Inhibition OF IgG-, F(ab′)2-and myeloma protein-induced erythrocyte aggregation, by small IgG-fragments

2016 ◽  
Vol 4 (4) ◽  
pp. 431-439
Author(s):  
Kazuhiko Imaizumi ◽  
Atsuko Imai ◽  
Tohru Maruyama ◽  
Takeshi Shiga
Keyword(s):  
Erythrocyte Aggregation ◽  
Myeloma Protein

The response of skin perfusion and of rheological and immunological variables to intravenous prostanoid administration in Raynaud’s phenomenon secondary to collagenosis

VASA ◽  
2005 ◽  
Vol 34 (4) ◽  
pp. 243-249 ◽  
Author(s):  
Drinda ◽  
Neumann ◽  
Pöhlmann ◽  
Vogelsang ◽  
Stein ◽  
...  
Keyword(s):  
Laser Doppler Flowmetry ◽  
Raynaud’S Phenomenon ◽  
Raynaud's Phenomenon ◽  
Plasma Viscosity ◽  
Laser Doppler ◽  
Erythrocyte Aggregation ◽  
Control Group ◽  
Long Term Effects ◽  
Doppler Flowmetry

Background: Prostanoids are used in the treatment of Raynaud’s phenomenon and acral perfusion disorders secondary to collagenosis. In subjective terms, intravenous administration of these agents produces success in more than 50% of patients. The therapeutic outcome of clinical administration of alprostadil or iloprost may vary from individual to individual. Patients and methods: The following variables were analysed in a cross-over study in 27 patients with collagenosis and Raynaud’s phenomenon: plasma viscosity and erythrocyte aggregation (rheological variables), partial pressure of oxygen and laser Doppler flowmetry in the finger region, and lymphocyte phenotyping and interleukin (IL) determinations (immunological variables). Results: Laser Doppler flowmetry revealed significant differences between patients with secondary Raynaud’s phenomenon and a control group of 25 healthy subjects. Laser Doppler readings did not change significantly as a result of the treatments. Therapy with iloprost produced a reduction in IL-1beta, L-selectin (CD 62 L) and IL-6. Conclusion: The change in immunological variables due to iloprost may explain the long-term effects of prostaglandins in the treatment of Raynaud’s phenomenon. From our results it is not possible to infer any preference for iloprost or alprostadil.

Bovine hypodermatosis in Stavropol region: distribution, pathogenesis, veterinary and sanitary assessment of slaughter products

2020 ◽  
pp. 7-10
Author(s):  
Vasiliy P. Petropavlovsky ◽  
◽  
Vyacheslav V. Marchenko ◽  
Lyudmila S. Vikulova ◽  
Olga D. Chepeleva ◽  
...  
Keyword(s):  
Preventive Measures ◽  
Climatic Conditions ◽  
The Body ◽  
Erythrocyte Aggregation ◽  
Economic Damage ◽  
Hydropic Degeneration ◽  
Hypoderma Lineatum ◽  
Hypoderma Bovis ◽  
Stavropol Region ◽  
Histomorphological Changes

Summary. Data on distribution of hypodermatosis among large horned cattle in Stavropol region are presented in the article. It was proved that this pathology is widespread in this region. From 12% to 38% of animals from the total number of examined livestock are affected. Ordinary subcutaneous botfly (stroma) Hypoderma bovis de Geer and south subcutaneous botfly (pischevodnik) Hypoderma lineatum de Villers parasites on large horned cattle. The species ratio of gadflies is: Hypoderma bovis (de Gee - 61.1%, Hypoderma lineatum de Villers - 38.9%). The disease is widespread in all climatic zones of Stavropol region. Animals of all age and sex groups are infected, but young animals are more often affected. Linear relationship between the indicators of the transformation of climatic conditions in Stavropol region, the spread of hypodermatosis and the timing of treatment and preventive measures were determined. Authors proved that the complete death of H. bovis and H. lineatum imago (regardless of the time of their hatching) was noted when the temperature drops to -3°C for two days. Thus, this temperature determines the start of treatment and preventive measures against hypodermatosis in the area of animal welfare. When analyzing the histomorphological changes caused by H. bovis and H. lineatum in the body of large horned cattle, perforation of the skin, swelling of adjacent tissues, disorganization of the stroma and structural elements, erythrocyte aggregation, hemorrhages, hydropic degeneration of cellular elements, tissue necrosis, polymorphonuclear leukocyte infiltration of affected organs and tissues were observed. The data on pathogenesis were presented, the analysis of economic damage and the veterinary and sanitary assessment of the products of slaughter of cattle with hypodermatosis were carried out.

