Abstract
A large complex of proteins, called CENPs, are associated with centromeric DNA. Some of them exhibit a cell cycle-related expression (e.g., CENP-E and -F) and are required for the transition from interphase to mitosis, whereas constitutive proteins (e.g., CENP-A, -B, -C, -G, and -H) reside permanently at the centromere and are essential for the correct kinetochore assembly. Poly(ADP-ribose) polymerase-1 (PARP-1), which plays an active role in many basic processes, was described as a possible regulator of CENPs. By multicolor immunofluorescence we therefore analyzed the distribution of PARP-1 and its interaction with CENP-B, -E, and -F during mitosis and apoptosis.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Antibiotics, Antineoplastic / pharmacology
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Antineoplastic Agents, Phytogenic / pharmacology
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Apoptosis / drug effects
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Apoptosis / physiology*
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Cell Nucleus / metabolism
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Centromere Protein B / metabolism*
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Chromosomal Proteins, Non-Histone / metabolism*
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Cytoplasm / metabolism
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Dactinomycin / pharmacology
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Etoposide / pharmacology
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Fluorescent Antibody Technique
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HeLa Cells
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Humans
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Immunohistochemistry
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Microfilament Proteins / metabolism
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Microscopy, Confocal
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Microscopy, Fluorescence
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Mitosis / physiology*
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Poly (ADP-Ribose) Polymerase-1
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Poly(ADP-ribose) Polymerases / metabolism*
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Protein Binding
Substances
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Antibiotics, Antineoplastic
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Antineoplastic Agents, Phytogenic
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Centromere Protein B
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Chromosomal Proteins, Non-Histone
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Microfilament Proteins
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centromere protein E
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centromere protein F
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Dactinomycin
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Etoposide
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PARP1 protein, human
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Poly (ADP-Ribose) Polymerase-1
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Poly(ADP-ribose) Polymerases