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Gréen, Anna
Alternative names
Publications (10 of 10) Show all publications
Sandestig, A., Gréen, A., Jonasson, J., Vogt, H., Wahlström, J., Pepler, A., . . . Stefanova, M. (2019). Could Dissimilar Phenotypic Effects of ACTB Missense Mutations Reflect the Actin Conformational Change?: Two Novel Mutations and Literature Review. Molecular Syndromology, 9(5), 259-265
Open this publication in new window or tab >>Could Dissimilar Phenotypic Effects of ACTB Missense Mutations Reflect the Actin Conformational Change?: Two Novel Mutations and Literature Review
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2019 (English)In: Molecular Syndromology, ISSN 1661-8769, E-ISSN 1661-8777, Vol. 9, no 5, p. 259-265Article in journal (Refereed) Published
Abstract [en]

The beta-actin gene encodes 1 of 6 different actin proteins. De novo heterozygous missense mutations in ACTB have been identified in patients with Baraitser-Winter syndrome (BRWS) and also in patients with developmental disorders other than BRWS, such as deafness, dystonia, and neutrophil dysfunction. We describe 2 different novel de novo missense ACTB mutations, c.208Camp;gt;G (p.Pro70Ala) and c.511Camp;gt;T (p.Leu171Phe), found by trio exome sequencing analysis of 2 unrelated patients: an 8-year-old boy with a suspected BRWS and a 4-year-old girl with unclear developmental disorder. The mutated residue in the first case is situated in the actin H-loop, which is involved in actin polymerization. The mutated residue in the second case (p.Leu171Phe) is found at the actin barbed end in the W-loop, important for binding to profilin and other actin-binding molecules. While the boy presented with a typical BRWS facial appearance, the girl showed facial features not recognizable as a BRWS gestalt as well as ventricular arrhythmia, cleft palate, thrombocytopenia, and gray matter heterotopia. We reviewed previously published ACTB missense mutations and ascertained that a number of them do not cause typical BRWS. By comparing clinical and molecular data, we speculate that the phenotypic differences found in ACTB missense mutation carriers might supposedly be dependent on the conformational change of ACTB.

Place, publisher, year, edition, pages
S. Karger, 2019
Keywords
ACTB gene; Actin; Baraitser-Winter syndrome; Missense mutation; Protein conformational change; Residue position
National Category
Medical Genetics
Identifiers
urn:nbn:se:liu:diva-156000 (URN)10.1159/000492267 (DOI)000456100700007 ()30733661 (PubMedID)2-s2.0-85052719319 (Scopus ID)
Available from: 2019-04-01 Created: 2019-04-01 Last updated: 2019-04-09Bibliographically approved
Smol, T., Petit, F., Piton, A., Keren, B., Sanlaville, D., Afenjar, A., . . . Ghoumid, J. (2018). MED13L-related intellectual disability: involvement of missense variants and delineation of the phenotype. Neurogenetics, 19(2), 93-103
Open this publication in new window or tab >>MED13L-related intellectual disability: involvement of missense variants and delineation of the phenotype
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2018 (English)In: Neurogenetics, ISSN 1364-6745, E-ISSN 1364-6753, Vol. 19, no 2, p. 93-103Article in journal (Refereed) Published
Abstract [en]

Molecular anomalies in MED13L, leading to haploinsufficiency, have been reported in patients with moderate to severe intellectual disability (ID) and distinct facial features, with or without congenital heart defects. Phenotype of the patients was referred to "MED13L haploinsufficiency syndrome." Missense variants in MED13L were already previously described to cause the MED13L-related syndrome, but only in a limited number of patients. Here we report 36 patients with MED13L molecular anomaly, recruited through an international collaboration between centers of expertise for developmental anomalies. All patients presented with intellectual disability and severe language impairment. Hypotonia, ataxia, and recognizable facial gestalt were frequent findings, but not congenital heart defects. We identified seven de novo missense variations, in addition to protein-truncating variants and intragenic deletions. Missense variants clustered in two mutation hot-spots, i.e., exons 15-17 and 25-31. We found that patients carrying missense mutations had more frequently epilepsy and showed a more severe phenotype. This study ascertains missense variations in MED13L as a cause for MED13L-related intellectual disability and improves the clinical delineation of the condition.

