Anne Carine Østvold

• Østvold, Anne Carine; Grundt, Kirsten & Wiese, Claudia (2022). NUCKS1 is a highly modified, chromatin-associated protein involved in a diverse set of biological and pathophysiological processes. Biochemical Journal. ISSN 0264-6021. 479(11), p. 1205–1220. doi: 10.1042/BCJ20220075.
• De Angelis, Paula; Schjølberg, Aasa Rambæk; Hughes, Juliana Bentes; Huitfeldt, Henrik; Andersen, Solveig Norheim & Østvold, Anne Carine (2018). Nondysplastic ulcerative colitis has high levels of the homologous recombination repair protein NUCKS1 and low levels of the DNA damage marker gamma-H2AX. Inflammatory Bowel Diseases. ISSN 1078-0998. 24(3), p. 593–600. doi: 10.1093/ibd/izx071. Full text in Research Archive
• Grundt, Kirsten; Thiede, Bernd & Østvold, Anne Carine (2017). Identification of kinases phosphorylating 13 sites in the nuclear, DNA-binding protein NUCKS. Biochimica et Biophysica Acta - Proteins and Proteomics. ISSN 1570-9639. 1865(3), p. 359–369. doi: 10.1016/j.bbapap.2016.12.009.
• Yue, Yangbo; Leung, Stanley G.; Liu, Yueyong; Huang, Yurong; Grundt, Kirsten & Østvold, Anne Carine [Show all 10 contributors for this article] (2016). Nucks1 synergizes with Trp53 to promote radiation lymphomagenesis in mice. OncoTarget. ISSN 1949-2553. 7(38), p. 61874–61889. doi: 10.18632/oncotarget.11297.
• Parplys, Ann C.; Zhao, Weixing; Sharma, Neelam; Groesser, Torsten; Liang, Fengshan & Maranon, David G. [Show all 14 contributors for this article] (2015). NUCKS1 is a novel RAD51AP1 paralog important for homologous recombination and genome stability. Nucleic Acids Research (NAR). ISSN 0305-1048. 43(20), p. 9817–9834. doi: 10.1093/nar/gkv859.
• Drosos, Yiannis; Kouloukoussa, Mirsini; Østvold, Anne Carine; Havaki, Sophia; Katsantoni, Eleni & Marinos, Evangelos [Show all 7 contributors for this article] (2014). Dynamic expression of the vertebrate-specific protein Nucks during rodent embryonic development. Gene Expression Patterns. ISSN 1567-133X. 14(1), p. 19–29. doi: 10.1016/j.gep.2013.10.001.
• Drosos, Y; Kouloukoussa, M; Østvold, Anne Carine; Grundt, Kirsten; Goutas, N & Vlachodimitropoulos, D [Show all 11 contributors for this article] (2009). NUCKS overexpression in breast cancer. Cancer Cell International. ISSN 1475-2867. 9. doi: 10.1186/1475-2867-9-19.
• Sargent, L M; Ensell, Mang X; Østvold, Anne Carine; Baldwin, Kimberly T; Kashon, Michael L & Lowry, David T [Show all 12 contributors for this article] (2008). Chromosomal changes in high- and low-invasive mouse lung adenocarcinoma cell strains derived from early passage mouse lung adenocarcinoma cell strains. Toxicology and Applied Pharmacology. ISSN 0041-008X. 233(1), p. 81–91. doi: 10.1016/j.taap.2008.01.031.
• Grundt, Kirsten; Haga, Ingvild Vågslid; Huitfeldt, Henrik & Østvold, Anne Carine (2007). Identification and characterization of two putative nuclear localization signals (NLS) in the DNA-binding protein MUCKS. BBA - Molecular Cell Research. ISSN 0167-4889. 1773, p. 1398–1406. doi: 10.1016/j.bbamcr.2007.05.013.
• Grundt, Kirsten; Haga, Ingvild Vågslid; Aleporou-Marinou, V; Drosos, Y; Wanvik, Birgit & Østvold, Anne Carine (2004). Characterization of the NUCKS gene on human chromosome 1q32.1 and the presence of a homologous gene in different species. Biochemical and Biophysical Research Communications - BBRC. ISSN 0006-291X. 323, p. 796–801. doi: 10.1016/j.bbrc.2004.08.153.
• Grundt, Kirsten; Skjeldal, Lars; Anthonsen, Henrik W.; Skauge, Tormod; Huitfeldt, Henrik & Østvold, Anne Carine (2002). A putative DNA-binding domain in the NUCKS protein. Archives of Biochemistry and Biophysics. ISSN 0003-9861. 407(2), p. 168–175.
• Slagsvold, Hege H.; Østvold, Anne Carine; Fallgren, Åsa Birgitta & Paulsen, Ragnhild Elisabeth (2002). Nuclear receptor and apoptosis initiator NGFI-B is a substrate for kinase ERK2. Biochemical and Biophysical Research Communications - BBRC. ISSN 0006-291X. 291, p. 1146–1150.
• Oksvold, Morten Pedersen; Huitfeldt, Henrik; Østvold, Anne Carine & Skarpen, Ellen (2002). UV induces tyrosine kinase-independent internalisation and endosome arrest of the EGF receptor. Journal of Cell Science. ISSN 0021-9533. 115(4), p. 793–803. Show summary

