Immunohistochemical analysis of the distribution of histone H5 and hemoglobin during chicken development

Moorman, Antoon F.M.; Schalekamp, M.; Boer, Piet A. J. de; Geerts, Willie J. C.; Lamers, Wouter H.; Charles, Roger

doi:10.1111/j.1432-0436.1987.tb00063.x

Cited by 7 publications

(6 citation statements)

References 23 publications

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“…Therefore, histone H5 is not a suitable marker for the early primitive erythropoieric cells. Moorman et al (1987) also observed that the first signs of adult erythropoiesis were seen in the extraembryonic yolk sac stalk rather than in the embryo itself, indicating that chicken red blood cell formation is reminiscent of the amphibian and mammalian condition rather than being a unique avian process.…”

Section: Introductionmentioning

confidence: 89%

“…The specificity of the polyclonal adult and fetal a-globin antibodies have been described previously (Schalekamp & Van Goor, 1984;Moorman et al, 1987). Isolation and specificity tests of adult and fetal i~-globin subunits were carried out according to Schalekamp & Van Goor (1984) and are summarized below.…”

Section: Antibodiesmentioning

confidence: 99%

“…Serial sections of 7 ~tm were cut on a Spencer rotary microtome and attached to chromalum-coated slides and stored at -20~ until use. The incubation procedure has been described elsewhere (Moorman & De Boer, I985;Moorman et al, 1987). Endogenous peroxidase activity was GEERTS, LAMERS and M O O R M A N inhibited by a pre-incubation of 30 min in 3% HzO z in PBS.…”

Section: Immunohistochemistrymentioning

confidence: 99%

“…The adult ~-globin antibody was not used for the double-staining since previous investigations (Moorman et al, 1987) had shown that both primitive and definitive chicken erythrocytes contain the adult ~-globin subunit. Combinations of fetal 13-globin and adult 13-globin were not used because both antibodies were of mouse origin.…”

Section: Specificity Of the 13 Antibodiesmentioning

confidence: 99%

“…In a previous immunohistochemical study (Moorman et al, 1987) antibodies against the erythrocyte-specific histone H5 and the fetal and adult ~-globin subunits were used. It was shown that histone H5 is present in erythrocytes of both the primitive and definitive lineage.…”

Section: Introductionmentioning

confidence: 99%

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Differences in erythropoiesis in normal chicken and quail embryos

1993

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Using antibodies against the fetal and adult forms of alpha- and beta-globin, it has been shown that erythropoiesis in the para-aortic foci (PAF) constitutes a major species-specific difference between chicken and quail embryos. In quail embryos, para-aortic foci are rare, small and rather heterogeneous with regard to their erythropoietic and haemopoietic cell composition. In contrast, the PAFs in chicken embryos are abundant and consist of large numbers of erythropoietic cells. In both species a time difference (approximately 1 day) is observed between the first expression of the fetal alpha- and beta-globin and the adult alpha- and beta-globin in erythropoietic cells. Adult erythropoiesis in both species can be detected first in the stalk of the yolk sac; this is similar to the situation in mammalian and amphibian species. From this time onward the number of circulating adult erythrocytes increases steadily. Whereas in chicken, large intraembryonic foci that can serve as sources for these adult cells arise concomitantly, no such foci can be detected in quail embryos, suggesting that the quail yolk sac is a major source for these adult red blood cells.

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Section: Introductionmentioning

confidence: 89%

Section: Antibodiesmentioning

confidence: 99%

Section: Immunohistochemistrymentioning

confidence: 99%

Section: Specificity Of the 13 Antibodiesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Differences in erythropoiesis in normal chicken and quail embryos

1993

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Different localization of dystrophin in developing and adult human skeletal muscle

et al. 1991

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Duchenne and Becker muscular dystrophy are caused by defects in dystrophin synthesis. Using affinity-purified polyclonal anti-dystrophin antibodies, we have studied immunohistochemically the subcellular localization of dystrophin in embryonic, fetal, and adult human skeletal muscle. In the embryonic stages dystrophin first appears in the sarcoplasm at the peripheral ends of the myotubes, immediately adjacent to the tendons, whereas in fetal stages dystrophin is found throughout the entire myofibers. In agreement with literature data, in adult muscle dystrophin expression was found to be restricted to the sarcolemma. The sarcoplasmic localization in embryonic and fetal tissue and the sarcolemmal localization of dystrophin in mature muscle suggests the accumulation of dystrophin in the cytoplasm prior to its integration into the membrane. These results increase our knowledge of the ontogenesis of dystrophin and may lead to a better understanding of the great diversity in pathological cases of Duchenne and Becker muscular dystrophy.

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