for zinc phthalocyanine, and satisfying stability in 50% (v/v) fetal bovine serum for 8 hours and in an aqueous environment at 4°C for 4–6 weeks. Under light irradiation we found a high production of singlet oxygen and the products showed no dark toxicity in vitro with macrophages (the target cells in vulnerable plaques), but at a low g/mL nanoparticle concentration killed efficiently the macrophages upon LED illumination. Injection of the contrast agent in atherosclerotic mice led to a visible fluorescence signal of zinc phthalocyanine in the atherosclerotic plaque at 30 minutes and in the lungs with a fast clearance of the nanoparticles. Zinc phthalocyanine loaded human serum albumin nanoparticles present an interesting candidate for the visualization and potentially photodynamic treatment of macrophages in atherosclerotic plaques.

scholarly journals Identification of complement activation sites in human immunodeficiency virus type-1 glycoprotein gp120

Blood ◽  
1996 ◽  
Vol 87 (6) ◽  
pp. 2329-2336 ◽  
Author(s):  
C Susal ◽  
M Kirschfink ◽  
M Kropelin ◽  
V Daniel ◽  
G Opelz
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Serum ◽  
Complement Activation ◽  
Classical Pathway ◽  
Serum Complement ◽  
Gp120 Sequence ◽  
Immunodeficiency Virus ◽  
Glycoprotein Gp120 ◽  
Hiv 1

Recombinant glycoprotein 120 (rgp120) of human immunodeficiency virus type-1 (HIV-1) activates the human complement system in the absence of anti-gp120 antibodies. HIV-1 glycoprotein gp120 can dissociate from the viral envelope either spontaneously or after binding of HIV-1 to the CD4 molecule. As a consequence, gp120 can circulate in the patient's serum and attach to the surface of uninfected CD4+ T cells. Complement activation by cell-bound HIV-1 glycoprotein gp120 with subsequent opsonization may represent a mechanism for the elimination of uninfected CD4+ cells by the reticuloendothelial system, thereby enhancing the progression of HIV disease. In the current study, the complement proteins C4,C3,C5,C9, and properdin were found to bind to a synthetic peptide covering positions 233–251 of the gp120BRU sequence on incubation with normal human serum. Complement activation by the peptide was comparable with that induced by aggregated IgG, complete rgp120, and the previously described complement-activating gp41-peptide 609y623. Activation occurred via the classical pathway and was abrogated in the presence of EDTA, Mg2+/EGTA, or C4-deficient human serum. Peptides partly overlapping the sequence 233–251 activated complement to a lesser extent. The complement-activating capacity of the gp120 sequence 233–251 was not restricted to the HIV-1BRU isolate, because a peptide from the corresponding sequence of the HIV-1MN strain was also capable of activating complement. An additional strong complement-activating site was identified in the gp120 sequence 321–360 of the HIV-1MN strain. These data indicate that distinct sites in gp120 are able to activate human serum complement via the classical pathway in the absence of anti-gp120 and independent of glycosylation.

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