Identification of a nuclear and of a cytoplasmic polypeptide whose relative proportions are sensitive to changes in the rate of cell proliferation

Bravo, Rodrigo; Fey, Stephen J.; Bellatin, Jaime; Larsen, Peter Mose; Arévalo, Jorge; Celis, Julio E.

doi:10.1016/0014-4827(81)90009-4

Cited by 202 publications

(96 citation statements)

References 17 publications

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“…It is an acidic, non-histone nuclear protein with an apparent isoelectric point of 4.8-4.9 and molecular mass of 33-36 kDa (Bravo et al, 1981;Mathews et al, 1984;Takasaki et al ., 1984). PCNA was finally identified as an auxiliary protein for DNA polymerase δ (Tan et al ., 1986;Bravo et al ., 1987;Prelich et al, 1987).…”

Section: Introductionmentioning

confidence: 99%

PCNA Protein Expression during Spermatogenesis of the Japanese Eel (Anguilla japonica)

Miura

Yamashita

2002

Zoological Science

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-Spermatogenesis can be initiated by a single injection of human chorionic gonadotropin (hCG) into the cultivated Japanese eel, which produces only spermatogonia in the testis. To isolate the genes responsible for regulating spermatogenesis, we performed a differential mRNA display using poly (A) + RNA extracted from the testes at different time points after hCG injection. Among several cDNA clones, the expression of which was initiated before the onset of meiosis, one clone has high homology with the proliferating cell nuclear antigen (PCNA). In this study, we investigated the protein expression of eel PCNA and found for the first time in any species that two forms (32-kDa and 36-kDa) of PCNA are present in the testis. Although the 36-kDa form existed in both the testis and spleen, the 32-kDa form was specifically expressed in the testis. In contrast to the appearance of 36-kDa PCNA 1 day after the hCG treatment, the 32-kDa PCNA appeared only 9 days after the hCG treatment, at which time active spermatogonial proliferation occurred in the testis. Both the 32-and 36-kDa forms were recognized by antibodies raised against different epitopes of PCNA, and their N-terminal amino acid sequences were identical. The 36-kDa form, but not the 32-kDa form, was recognized by antibodies against phosphoamino acids. These results suggest that the two PCNA proteins are the same molecule with different chemical modifications, including phosphorylation. We discuss the roles of these two forms of PCNA in the spermatogenesis of the Japanese eel.

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Section: Introductionmentioning

confidence: 99%

PCNA Protein Expression during Spermatogenesis of the Japanese Eel (Anguilla japonica)

Miura

Yamashita

2002

Zoological Science

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“…Lower labelling appeared at the time of close reciprocal pronuclei contact (late S-phase). It (Bravo et al, 1981 Localization but not synthesis of cyclin/PCNA was found to be dependent on DNA replication (Bravo and Macdonald-Bravo, 1985 …”

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confidence: 99%

Immunocytochemical localization of cyclin/proliferating cell nuclear antigen (PCNA) in fertilized eggs of mice

Baran¹,

Veselá²,

Rehák³

et al. 1992

Reprod. Nutr. Dev.

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Summary ― lmmunolocalization of cyclin/PCNA (proliferating cell nuclear antigen) was performed with monoclonal antibody using immunogold methods on ultrathin cryosections of fertilized mouse eggs. lmmunolabeling in pronuclei was checked 20, 22, 24 and 26 h after HCG injection. A relation between onset of pronuclei migration (early S-phase) and appearance of colloidal particle clusters was found. Afterwards, (mid S-phase) the increase of labelling and the localization of cyclin/PCNA were found throughout the pronuclei, except in the nucleolar bodies. Lower labelling appeared at the time of close reciprocal pronuclei contact (late S-phase). It is concluded that bulk and distribution of cyclin/PCNA in pronuclei is closely related to the progression of first interphase after fertilization.

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“…The six tropomyosin isoforms Tml through Tm6, numbered by the convention of Matsumura and colleagues (25,(27)(28)(29) and Franza and Garrels (7) were identified, when present, along with two abundant unidentified polypeptides, a and b, that migrated to the same isoelectric point (pI, -4.5) and molecular weight range (Mr, 30,000 to 38,000). Polypeptide b may have been the antigenic nuclear polypeptide cyclin (3,7).…”

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confidence: 99%

Tropomyosin isoform switching in tumorigenic human fibroblasts.

Leavitt¹,

Latter²,

Lutomski³

et al. 1986

Mol. Cell. Biol.

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We identified six tropomyosin (Tm) isoforms in diploid human fibroblasts. We used computerized microdensitometry of 2-dimensional protein profiles to measure the relative rates of synthesis and abundance of the individual Tm isoforms and actin, the two major structural constituents of microfilaments. In carcinogen-transformed human fibroblasts (HuT-14), the rates of synthesis of three Tm isoforms (Tml, Tm2, and Tm6) were greatly decreased relative to normal diploid parental fibroblasts and to actin. In contrast, related nontumorigenic HuT fibroblasts which are "immortalized" and anchorage independent exhibited both slight down-regulation of Tml and Tm6 and 3.5-fold up-regulation of Tm3. Thus, Tm isoform switching from the predominance of the larger more avid Tm isoforms (Tml, Tm2, Tm3, and Tm6) to the smaller, less avid Tm isoforms (Tm4 and TmS) in microfilaments was a transformation-induced change correlated with tumorigenicity in human fibroblasts.

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Identification of a nuclear and of a cytoplasmic polypeptide whose relative proportions are sensitive to changes in the rate of cell proliferation

Cited by 202 publications

References 17 publications

PCNA Protein Expression during Spermatogenesis of the Japanese Eel (Anguilla japonica)

PCNA Protein Expression during Spermatogenesis of the Japanese Eel (Anguilla japonica)

Immunocytochemical localization of cyclin/proliferating cell nuclear antigen (PCNA) in fertilized eggs of mice

Tropomyosin isoform switching in tumorigenic human fibroblasts.

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