  We have compared the activation and trafficking of epidermal growth factor receptor (EGFR) induced by UV light and EGF. Tyrosine phosphorylation of EGFR was not detected in UV-exposed cells by immunoblotting of whole cell lysates or EGFR immunoprecipitates with antibodies specific for each of the five activated autophosphorylation sites of EGFR. In addition, EGFR of UV-irradiated cells did not demonstrate increased (32)P-incorporation. However, UV-exposed cells demonstrated a gel mobility shift of EGFR, which was not abolished by alkaline phosphatase treatment. UV-exposure did not induce dimerisation of EGFR. Furthermore, UV induced internalisation of EGFR without polyubiquitination or degradation. UV-exposed EGFR was transferred to early endosomes and arrested in transferrin-accessible endosomes close to the cell surface. Whereas inhibition of the EGFR tyrosine kinase effectively inhibited tyrosine phosphorylation and internalisation of EGF-activated EGFR, internalisation of UV-exposed EGFR was unaffected. UV induced neither relocalisation of Shc and Grb2 nor activation of Raf, but activation of MEK and MAPK was observed. Our work indicates that UV induces internalisation of EGFR independent of its phosphorylation or receptor tyrosine kinase activation, and altered EGFR trafficking compared with ligand-activated receptor. In addition, MAPK activation by UV does not appear to be mediated by EGFR activation.

• Grundt, Kirsten; Skjeldal, Lars; Anthonsen, Henrik W.; Skauge, Tormod; Huitfeldt, Henrik & Østvold, Anne Carine (2002). A putative DNA-binding domain in the NUCKS protein. Archives of Biochemistry and Biophysics. ISSN 0003-9861. 407, p. 168–175. Show summary

  We have studied the DNA binding properties of a NUCKS derived, synthetic peptide containing an extended GRP motif. This peptide binds to random sequence DNA, but did not bind preferentially to poly (dA-dT). A synthetic peptide with the same amino acid composition but with a random sequence did not bind to DNA, suggesting that the structure of the DNA binding domain plays a pivotal role for the interaction with DNA. NMR and graphic modeling were employed to investigate the structure of the synthetic peptide. It was shown that the DNA binding peptide constituted an a¿helix in phosphate buffer at pH 5.5. Docking results indicated an almost perfect fit for this small, helical peptide into the major groove of DNA with the possibility of four basic residues to interact with the phosphate backbone of DNA. One consensus site for phosphorylation by Cdk1 is located in the N-terminal end of the DNA binding peptide. Upon phosphorylation of this site, the binding to DNA was completely prohibited. Immunofluorescence experiments showed that NUCKS was located in the nuclei in proliferating cells in interphase of the cell cycle, but was distributed throughout the cytoplasm in mitotic cells.

