Immunochemical properties of embryonic and adult specific antigens of chicken erythrocytes

Krsmanovic, V.; Jp, Blanchet; Greenland, Timothy; Aupoix, M.

doi:10.1016/0014-4827(79)90401-4

Cited by 14 publications

(7 citation statements)

References 16 publications

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“…The monoclonal antibody against CFA8 (clone 190-4) has already been shown to immunoprecipitate a cell surface molecule of approximately 50,000 daltons molecular weight [24]. This is similar to 48,000-dalton-molecular-weight precipitates previously described for the chicken embryonic antigen system [30,31]. Recent results indicated that QFA and CFA are carried on many of the same cell surface molecules in the Japanese quail [32].…”

Section: Discussionmentioning

confidence: 74%

Avian developmental antigens: Expression on erythrocytes of chickens, Japanese quail, and quail‐chicken hybrids

1984

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Monoclonal and polyclonal antibodies were used to examine the expression of three erythroid developmental antigen systems in the chicken, Japanese quail, and quail‐chicken hybrid. Chicken fetal antigen (CFA), quail fetal antigen (QFA), and chicken adult antigen (CAA) each represent a series of cell‐surface glycorproteins associated with the development of avian hematopoietic cells. Monoclonal anti‐CFA antibodies from clones 190‐4 and 288‐1.1.1.2 supernatants were shown to react against epitopes associated with CFA determinants 8 and 2, respectively. Using complement‐mediated microcytotoxicity, these reagents permitted the identification of different erythroid subpopulations in the neonatal chicken and hybrid; therefore, heterogeneity in cell surface CFA determinants among mature peripheral erythrocytes should serve as a useful tool for analyzing erythroid development. In the case of CAA, erythrocytes from adult hybrids were found to express the same complement of CAA determinants identified in the chicken, and CAA appeared much earlier in the hybrid than in either of the parental species. Similarly, two species‐restricted fetal antigens associated with similar glycoproteins, CFA8 and QFA, had similar developmental profiles in their respective species, the chicken and quail. In contrast, these antigens were dominantly expressed but exhibited different developmental profiles on erythrocytes from the hybrids. While quail‐chicken hybrids exhibited apparent genomic interactions in the expression of these developmental antigens, no evidence for the existence of hybrid‐specific fetal antigens was obtained.

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Section: Discussionmentioning

confidence: 74%

Avian developmental antigens: Expression on erythrocytes of chickens, Japanese quail, and quail‐chicken hybrids

1984

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“…V 8 protease concentrations were a, d 0.25 I~g/ml; b, e 1.25 t~g/ ml; or c, f, g--j 10 ~g/ml. The stacking gel, in which 1 mM EDTA was included, contained 3 per cent acrylamide and the separating gel 14 per cent embryo erythroeytes (22). However, in order to prevent cell differentiation, the erythroleukemia cells transformed with the ts 34AEV mutant maintained at the nonpermissive temperature in the absence of anemic chicken serum showed no migration change for embryo-immature 50 kDa antigens (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The antiserum to embryonic chicken erythrocytcs (anti-E serum) was raised in rabbits and absorbed as previously described (5,22). This serum precipitates from homologous erythroeytes a 48,000 Da glycoprotein composed of a major component referred to as Im48 kDa antigen, expressed Mso on immature adult erythroid cells, and a minor component peculiar to embryonic erythroeytes referred to as E~ 48 kDa antigen (24).…”

Section: Seramentioning

confidence: 99%

“…The 14C-methylated MW markers used, i.e., myosin (200 kDa), phosphorylase b (92 kDa), Mbumin (69 kDa), ovalbumin (46 kDa), carbonic anhydrase (30 kDa), and lysozyme (14 kDa) were supplied by Amersham l~adiochemical Centre, U.K. After migration the gels were stained, destained and dried (22), then autoradiographed using X-Omat films and Dupont Lightning-Plus intensifying screens. Excised bands from dried gels, containing 125I-tabelled molecules were subjected to partial hydrolysis by V 8 protease from Staphylococcus anreus (Miles), as described by Cr~EVELAND et al (8).…”