Place, publisher, year, edition, pages
SPRINGER, 2018
Keywords
MED13L; Intellectual disability; Mediator complex; Cardiopathy
National Category
Medical Genetics
Identifiers
urn:nbn:se:liu:diva-148255 (URN)10.1007/s10048-018-0541-0 (DOI)000432523600003 ()29511999 (PubMedID)
Available from: 2018-06-04 Created: 2018-06-04 Last updated: 2019-05-02
Gréen, A., Green, H., Rehnberg, M., Svensson, A., Gunnarsson, C. & Jonasson, J. (2015). Assessment of HaloPlex Amplification for Sequence Capture and Massively Parallel Sequencing of Arrhythmogenic Right Ventricular Cardiomyopathy-Associated Genes. Journal of Molecular Diagnostics, 17(1), 31-42
Open this publication in new window or tab >>Assessment of HaloPlex Amplification for Sequence Capture and Massively Parallel Sequencing of Arrhythmogenic Right Ventricular Cardiomyopathy-Associated Genes
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2015 (English)In: Journal of Molecular Diagnostics, ISSN 1525-1578, E-ISSN 1943-7811, Vol. 17, no 1, p. 31-42Article in journal (Refereed) Published
Abstract [en]

The genetic basis of arrhythmogenic right ventricular cardiomyopathy (ARVC) is complex. Mutations in genes encoding components of the cardiac desmosomes have been implicated as being causally related to ARVC. Next-generation sequencing allows parallel sequencing and duplication/deletion analysis of many genes simultaneously, which is appropriate for screening of mutations in disorders with heterogeneous genetic backgrounds. We designed and validated a next-generation sequencing test panel for ARVC using HaloPlex. We used SureDesign to prepare a HaloPlex enrichment system for sequencing of DES, DSC2, DSG2, DSP, JUP, PKP2, RYR2, TGFB3, TMEM43, and TIN from patients with ARVC using a MiSeq instrument. Performance characteristics were determined by comparison with Sanger, as the gold standard, and TruSeq Custom Amplicon sequencing of DSC2, DSG2, DSP, JUP, and PKP2. All the samples were successfully sequenced after HaloPlex capture, with greater than99% of targeted nucleotides covered by greater than20x. The sequences were of high quality, although one problematic area due to a presumptive context-specific sequencing error causing motif Located in exon 1 of the DSP gene was detected. The mutations found by Sanger sequencing were also found using the HaloPlex technique. Depending on the bioinformatics pipeline, sensitivity varied from 99.3% to 100%, and specificity varied from 99.90/0 to 100%. Three variant positions found by Sanger and HaloPlex sequencing were missed by TruSeq Custom Amplicon owing to Loss of coverage.

Place, publisher, year, edition, pages
Elsevier, 2015
National Category
Basic Medicine Cardiac and Cardiovascular Systems
Identifiers
urn:nbn:se:liu:diva-113731 (URN)10.1016/j.jmoldx.2014.09.006 (DOI)000347143100006 ()25445213 (PubMedID)
Available from: 2015-01-30 Created: 2015-01-29 Last updated: 2018-01-11
Gréen, A., Sarg, B., Green, H., Lönn, A., Lindner, H. H. & Rundquist, I. (2011). Histone H1 interphase phosphorylation becomes largely established in G(1) or early S phase and differs in G(1) between T-lymphoblastoid cells and normal T cells. EPIGENETICS and CHROMATIN, 4(15)
Open this publication in new window or tab >>Histone H1 interphase phosphorylation becomes largely established in G(1) or early S phase and differs in G(1) between T-lymphoblastoid cells and normal T cells
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2011 (English)In: EPIGENETICS and CHROMATIN, ISSN 1756-8935, Vol. 4, no 15Article in journal (Refereed) Published
Abstract [en]