• Johannessen, Lene E.; Haugen, Karianne Eide; Østvold, Anne Carine; Stang, Espen & Madshus, Inger Helene (2001). Heterodimerization of the epidermal growth factor (EGF) receptor and ErbB2 and the affinity of EGF binding are regulated by different mechanisms. Biochemical Journal. ISSN 0264-6021. 356, p. 87–96.
• Haug, Lise Sofie & Østvold, Anne Carine (2000). Regulation of type I IP3 receptors and neurodegeneration. Current Topics in Biochemical Research. ISSN 0972-4583. 2, p. 77–89.
• Haug, Lise Sofie; Walaas, Sven Ivar & Østvold, Anne Carine (2000). Degradation of the Type I Inositol 1,4,5-Trisphosphate Receptor by Caspase-3 in SH-SY5Y Neuroblastoma Cells Undergoing Apoptosis. Journal of Neurochemistry. ISSN 0022-3042. 75(5), p. 1852–1861.
• Walaas, Sven Ivar & Østvold, Anne Carine (1999). Analysis of protein phosphorylation. In Higgins, S.J. & Hames, B.D. (Ed.), Post-Translational Processing. A Practical Approach. Oxford University Press. ISSN 0-19-963794-6. p. 95–133.
• Haug, Lise Sofie; Jensen, Vidar; Hvalby, Øyvind Christian; Walaas, Sven Ivar & Østvold, Anne Carine (1999). Phosphorylation of the inositol 1,4,5-trisphosphate receptor by cyclic nucleotide-dependent kinases in vitro and in rat cerebellar slices in situ. Journal of Biological Chemistry. ISSN 0021-9258. 274(11), p. 7467–7473. Show summary

  We have examined cyclic nucleotide-regulated phosphorylation of the neuronal type I inositol 1,4,5-trisphosphate (IP3) receptor immunopurified from rat cerebellar membranes in vitro and in rat cerebellar slices in situ. The isolated IP3 receptor protein was phosphorylated by both cAMP- and cGMP-dependent protein kinases on two distinct sites as determined by thermolytic phosphopeptide mapping, phosphopeptide 1, representing Ser-1589, and phosphopeptide 2, representing Ser-1756 in the rat protein (Ferris, C. D., Cameron, A. M., Bredt, D. S., Huganir, R. L., and Snyder, S. H. (1991) Biochem. Biophys. Res. Commun. 175, 192-198). Phosphopeptide maps show that cAMP-dependent protein kinase (PKA) labeled both sites with the same time course and same stoichiometry, whereas cGMP-dependent protein kinase (PKG) phosphorylated Ser-1756 with a higher velocity and a higher stoichiometry than Ser-1589. Synthetic decapeptides corresponding to the two phosphorylation sites (peptide 1, AARRDSVLAA (Ser-1589), and peptide 2, SGRRESLTSF (Ser-1756)) were used to determine kinetic constants for the phosphorylation by PKG and PKA, and the catalytic efficiencies were in agreement with the results obtained by in vitro phosphorylation of the intact protein. In cerebellar slices prelabeled with [32P]orthophosphate, activation of endogenous kinases by incubation in the presence of cAMP/cGMP analogues and specific inhibitors of PKG and PKA induced in both cases a 3-fold increase in phosphorylation of the IP3 receptor. Thermolytic phosphopeptide mapping of in situ labeled IP3 receptor by PKA showed labeling on the same sites (Ser-1589 and Ser-1756) as in vitro. In contrast to the findings in vitro, PKG preferentially phosphorylated Ser-1589 in situ. Because both PKG and the IP3 receptor are specifically enriched in cerebellar Purkinje cells, PKG may be an important IP3 receptor regulator in vivo.

• Borgne, Annie; Østvold, Anne Carine; Flament, Stéphane & Meijer, Laurent (1999). Intra-M phase-promoting factor phosphorylation of cyclin B at the prophase/metaphase transition. Journal of Biological Chemistry. ISSN 0021-9258. 274(17), p. 11977–11986.
• Haug, Lise Sofie; Østvold, Anne Carine; Torgner, Ingeborg Aasland; Roberg, Bjørg Åse; Dvoráková, Lenka & Stastný, F. [Show all 7 contributors for this article] (1998). Intracerebroventricular administration of quinolinic acid induces a selective decrease of inositol (1,4,5)-trisphosphate receptor in rat brain. Neurochemistry International. ISSN 0197-0186. 33, p. 109–119. Show summary

