Comparative Immunochemical Study of Human Erythrocyte Glycoproteins

Lee, L. T.; Janney, F A; Deas, Judith; Howe, Calderón

doi:10.3181/00379727-158-40240

Cited by 3 publications

(2 citation statements)

References 7 publications

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“…In addition, both antisera were found to contain high titers of agglutinins for erythrocytes of groups A, B, and O(H). These agglutinins were active at both 37 and 40C and were not inhibited by highly purified and potent blood group substances from extra-erythrocytic sources (16). Part of this broadly specific agglutinin response was CA reactive with human erythrocytes but not with rabbit erythrocytes.…”

Section: Discussionmentioning

confidence: 92%

Cold hemagglutinin cross-reactivity with Mycoplasma pneumoniae

Janney¹,

Lee²,

Howe³

1978

Infect Immun

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Convalescent sera from proven cases of infection with Mycoplasma pneumoniae, and rabbit antisera to M. pneumoniae and to human erythrocyte glycoprotein contained cold hemagglutinins which were reactive only for human erythrocytes. Only the human serum cold agglutinins were inhibited by soluble integral glycoproteins derived from human erythrocyte ghosts by treatment with chloroform-methanol. Rabbit antiserum to chloroform-methanol glycoprotein, as well as to M. pneumoniae, fixed complement with either M. pneumoniae or chloroform-methanol glycoprotein antigens. The findings support the hypothesis that the cold agglutinins elicited by M. pneumoniae infection represent a cross-reaction between determinants common to erythrocyte glycoprotein containing I antigen and the membrane of M. pneumoniae.Cold agglutinins (CA) which appear in the serum during the course of human infection with Mycoplasma pneumoniae have specificity for the I antigen, the determinants) of which involve N-acetylneuraminic acid (6,20). The I specificity is detectable in glycoproteins solubilized from erythrocyte membranes by any of several procedures (15) and in various body fluids. These soluble I-like substances display considerable heterogeneity as judged by immunochemical analysis with anti-I sera from patients with the chronic "cold agglutinin syndrome" unrelated to infection with M. pneumoniae. The mechanism by which CA are elicited by M. pneumoniae has not yet been clearly defined. We present further evidence which suggests that early (immunoglobulin M [IgM]) CA antibody evoked by M. pneumoniae is crossreactive with native erythrocyte antigens which share determinants with M. pneumoniae. MATERIALS AND METHODS M. pneumoniae, The FH strain of M. pneumoniae was obtained through the courtesy of William Mogabgab, Tulane University School of Medicine. It had been isolated in embryonated eggs from the sputum of a patient with CA-positive pneumonia (18) and was subsequently maintained in broth and agar media as described by Chanock et al. (2). The organism was grown in bulk by the method of Somerson et al. (23) in 5-liter Povitsky bottles containing 300 ml of broth.After inoculation, bottles were incubated at 37°C until a confluent sheet of colonies had attached to the surface, usually within a period of 3 to 5 days, during which the pH of the medium dropped to ca. 6.5. The broth was decanted and discarded. The sheet of organisms adherent to the glass was washed three times with phosphate-buffered saline, pH 7.2 and scraped into phosphate-buffered saline with a rubber policeman. The organisms were washed three times more in phosphate-buffered saline by alternate centrifugation at 800 x g for 30 min and resuspension, and finally resuspended to the desired concentration and stored at -70'C until used. Colony counts of M. pneumoniae were done by the method of Kim et al. (14).Antigens for complement fixation (CF) tests. Water-soluble glycoproteins were obtained by treatment of human erythrocyte ghosts with chloroform-methanol (CM) (9). The product of...

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Section: Discussionmentioning

confidence: 92%

Cold hemagglutinin cross-reactivity with Mycoplasma pneumoniae

Janney¹,

Lee²,

Howe³

1978

Infect Immun

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“…The increased levels of hexadecanoylcarnitine, hexadecenoylcarnitine, octadecanoylcarnitine, and oleoylcarnitine (Table S2A) likely relate to energy metabolism and fatty acid oxidation. The increase of ribose and nicotinamine may relate to pentose phosphate cycle and glycohydrolysis. − The increase in ornithine and the decrease in arginine may result from erythrocyte arginase activity . The increase of glutamate and aspartate could be the result of glutaminase and asparaginase activities, and the increase of normetanephrine levels may be related to erythrocyte catechol- O -methyltransferase (COMT) activity. , The observed increase in sphingolipid metabolites may be due to release from platelets and erythrocytes or due to lysophospholipase activity of autaxin. , However, Scherer et al found increases in certain sensitive metabolites, such as lysophosphatidic acid, also in dependence on the extraction method .…”

Section: Discussionmentioning

confidence: 99%

An Integrated Analysis of Metabolites, Peptides, and Inflammation Biomarkers for Assessment of Preanalytical Variability of Human Plasma

et al. 2019

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Discrepancies in blood sample collection and processing could have a significant impact on levels of metabolites, peptides, and protein biomarkers of inflammation in the blood; thus, sample quality control is critical for successful biomarker identification and validation. In this study, we analyzed the effects of several preanalytical processing conditions, including different storage times and temperatures for blood or plasma samples and different centrifugation forces on the levels of metabolites, peptides, and inflammation biomarkers in human plasma samples using ethylenediaminetetraacetic acid (EDTA) as an anticoagulant. Temperature was found to be the major factor for metabolite variation, and both time and temperature were identified as major factors for peptide variation. For inflammation biomarkers, temperature played different roles depending on the sample type (blood or plasma). Low temperature affected inflammation biomarkers in blood, while room temperature impacted inflammation biomarkers in plasma.

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Immunochemical studies on Tn erythrocyte glycoprotein

Lt¹,

Frank²,

Jongh³

et al. 1981

Blood

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Glycoproteins were extracted from membranes of erythrocytes that displayed Tn polyagglutination and were compared chemically and immunologically with glycoproteins of group O, MN cells. Tn glycoprotein had lower than normal NANA : protein and sugar : protein ratios, as revealed by direct analysis and polyacrylamide gel electrophoresis, and displayed slower immunoelectrophoretic mobility than glycoproteins of group O, MN cells. Agglutination of Tn cells by Salvia sclarea lectin was inhibited by Tn glycoprotein but not by O, MN glycoprotein. Tn and MN glycoproteins were equally potent inhibitors of influenza virus HA. Our findings indicate than Tn-specific determinants are part of the glycophorin molecule.

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Comparative Immunochemical Study of Human Erythrocyte Glycoproteins

Cited by 3 publications

References 7 publications

Cold hemagglutinin cross-reactivity with Mycoplasma pneumoniae

Cold hemagglutinin cross-reactivity with Mycoplasma pneumoniae

An Integrated Analysis of Metabolites, Peptides, and Inflammation Biomarkers for Assessment of Preanalytical Variability of Human Plasma

Immunochemical studies on Tn erythrocyte glycoprotein

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