Alcohol Intake and Erythrocyte Aggregation

1955 ◽  
Vol 16 (4) ◽  
pp. 614-618 ◽  
Author(s):  
O. Forsander ◽  
Heikki Suomalainen
Keyword(s):  
Alcohol Intake ◽  
Erythrocyte Aggregation

Methodological Aspects of Erythrocyte Aggregation

2007 ◽  
Vol 2 (3) ◽  
pp. 240-245 ◽  
Author(s):  
Alexander Pribush ◽  
Naomi Meyerstein
Keyword(s):  
Erythrocyte Aggregation ◽  
Methodological Aspects

Macroglobulinemia: The Usefulness of DL-Penicillamine and Paper Electrophoresis in Diagnosis

1964 ◽  
Vol 10 (7) ◽  
pp. 600-605 ◽  
Author(s):  
Donald J Campbell ◽  
Thomas Boenisch
Keyword(s):  
Paper Electrophoresis ◽  
Myeloma Protein

Abstract The change in mobility of an abnormal globulin peak during paper electrophoresis in the presence of DL-penicillamine is the most useful of simple procedures suggested for differentiation between macroglobulin and myeloma protein. However, not all cases indicating macroglobulin by this procedure will correlate with criteria based on ultracentrifuge analysis or antigenic reaction.

Erythrocyte aggregation: Bridging by macromolecules and electrostatic repulsion by sialic acid

1991 ◽  
Vol 1067 (2) ◽  
pp. 221-226 ◽  
Author(s):  
Yoji Izumida ◽  
Akitoshi Seiyama ◽  
Nobuji Maeda
Keyword(s):  
Sialic Acid ◽  
Erythrocyte Aggregation ◽  
Electrostatic Repulsion

Influence of acute-phase proteins on erythrocyte aggregation

Biorheology ◽  
1995 ◽  
Vol 32 (2-3) ◽  
pp. 218-218 ◽  
Author(s):  
X WENG ◽  
G CLOUTIER ◽  
R BEAULIEU
Keyword(s):  
Acute Phase ◽  
Acute Phase Proteins ◽  
Erythrocyte Aggregation

scholarly journals Anti-immunoglobulin antibodies. I. Expression of cross-reactive idiotypes and Ir gene control of the response to IgG2a of the b allotype.

1980 ◽  
Vol 151 (6) ◽  
pp. 1334-1348 ◽  
Author(s):  
C Bona ◽  
P K Mongini ◽  
K E Stein ◽  
W E Paul
Keyword(s):  
Poor Response ◽  
Domain Specificity ◽  
Gene Control ◽  
Constant Region ◽  
Myeloma Protein ◽  
Histocompatibility Complex ◽  
Heavy Chain Constant Region ◽  
Ch2 Domain ◽  
Ig Heavy Chain ◽  
Ir Genes

The anti-allotype antibody response to the b allotypic form of IgG2a is regulated by major histocompatibility complex (MHC)-encoded immune response (Ir) genes. Mice of d, b, p, q, r, and s haplotypes make a strong anti-allotype response on immunization with the CBPC101 myeloma protein (IgG2ab), whereas mice of the k, m, a, a1, u, and z haplotypes made no, or a very poor, response. All responder strains produce anti-IgG2ab antibodies which share common idiotypes (Id) without relation to the allelic forms of the Ig heavy-chain-constant region genes that the responding mice possess. Isoelectric focusing analysis of the anti-allotype antibodies produced in various strains of mice showed that they are of limited heterogeneity and quite similar from strain to strain. Five out of six hybridoma products with specificity for CBPC101 allotype expressed cross-reactive idiotypes (IdX). Two of hybridoma products expressing IdX identify CH3-domain determinants, and one has been assigned a CH2-domain specificity.

scholarly journals Characterization of the hydroxyproline-rich protein core of an arabinogalactan-protein secreted from suspension-cultured Lolium multiflorum (Italian ryegrass) endosperm cells

1989 ◽  
Vol 264 (3) ◽  
pp. 857-862 ◽  
Author(s):  
P A Gleeson ◽  
M McNamara ◽  
R E H Wettenhall ◽  
B A Stone ◽  
G B Fincher
Keyword(s):  
Polyclonal Antibodies ◽  
Lolium Multiflorum ◽  
Italian Ryegrass ◽  
Arabinogalactan Protein ◽  
Myeloma Protein ◽  
Protein Core ◽  
Liquid Suspension ◽  
Peptide Component ◽  
Immunodominant Epitopes

An arabinogalactan-protein (AGP) purified from the filtrate of liquid-suspension-cultured Italian-ryegrass (Lolium multiflorum) endosperm cells by affinity chromatography on myeloma protein J539-Sepharose was deglycosylated with trifluoromethanesulphonic acid to remove polysaccharide chains that are covalently associated with hydroxyproline residues in the peptide component of the proteoglycan. The protein core, which accounts for less than 10% (w/w) of the intact proteoglycan, was purified by h.p.l.c. It has an apparent Mr of 35,000, but reacts very poorly with both Coomassie Brilliant Blue R and silver stains. Amino-acid-sequence analysis of the N-terminus of the h.p.l.c.-purified protein core and of tryptic peptides generated from the unpurified protein reveals a high content of hydroxyproline and alanine. These are sometimes arranged in short (Ala-Hyp) repeat sequences of up to six residues. Polyclonal antibodies raised against the protein core do not cross-react with native AGP, the synthetic peptide (Ala-Hyp)4, poly-L-hydroxyproline or poly-L-proline. The results suggest that the polysaccharide chains in the native AGP render the protein core of the proteoglycan inaccessible to the antibodies and that the immunodominant epitopes include domains of the protein other than those rich in Ala-Hyp repeating units.

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