  [3H]inositol(1,4,5)-trisphosphate (IP3) binding studies have shown decreased [3H]IP3 binding to brain tissue in several neurodegenerative diseases, including Alzheimer's and Huntington's diseases. In addition, previous results obtained from brains of Alzheimer patients indicated a reduction of IP3-receptor protein correlated to neuronal loss. The neurotoxic effect of the glutamate receptor agonist quinolinic acid (QUIN) was therefore examined with respect to the level of IP3-receptor immunoreactivity in rat brain. Neuronal lesions were estimated with antibodies to marker proteins for striatal medium-sized spiny neurons (dopamine- and cyclic AMP-regulated phosphoprotein, Mr 32,000; DARPP-32), synaptic vesicles(synaptophysin), mitochondria (phosphate-activated glutaminase; PAG) and glial cells (glial fibrillary acidic protein; GFAP). Injection of QUIN into rat neostriatum induced a massive loss of striatal medium-sized spiny neurons, and led to a comparable loss of IP3-receptor and PAG immunoreactivity, suggesting a neuronal localisation of both these proteins. In an effort to induce less pronounced excitotoxic damage, intracerebroventricular infusion of QUIN was performed. Following this lesion, the neostriatum showed a negligible loss of DARPP-32 immunoreactivity (-11+/-5%), but contained only 43+/-3% of IP3-receptor immunoreactivity levels compared to controls. In the hippocampus, cerebellum and entorhinal cortex, the IP3-receptor loss was less pronounced. The decrease in the level of IP3-receptor immunoreactivity appears to be selective with respect to the other proteins studied, and the IP3-receptor thus shows extreme sensitivity to QUIN neurotoxicity in the neostriatum.

• Walaas, Sven Ivar & Østvold, Anne Carine (1996). Analysis of Protein Phosphorylation in Intact Cells and Extracts. In Hemmings, H. C. Jr (Eds.), Neuromethods, Vol. 30: Regulatory Protein Modification: Techniques and Protocols. Humana Press Inc., Totowa, NJ, USA. p. 1–43.
• Haug, Lise Sofie; Østvold, Anne Carine; Cowburn, Richard F.; Garlind, Anita; Winblad, Bengt & Bogdanovich, Nenad [Show all 7 contributors for this article] (1996). Decreased Inositol (1,4,5)-Trisphosphate Receptor Levels in Alzheimer's Disease Cerebral Cortex: Selectivety of Changes and Possible Correlation of Pathological Severity. Neurodegeneration. ISSN 1055-8330. 5, p. 169–176.
• Magnusson, Andres; Haug, Lise Sofie; Walaas, Sven Ivar & Østvold, Anne Carine (1993). Calcium-induced degradation of the Inositol (1,4,5)-trisphosphate receptor/Ca(2+)-channel. FEBS Letters. ISSN 0014-5793. 323(3), p. 229–232. Show summary

  Ca(2+)-induced degradation of the neuronal inositol (1,4,5)-trisphosphate receptor, a protein which regulates Ca(2+)-release from intracellular stores, has been examined. The IP3-receptor, immunopurified from rat cerebellum, appeared to be an excellent substrate for purified Ca(2+)-activated neutral protease (calpain). Incubation of membranes or immunopurified IP3-receptor with Ca2+ and cerebellar cytosol also resulted in degradation of the receptor. Two main fragments with approximate molecular masses of 130 and 95 kDa were generated, both of which appeared to derive from the carboxyterminal Ca(2+)-channel-containing part of the protein. These data suggest that activation of the IP3-receptor, by causing increases in intracellular [Ca2+], might result in degradation of the N-terminal, IP3-binding part of the receptor.

• Mælandsmo, Gunhild Mari; Østvold, Anne Carine & Laland, S. G. (1989). Phosphorylation of the high mobility-group-like protein P1 by casein kinase-2. European Journal of Biochemistry (EJB). ISSN 0014-2956. p. 529–534.