Background: Histone H1 is an important constituent of chromatin, and is involved in regulation of its structure. During the cell cycle, chromatin becomes locally decondensed in S phase, highly condensed during metaphase, and again decondensed before re-entry into G(1). This has been connected to increasing phosphorylation of H1 histones through the cell cycle. However, many of these experiments have been performed using cell-synchronization techniques and cell cycle-arresting drugs. In this study, we investigated the H1 subtype composition and phosphorylation pattern in the cell cycle of normal human activated T cells and Jurkat T-lymphoblastoid cells by capillary electrophoresis after sorting of exponentially growing cells into G(1), S and G(2)/M populations. less thanbrgreater than less thanbrgreater thanResults: We found that the relative amount of H1.5 protein increased significantly after T-cell activation. Serine phosphorylation of H1 subtypes occurred to a large extent in late G(1) or early S phase in both activated T cells and Jurkat cells. Furthermore, our data confirm that the H1 molecules newly synthesized during S phase achieve a similar phosphorylation pattern to the previous ones. Jurkat cells had more extended H1.5 phosphorylation in G(1) compared with T cells, a difference that can be explained by faster cell growth and/or the presence of enhanced H1 kinase activity in G(1) in Jurkat cells. less thanbrgreater than less thanbrgreater thanConclusion: Our data are consistent with a model in which a major part of interphase H1 phosphorylation takes place in G(1) or early S phase. This implies that H1 serine phosphorylation may be coupled to changes in chromatin structure necessary for DNA replication. In addition, the increased H1 phosphorylation of malignant cells in G(1) may be affecting the G(1)/S transition control and enabling facilitated S-phase entry as a result of relaxed chromatin condensation. Furthermore, increased H1.5 expression may be coupled to the proliferative capacity of growth-stimulated T cells.

Place, publisher, year, edition, pages
BioMed Central, 2011
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-71559 (URN)10.1186/1756-8935-4-15 (DOI)000295461100001 ()
Note
Funding Agencies|Austrian Science Foundation| I23-B03 |EC Sixth Framework Programme| ERAS-CT-2003-980409 |Swedish Cancer Society||Available from: 2011-10-21 Created: 2011-10-21 Last updated: 2011-10-24
Trinks, C., Severinsson, E. A., Holmlund, B., Gréen, A., Green, H., Jönsson, J.-I., . . . Walz, T. (2011). The pan-ErbB tyrosine kinase inhibitor canertinib induces caspase-mediated cell death in human T-cell leukemia (Jurkat) cells. Biochemical and Biophysical Research Communications - BBRC, 410(3), 422-427
Open this publication in new window or tab >>The pan-ErbB tyrosine kinase inhibitor canertinib induces caspase-mediated cell death in human T-cell leukemia (Jurkat) cells
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2011 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 410, no 3, p. 422-427Article in journal (Refereed) Published
Abstract [en]

Canertinib is a novel ErbB-receptor inhibitor currently in clinical development for the treatment of solid tumors overexpressing ErbB-receptors. We have recently demonstrated that canertinib displays anti-proliferative and pro-apoptotic effects in human myeloid leukemia cells devoid of ErbB-receptors. The mechanism mediating these effects are however unknown. In this study, we show that canertinib is able to act as a multi-kinase inhibitor by inhibition of several intracellular kinases involved in T-cell signaling such as Akt, Erk1/2 and Zap-70, and reduced Lck protein expression in the human T-cell leukemia cell line Jurkat. Treatment with canertinib at a concentration of 2 mu M caused accumulation of Jurkat cells in the G(1) cell cycle phase and increased doses induced apoptosis in a time-dependent manner. Apoptotic signs of treated cells were detected by Annexin V staining and cleavage of PARP, caspase-3, -8, -9, -10 and Bid. A subset of the pro-apoptotic signals mediated by canertinib could be significantly reduced by specific caspase inhibitors. Taken together, these results demonstrate the dual ability of canertinib to downregulate important signaling pathways and to activate caspase-mediated intrinsic apoptosis pathway in human T-cell leukemia cells.

Place, publisher, year, edition, pages
Elsevier Science B.V., Amsterdam, 2011
Keywords
T-cell leukemia; Canertinib; ErbB-receptor; Apoptosis; Caspase; Intracellular signaling
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-69797 (URN)10.1016/j.bbrc.2011.05.148 (DOI)000292797700009 ()
Available from: 2011-08-10 Created: 2011-08-08 Last updated: 2017-12-08
Gréen,, A., Lönn, A., Holmgren Peterson, K., Öllinger, K. & Rundquist, I. (2010). Translocation of Histone H1 Subtypes Between Chromatin and Cytoplasm During Mitosis in Normal Human Fibroblasts. Cytometry Part A, 77A(5), 478-484
Open this publication in new window or tab >>Translocation of Histone H1 Subtypes Between Chromatin and Cytoplasm During Mitosis in Normal Human Fibroblasts
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2010 (English)In: Cytometry Part A, ISSN 1552-4922, E-ISSN 1552-4930, Vol. 77A, no 5, p. 478-484Article in journal (Refereed) Published
Abstract [en]

