Chromatin structure and specificity revealed by immunological techniques

Bustin, Michael

doi:10.1016/0014-5793(76)80715-6

Cited by 29 publications

(6 citation statements)

References 64 publications

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“…The well-known relationship between troponin Ca 2+ affinity and cTnI phosphorylation at serine residues 22/23 led us to suspect elevated cTnI phosphorylation in Pkd 2+ / − hearts. 134 , 135 Western blots subsequently confirmed this hypothesis ( Fig. 4D ).…”

Section: Computational Modeling To Analyze Cardiomyocyte Maturationsupporting

confidence: 61%

Article Commentary: Prospects forIn VitroMyofilament Maturation in Stem Cell-Derived Cardiac Myocytes

Schwan

Campbell

2015

Biomark�Insights

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Cardiomyocytes derived from human stem cells are quickly becoming mainstays of cardiac regenerative medicine, in vitro disease modeling, and drug screening. Their suitability for such roles may seem obvious, but assessments of their contractile behavior suggest that they have not achieved a completely mature cardiac muscle phenotype. This could be explained in part by an incomplete transition from fetal to adult myofilament protein isoform expression. In this commentary, we review evidence that supports this hypothesis and discuss prospects for ultimately generating engineered heart tissue specimens that behave similarly to adult human myocardium. We suggest approaches to better characterize myofilament maturation level in these in vitro systems, and illustrate how new computational models could be used to better understand complex relationships between muscle contraction, myofilament protein isoform expression, and maturation.

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Section: Computational Modeling To Analyze Cardiomyocyte Maturationsupporting

confidence: 61%

Article Commentary: Prospects forIn VitroMyofilament Maturation in Stem Cell-Derived Cardiac Myocytes

Schwan

Campbell

2015

Biomark�Insights

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“…have been noted; e.g., the HI histones are both chemically and immunologically heterogeneous (Bustin & Stollar, 1972;Bustin, 1976). Antisera to HI histone subfractions showed little immunological correspondence between those of rat and calf thymus (Bustin & Stollar, 1973).…”

Section: Discussionmentioning

confidence: 99%

Cell-specific antigens in chicken erythroid nuclei: species specificity

Krajewska¹,

Briggs²,

Hnilica³

1979

Biochemistry

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Antisera raised to dehistonized chicken reticulocyte chromatin were tested for their cell and species specificity. Quantitative microcomplement fixation and immunohistochemical localization revealed the presence in chromatin of erythroid cell-specific nonhistone protein antigen(s). The antigenic specificity was shown to depend on the association of the antigenic protein(s) with deoxyribonucleic acid (DNA). Although the antisera were exceptionally cell specific, they cross-reacted with erythroid cells of other avian species. The extent of cross-reactivity was found to approximate the phylogenetic distances of the tested avian species. Erythroid cells from fish and amphibians were not reactive. Reconstitution experiments of partially purified chicken reticulocyte chromosomal nonhistone protein antigens with DNAs isolated from several vertebrate species showed that the species specificity of the antigenic complexes is determined principally by the species origin of the nonhistone proteins. Our results show that a cell-specific chromosomal nonhistone protein(s) has undergone evolutionary change and the relative immunological differences are consistent with the accepted phylogenetic distances of the species examined.

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“…Most immunochemical studies on the structure and function of chromatin have used histone antibodies as analytical probes (Bustin, 1976(Bustin, , 1978(Bustin, , 1979. Such studies are based on the principle that the accessibility of histones at the surface of chromatin can be revealed with antibodies directed against antigenic determinants (or epitopes) of histone molecules.…”

Section: Introductionmentioning

confidence: 99%

“…© IRL Press Ltd., Oxford, England. 0261-4189/82/0104-0421$2.00.0 al., 1976;Absolom and Van Regenmortel, 1977). Since a 10-fold molar excess of peptide CN3 over intact H3 inhibited the binding in the H3 -anti H3 reaction by 8307, the antigenic activity of this fragment seemed particularly well preserved, and the corresponding epitope appeared a good candidate for further immunochemical investigations.…”

Section: Introductionmentioning

confidence: 99%

Immunochemical localization of the C-terminal hexapeptide of histone H3 at the surface of chromatin subunits.

Muller¹,

Himmelspach²,

Regenmortel³

1982

The EMBO Journal

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The C‐terminal hexapeptide of histone H3 of chicken erythrocytes (residues 130‐135) corresponding to the sequence Ile‐Arg‐Gly‐Glu‐Arg‐Ala (IRGERA) was prepared by solid‐phase peptide synthesis and, after coupling to bovine serum albumin, was used to elicit antibodies in rabbits. The antigenic activity of the synthetic peptide IRGERA was found to be very similar to that of the natural CN3 fragment (residues 121‐135), and it inhibited the H3‐anti H3 reaction in complement fixation, solid‐phase radioimmunoassay, and enzyme‐linked immunosorbent assay. Antibodies induced by IRGERA were found to bind equally well to IRGERA coupled to hemocyanin, to the intact H3 molecule, and to chromatin subunits (nucleosomes and core particles). The results demonstrate that the C‐terminal hexapeptide of histone H3 is located at the surface of chromatin subunits and agree with current models proposed for the spatial organization of the chromatin core particle.

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Chromatin structure and specificity revealed by immunological techniques

Cited by 29 publications

References 64 publications

Article Commentary: Prospects forIn VitroMyofilament Maturation in Stem Cell-Derived Cardiac Myocytes

Article Commentary: Prospects forIn VitroMyofilament Maturation in Stem Cell-Derived Cardiac Myocytes

Cell-specific antigens in chicken erythroid nuclei: species specificity

Immunochemical localization of the C-terminal hexapeptide of histone H3 at the surface of chromatin subunits.

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