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• Østvold, Anne Carine & Grundt, Kirsten (2008). NUCKS expression is correlated with early onset of breast adenocarcinomas. Histopathology. ISSN 0309-0167. 53, p. 34–35.
• Skjeldal, Lars; Anthonsen, Henrik W.; Skauge, Tormod & Østvold, Anne Carine (2003). NMR and computer modeling of NUCKS binding to DNA.
• Skjeldal, Lars; Grundt, Kirsten; Østvold, Anne Carine; Anthonsen, Henrik W. & Skauge, Tormod (2003). NMR and graphic modeling of a protein-DNA complex.
• Skjeldal, Lars; Østvold, Anne Carine; Skauge, Tormod & Anthonsen, Henrik W. (2002). Computer modeling of NUCKS binding to DNA.
• Skjeldal, Lars; Østvold, Anne Carine; Anthonsen, Henrik W. & Skauge, Tormod (2002). DNA binding of NUCKS.
• Johannessen, Lars Erik; Haugen, Karianne Eide; Østvold, Anne Carine; Stang, Espen & Madshus, Inger Helene (2001). Dimerisation of the epidermal growth factor receptor.
• Hankø, Erik; Hansen, Thor Willy Ruud; Østvold, Anne Carine & Walaas, Sven Ivar (2001). Magnitude of bilirubin-mediated inhibition of protein phosphorylation is dependent on substrate characteristics.
• Haug, Lise Sofie; Torgner, Ingeborg Aasland & Østvold, Anne Carine (1999). Characterization of the cell death process in SH-SY5Y human neuroblastoma cells induced by bilirubin.
• Haug, Lise Sofie; Dvoráková, Lenka; Walaas, Sven Ivar & Østvold, Anne Carine (1998). The inositol (1,4,5)-trisphosphate receptor/Ca2+ channel protein is selectively decreased in rat brains treated with quinolinic acid.
• Haug, Lise Sofie; Jensen, Vidar; Hvalby, Øyvind Christian; Walaas, Sven Ivar & Østvold, Anne Carine (1998). Stimulation of cyclic GMP-dependent protein kinase leads to phosphorylation of type I inositol trisphosphate-receptor in rat cerebellar slices.
• Haug, Lise Sofie; Østvold, Anne Carine & Walaas, Sven Ivar (1997). Regulation of the neuronal IP3-receptor: a possible correlation to Alzheimer's disease.
• Hansen, Thor Willy Ruud; Mathiesen, Siri B. W.; Østvold, Anne Carine & Walaas, Sven Ivar (1997). Bilirubin inhibits casein kinase 2 by a non-competitive mechanism. Show summary

  Background B has been shown to inhibit several phosphorylation systems. As protein phosphorylation plays a key role in the regulation of many neuronal processes, this effect of B may be an important contributor to its well known neurotoxicity. Thus far the effects of B had been examined in phosphorylation systems with substrate consensus sequences consisting of basic amino acids. In order to evaluate the importance of the substrate characteristics for B effects. We have examined the effects of B on CK2, which preferentially phosphorylates a sequence of acidic residues. Materials/methods The nuclear protein Pl and the synthetic CK-2 peptide substrate were phosphorylated by CK -2 in the presence (or absence) of 0-320 µM B. The results were quantitated by gel electrophoresis (Pl) or filtration (peptide) and Cerenkov counting. Results B inhibited phosphorylation of both substrates by CK.2. Half-maximal inhibition of Pl phosphorylation was achieved at appr. 1 00 gM B. Kinetic analysis of B effects on phosphorylation of the peptide showed appr.70% reduction of Vmax without obvious effects on Km. Similarly, with ATP as substrate Vmax was reduced by 33%. These results are compatible with a noncompetitive mechanism of inhibition. Discussion T'hese results are consistent with the interpretation that inhibitory effects of B on protein/peptide phosphorylation are not dependent upon specific substrate properties. In particular the effects of B appear not to depend on the charge of the consensus sequence, since B was as potent against the CK-2 peptide containing multiple aspartates as previously found with PKA and substrates containing arginines. It therefore appears likely that the inhibitory effects of B on protein/peptide phosphorylation reactions is related to properties of the protein kinases. B is known to bind to lysine, i.a. on albumin and ligandin. We speculate that B binding to lysine, an invariant presence in subdomain II of the protein kinase family, may be important for the effects of B on protein phosphorylation systems.

• Aschim, Elin Leirvoll; Østvold, Anne Carine & Eskild, Winnie (1997). Regulation of CRBP1 function.
• Haug, Lise Sofie; Østvold, Anne Carine; Torgner, Ingeborg Aasland; Roberg, Bjørg Åse; Dvoráková, Lenka & Walaas, Sven Ivar (1996). Type I inositol (1,4,5)-trisphosphate receptor and phosphate-activated glutaminase are highly enriched in neurons as compared to glial cells in rat neostriatum.
• Eskild, Winnie & Østvold, Anne Carine (1996). Regulation of CRBP1 activity - Possible involvement of protein kinase C.
• Haug, Lise Sofie; Cowburn, Richard F.; Walaas, Sven Ivar & Østvold, Anne Carine (1995). The Inositol (1,4,5)-trisphosphate receptor is selectively degraded in brain tissues from patients with Alzheimer's disease.
• Haug, Lise Sofie; Walaas, Sven Ivar & Østvold, Anne Carine (1994). Phosphorylation of purified IP3-receptor from rat cerebellum by cyclic GMP-dependent protein kinase.
• Haug, Lise Sofie; Østvold, Anne Carine & Walaas, Sven Ivar (1993). Calcium-induced degradation of the IP3-receptor/Ca(2+)-channel.

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