Histone H1 is an important constituent of chromatin which undergoes major structural rearrangements during mitosis. However, the role of H1, multiple H1 subtypes and H1 phosphorylation is still unclear. In normal human fibroblasts, phosphorylated H1 was found located in nuclei during prophase and in both cytoplasm and condensed chromosomes during metaphase, anaphase and telophase as detected by immunocytochemistry. Moreover, we detected remarkable differences in the distribution of the histone H1 subtypes H1.2, H1.3 and H1.5 during mitosis. H1.2 was found in chromatin during prophase, and almost solely in the cytoplasm of metaphase and early anaphase cells. In late anaphase it appeared in both chromatin and cytoplasm, and again in chromatin during telophase. H1.5 distribution pattern resembled that of H1.2, but some H1.5 remained situated in chromatin during metaphase and early anaphase. H1.3 was detected in chromatin in all cell cycle phases. We propose therefore, that H1 subtype translocation during mitosis is controlled by phosphorylation, in combination with H1 subtype inherent affinity. We conclude that H1 subtypes, or their phosphorylated variants, may be signalling molecules in mitosis or that they leave chromatin in a regulated way to give access for chromatin condensing factors or transcriptional regulators during mitosis.

Place, publisher, year, edition, pages
John Wiley & Sons, 2010
Keywords
Histone H1, Chromatin, Cell cycle, Mitosis
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-16383 (URN)10.1002/cyto.a.20851 (DOI)000277174000009 ()20104577 (PubMedID)
Available from: 2009-01-20 Created: 2009-01-20 Last updated: 2017-12-14Bibliographically approved
Gréen, A. (2009). Histone H1: Subtypes and phosphorylation in cell life and death. (Doctoral dissertation). Linköping: Linköping University Electronic Press
Open this publication in new window or tab >>Histone H1: Subtypes and phosphorylation in cell life and death
2009 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The genetic information of a human diploid cell is contained within approximately 2 metres of linear DNA. The DNA molecules are compacted and organized in various ways to fit inside the cell nucleus. Various kinds of histones are involved in this compaction. One of these histones, histone H1 is the topic of the present thesis. In addition to its structural role, H1 histones have been implicated in various processes, for example gene regulation and inhibition of chromatin replication.

H1 histones, also termed linker histones, are relatively conserved proteins, and the various subtypes seem to have different and important functions even though redundancy between the subtypes has been demonstrated. Despite the sequence conservation of H1 subtypes, two sequence variations were detected within the H1.2 and H1.4 subtypes using hydrophilic interaction liquid chromatographic separation of H1 proteins from K562 and Raji cell lines in Paper I in the present thesis. The variations were confirmed by genetic analysis, and the H1.2 sequence variation was also found in genomic DNA of normal blood donors, in an allele frequency of 6.8%. The H1.4 sequence variation was concluded to be Raji specific. The significance of H1 microsequence variants is unclear, since the physiological function of H1 histones remains to be established.

H1 histones can be phosphorylated at multiple sites. Changes in H1 phosphorylation has been detected in apoptosis, the cell cycle, gene regulation, mitotic chromatin condensation and malignant transformation. Contradictory data have been obtained on H1 phosphorylation in apoptosis, and many results indicate that H1 dephosphorylation occurs during apoptosis. We and others hypothesized that cell cycle effects by the apoptosis inducers may have affected previous studies. In Paper II, the H1 phosphorylation pattern was investigated in early apoptosis in Jurkat cells, taking cell cycle effects into account. In receptor-mediated apoptosis, apoptosis occurs with a mainly preserved phosphorylation pattern, while Camptothecin induced apoptosis results in rapid dephosphorylation of H1 subtypes, demonstrating that H1 dephosphorylation is not a general event in apoptosis, but may occur upon apoptosis induction via the mitochondrial pathway. The dephosphorylation may also be a result of early cell cycle effects or signalling.Therefore, the H1 phosphorylation pattern in the cell cycle of normal activated T cells was investigated in Paper IV in this thesis. Some studies, which have been made using cancer cell lines from various species and cell synchronization, have indicated a sequential addition of phosphate groupsacross the cell cycle. Normal T cells and cell sorting by flow cytometry were used to circumvent side-effects from cell synchronization. The data demonstrate that a pattern with phosphorylated serines is established in late G1/early S phase, with some additional phosphorylation occurring during S, and further up-phosphorylation seems to occur during mitosis. Malignant transformation may lead to an altered G1 H1 phosphorylation pattern, as was demonstrated using sorted Jurkat T lymphoblastoid cells.