Section: Immune Precipitation and Partial Proteolysismentioning

confidence: 99%

“…l0 s cells were surface-labelled with lesI (0.3 mCi) by the method of MoRisox (28), as described previously (22). The iodinated cell membranes were dissociated by resuspending the cells in 1 ml of RIPA buffer (7) containing 150 m~I NaC1, 10 mM Tris-HC1 pH 7.2, 1 per cent Triton X-100, 1 per cent sodium desoxycholate, 0.1 per cent SDS and 1 per cent Aprotinin (Sigma) as protease inhibitor.…”

Section: Preparation Of Radio-labelled Antigensmentioning

confidence: 99%

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AEV-transformed erythroleukemia cell induced differentiation: Expression of specific cell membrane antigenic molecules

Raynaud

Biquard²,

Chambard

et al. 1987

Archives of Virology

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A simultaneous decay of the expression of Im 140 kDa, Im 150 kDa and Im 160 kDa high MW membrane antigens, concomitant with the cell proliferation arrest, was observed during erythropoietin induced differentiation of ts 34 AEV-transformed erythroid cells cultivated at the restrictive temperature. Expression of embryo-immature antigens was maintained during induced differentiation of erythroleukemia cells, but their MW shifted from 50 to 48 kDa, which corresponds to the MW of embryo-immature antigens detected on normal erythroid cells. In the absence of erythropoietin at the restrictive temperature, conditions under which the ts 34 AEV-transformed erythroid cells fail to differentiate and maintain their capacity to proliferate, the expression of high MW antigens as well as the expression of embryo-immature antigens remained unaffected. Therefore, it is shown that the expression of specific membrane antigens is modulated under conditions rendering the erythroleukemia cell differentiation process possible.

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The chicken erythrocyte-specific MHC antigen. Characterization and purification of the B-G antigen by monoclonal antibodies

et al. 1987

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Mouse monoclonal antibodies with B-G antigen (major histocompatibility complex class IV) specificity were obtained after immunization with erythrocytes or partially purified B-G antigen. The specificities of the hybridoma antibodies were determined by precipitation of B-G antigens from 125I-labeled chicken erythrocyte membranes (CEM) followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and autoradiography. The B-G antigen had an approximate molecular mass of 46-48 kd in reduced samples, depending on the haplotype, and in unreduced samples contained either dimers (85 kd), when labeled erythrocytes were the antigen source, or trimers (130 kd), when B-G was purified and precipitated from CEM. The B-G antigen was unglycosylated as studied by in vitro synthesis in the presence or absence of tunicamycin, binding experiments with lectin from Phaseolus limensis, and treatment of purified B-G antigen with Endoglycosidase-F or trifluoromethanesulfonic acid. Two-way sequential immunoprecipitation studies of erythrocyte membrane extracts with anti-B-G alloantisera and monoclonal antibodies revealed only one population of B-G molecules. Pulse-chase experiments have shown B-G to be synthesized as a monomer, with dimerization taking place after 20-30 min. No change in the monomer's molecular mass due to posttranslational modifications was revealed. The antigen was purified from detergent extract of CEM by affinity chromatography with a monoclonal antibody, and then reduced and alkylated and affinity-purified once more. Finally, reverse-phase chromatography resulted in a pure product. The B-G antigen was identified in the various fractions by rocket immunoelectrophoresis. The final product was more than 99% pure, as estimated by SDS-PAGE analysis followed by silver stain of proteins. The yield from the affinity chromatography step was 3-4 micrograms B-G/ml blood, calculated from Coomassie-stained SDS-PAGE of B-G using ovalbumin standards. The monoclonal antibodies were also used to identify the B-G (class IV) precipitation arc in crossed immunoelectrophoresis. No common precipitate with the B-F (class I) antigen was observed.

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Immunochemical properties of embryonic and adult specific antigens of chicken erythrocytes

Cited by 14 publications

References 16 publications

Avian developmental antigens: Expression on erythrocytes of chickens, Japanese quail, and quail‐chicken hybrids

Avian developmental antigens: Expression on erythrocytes of chickens, Japanese quail, and quail‐chicken hybrids

AEV-transformed erythroleukemia cell induced differentiation: Expression of specific cell membrane antigenic molecules

The chicken erythrocyte-specific MHC antigen. Characterization and purification of the B-G antigen by monoclonal antibodies

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