During mitosis, certain H1 subtypes may be relocated to the cytoplasm. In Paper III, the location of histones H1.2, H1.3 and H1.5 during mitosis was investigated. Histone H1.3 was detected in cell nuclei in all mitotic stages, while H1.2 was detected in the nucleus during prophase and telophase, and primarily in the cytoplasm during metaphase and early anaphase. H1.5 was located mostly to chromatin during prophase and telophase, and to both chromatin and cytoplasm during metaphase and anaphase. Phosphorylated H1 was located in chromatin in prophase, and in both chromatin and cytoplasm during metaphase, anaphase and telophase, indicating that the mechanism for a possible H1 subtype relocation to the cytoplasm is phosphorylation.

In conclusion, data obtained during this thesis work suggest that H1 histones and their phosphorylation may participate in the regulation of events in the cell cycle, such as S-phase progression and mitosis, possibly through altered interactions with chromatin, and/or by partial or complete removal of subtypes or phosphorylated variants from chromatin.

Place, publisher, year, edition, pages
Linköping: Linköping University Electronic Press, 2009. p. 97
Series
Linköping University Medical Dissertations, ISSN 0345-0082 ; 1086
National Category
Cell Biology
Identifiers
urn:nbn:se:liu:diva-15925 (URN)978-91-7393-757-3 (ISBN)
Public defence
2009-01-16, Berzeliussalen, Hälsouniversitetet, Linköpings Universitet, Linköping, 09:00 (English)
Opponent
Supervisors
Available from: 2009-01-20 Created: 2008-12-16 Last updated: 2009-06-24Bibliographically approved
Gréen, A., Sarg, B., Koutzamani, E., Genheden, U., Lindner, H. H. . & Rundquist, I. (2008). Histone H1 Dephosphorylation Is Not a General Feature in Early Apoptosis. Biochemistry, 47, 7539-7547
Open this publication in new window or tab >>Histone H1 Dephosphorylation Is Not a General Feature in Early Apoptosis
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2008 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 47, p. 7539-7547Article in journal (Refereed) Published
Abstract [en]

Histone H1 is a family of nucleosomal proteins that exist in a number of subtypes. These subtypes can be modified after translation in various ways, above all by phosphorylation. Increasing levels of H1 phosphorylation has been correlated with cell cycle progression, while both phosphorylation and dephosphorylation of histone H1 have been linked to the apoptotic process. Such conflicting results may depend on which various apoptosis-inducing agents cause apoptosis via different apoptotic pathways and often interfere with cell proliferation. Therefore, we investigated the relation between apoptosis and H1 phosphorylation in Jurkat cells after apoptosis induction via both the extrinsic and intrinsic pathways and by taking cell cycle effects into account. After apoptosis induction by anti-Fas, no significant dephosphorylation, as measured by capillary electrophoresis, or cell cycle-specific effects were detected. In contrast, H1 subtypes were rapidly dephosphorylated when apoptosis was induced by camptothecin. We conclude that histone H1 dephosphorylation is not connected to apoptosis in general but may be coupled to apoptosis by the intrinsic pathway or to concomitant growth inhibitory signaling.

Place, publisher, year, edition, pages
ACS Publications, 2008
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-16382 (URN)10.1021/bi702311x (DOI)
Available from: 2009-01-20 Created: 2009-01-20 Last updated: 2017-12-14Bibliographically approved
Sarg, B., Gréen, A. ., Söderkvist, P., Helliger, W. ., Rundquist, I. . & Lindner, H. H. . (2005). Characterization of sequence variations in human histone H1.2 and H1.4 subtypes. The FEBS Journal, 272(14), 3673 -3683
Open this publication in new window or tab >>Characterization of sequence variations in human histone H1.2 and H1.4 subtypes
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2005 (English)In: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658, Vol. 272, no 14, p. 3673 -3683Article in journal (Refereed) Published
Abstract [en]

In humans, eight types of histone H1 exist (H1.1–H1.5, H1°, H1t and H1oo), all consisting of a highly conserved globular domain and less conserved N- and C-terminal tails. Although the precise functions of these isoforms are not yet understood, and H1 subtypes have been found to be dispensable for mammalian development, it is now clear that specific functions may be assigned to certain individual H1 subtypes. Moreover, microsequence variations within the isoforms, such as polymorphisms or mutations, may have biological significance because of the high degree of sequence conservation of these proteins. This study used a hydrophilic interaction liquid chromatographic method to detect sequence variants within the subtypes. Two deviations from wild-type H1 sequences were found. In K562 erythroleukemic cells, alanine at position 17 in H1.2 was replaced by valine, and, in Raji B lymphoblastoid cells, lysine at position 173 in H1.4 was replaced by arginine. We confirmed these findings by DNA sequencing of the corresponding gene segments. In K562 cells, a homozygous GCC→GTC shift was found at codon 18, giving rise to H1.2 Ala17Val because the initial methionine is removed in H1 histones. Raji cells showed a heterozygous AAA→AGA codon change at position 174 in H1.4, corresponding to the Lys173Arg substitution. The allele frequency of these sequence variants in a normal Swedish population was found to be 6.8% for the H1.2 GCC→GTC shift, indicating that this is a relatively frequent polymorphism. The AAA→AGA codon change in H1.4 was detected only in Raji cells and was not present in a normal population or in six other cell lines derived from individuals suffering from Burkitt's lymphoma. The significance of these sequence variants is unclear, but increasing evidence indicates that minor sequence variations in linker histones may change their binding characteristics, influence chromatin remodeling, and specifically affect important cellular functions.

Place, publisher, year, edition, pages
Wiley InterScience, 2005
Keywords
HILIC, linker histones, sequence variants, SNP, tumor cell lines
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-16381 (URN)10.1111/j.1742-4658.2005.04793.x (DOI)
Available from: 2009-01-20 Created: 2009-01-20 Last updated: 2017-12-14Bibliographically approved
Gréen, A., Sarg, B., Gréen, H., Lönn, A., Lindner, H. & Rundquist, I.Histone H1 interphase phosphorylation pattern becomes largely established during G1/S transition in proliferating cells.
Open this publication in new window or tab >>Histone H1 interphase phosphorylation pattern becomes largely established during G1/S transition in proliferating cells
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(English)Manuscript (Other academic)
Abstract [en]

Histone H1 is an important constituent of chromatin, and is believed to be involved in regulation of chromatin structure. During the cell cycle, chromatin becomes locally decondensed in S phase, highly condensed during metaphase and again decondensed before re-entry into G1. This has been connected to increasing phosphorylation of H1 histones during the cell cycle. However, many of these experiments have been performed in non-human and human cancer   cell lines, and by the use of cell synchronization techniques and cell cycle-arresting drugs. In this study, we have investigated the H1 subtype composition and phosphorylation pattern in the cell cycle. Exponentially growing normal human activated T cells and Jurkat lymphoblastoid cells were sorted by fluorescence activated cell sorting into G1, S and G2/M populations, without the use of cell cycle arresting drugs. We found that the H1.5 protein level increased after T-cell activation. Our data indicate that serine phosphorylation of H1 subtypes occurred to a large extent in late G1 phase or early S, while some additional serine phosphorylation took place during S, G2 and M phases. Furthermore, our data suggest that the newly synthesized H1 molecules during S phase also achieve a similar phosphorylation pattern as the previous ones. Jurkat cells showed more extended H1.5 phosphorylation in G1 compared with T cells, a difference that can be explained by faster cell growth and/or the presence of enhanced H1 kinase activity in G1 in Jurkat cells. In conclusion, our data is consistent with a model where a major part of interphase H1 serine phosphorylation takes place within a narrow time window during the G1/Stransition. This implies that H1 serine phosphorylation may be coupled to changes in chromatin structure necessary for DNA replication.

National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-16384 (URN)
Available from: 2009-01-20 Created: 2009-01-20 Last updated: 2010-01-14Bibliographically approved
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