Tasks performed
- Histology
- Microscopy
- Standard PCR
- Practical course in hematology
- Laboratory maintenance
- Purchasing
- Web Publishing
Tags:
Laboratory work,
Histology,
Microscopy,
Purchasing,
Training
Publications
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Maghazachi, Azzam A; Sand, Kristin Larsen & Al-Jaderi, Zaidoon
(2016).
Glatiramer acetate, dimethyl fumarate, and monomethyl fumarate upregulate the expression of CCR10 on the surface of natural killer cells and enhance their chemotaxis and cytotoxicity.
Frontiers in Immunology.
ISSN 1664-3224.
7.
doi:
10.3389/fimmu.2016.00437.
Show summary
In vitro harnessing of immune cells is the most important advance in the field of cancer immunotherapy. Results shown in the current paper may be used to harness natural killer (NK) cells in vitro. It is observed that drugs used to treat multiple sclerosis such as glatiramer acetate, dimethyl fumarate, and monomethyl fumarate upregulate the expression of chemokines receptor 10 (CCR10) on the surface of human IL-2-activated NK cells. This is corroborated with increased chemotaxis of these cells toward the concentration gradients of the ligands for CCR10, namely CCL27 and CCL28. It is also demonstrated that these three drugs enhance NK cell cytotoxicity against tumor target cells, an activity that is abrogated by prior incubation of the cells with anti-CCR10 antibody. Because CCL27 and CCL28 are secreted by selective tumor types such as malignant melanoma, squamous cell carcinomas, and colorectal cancer, respectively, it is hypothesized that activated NK cells may be harnessed in vitro with any of these drugs before utilizing them as a therapeutic modality for cancer.
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Vego, Heidi; Sand, Kristin Larsen; Høglund, Rune Alexander; Fallang, Lars-Egil; Gundersen, Glenn & Holmøy, Trygve
[Show all 7 contributors for this article]
(2016).
Monomethyl fumarate augments NK cell lysis of tumor cells through degranulation and the upregulation of NKp46 and CD107a.
Cellular & Molecular Immunology.
ISSN 1672-7681.
13(1),
p. 57–64.
doi:
10.1038/cmi.2014.114.
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Sand, Kristin Larsen; Flatebø, Torun; Andersen, Marian Berge & Maghazachi, Azzam
(2013).
Effects of exercise on leukocytosis and blood hemostasis in 800 healthy young females and males.
World Journal of Experimental Medicine.
ISSN 2220-315X.
3(1),
p. 11–20.
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Aas, Vigdis; Sand, Kristin Larsen; Åsheim, Hans-Christian; Benestad, Haakon Breien & Iversen, Jens Gustav Heber
(2013).
C-Reactive Protein Triggers Calcium Signalling in Human Neutrophilic Granulocytes via FcγRIIa in an Allele-Specific Way.
Scandinavian Journal of Immunology.
ISSN 0300-9475.
77(6),
p. 442–451.
doi:
10.1111/sji.12049.
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Troitskaya, Maria P.; Baysa, Anton; Vaage, Ingvar Jarle; Sand, Kristin Larsen; Maghazachi, Azzam & Valen, Guro
(2012).
IL-17 level is reduced during acute myocardial infarction. Role of chemokine receptor expression in monocytes and their in vitro chemotaxis towards chemokines.
Toxins.
ISSN 2072-6651.
4(12),
p. 1427–1439.
doi:
10.3390/toxins4121427.
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Rolin, Johannes; Sand, Kristin Larsen; Knudsen, Eirunn & Maghazachi, Azzam
(2010).
FTY720 and SEW2871 reverse the inhibitory effect of S1P on natural killer cell mediated lysis of K562 tumor cells and dendritic cells but not on cytokine release.
Cancer Immunology and Immunotherapy.
ISSN 0340-7004.
59(4),
p. 575–586.
doi:
10.1007/s00262-009-0775-7.
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Rolin, Johannes; Sand, Kristin Larsen; Knudsen, Eirunn & Maghazachi, Azzam
(2009).
FTY720 and SEW2871 reverse the inhibitory effect of S1P on natural killer cell mediated lysis of K562 tumor cells and dendritic cells but not on cytokine release.
Cancer Immunology and Immunotherapy.
ISSN 0340-7004.
doi:
10.1007/s00262-009-0775-7.
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De, Blasio Birgitte Freiesleben; Røttingen, John-Arne; Sand, Kristin Larsen; Giaever, I & Iversen, Jens Gustav Heber
(2004).
Global, synchronous oscillations in cytosolic calcium and adherence in bradykinin-stimulated Madin-Darby canine kidney cells.
Acta Physiologica Scandinavica.
ISSN 0001-6772.
180,
p. 335–346.
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Melien, Øyvind; Nilssen, Laila Sortvik; Dajani, Olav Faial; Sand, Kristin Larsen; Sandnes, Dagny Lise & Iversen, Jens Gustav
[Show all 7 contributors for this article]
(2002).
Ca2+-mediated activation of ERK in hepatocytes by norepinephrine and prostaglandin F2-alpha: role of calmodulin and src kinases.
BMC Cell Biology.
ISSN 1471-2121.
3(5).
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Aas, Vigdis; Algerøy, Siri; Sand, Kristin Larsen & Iversen, Jens Gustav
(2001).
Fibronectin Promotes Calcium Signaling by Interferon-gamma in Human Neutrophils via G-protein and Sphingosine Kinase-Dependent Mechanisms.
Cell Adhesion and Communication.
ISSN 1061-5385.
8(3),
p. 125–138.
Show summary
A common intracellular signal activating polymorphonuclear leukocyte (PMN) in inflammation is a change in cytosolic calcium concentration. Previously, we have shown that interferon-gamma (IFN-gamma) induces transient calcium signals in PMN, but only after intracellular calcium store depletion. Using a digital imaging system, we show that adhesion of PMN is critical for IFN-gamma induced calcium signals, and when attached to the optimal coating, the calcium signals are evoked even in presence of extracellular calcium, i.e. non-depleted calcium stores. Adhesion to fibronectin, pure or extracted from plasma by gelatin, improved the IFN-gamma responses compared with serum, plasma or vitronectin coats. In accordance with previous observations, IFN-gamma induced calcium signals in fibronectin adherent cells were totally abolished by the G-protein inhibitor pertussis toxin and were also clearly depressed by pertussis toxin and the sphingosine kinase inhibitors dimethylsphingosine (DMS) and N-acetyl-D-sphingosine (N-Ac-Sp). PMN contact with fibronectin alone, measured in cells sedimenting onto a fibronectin coated surface or by addition of fibronectin to glass adherent cells, evoked transient calcium signals in PMN. However, they were also clearly depressed by pertussis toxin and the sphingosine kinase inhibitors DMS, dihydrosphingosine (DHS), and N-Ac-Sp. When the product of sphingosine kinase activity, sphingosine 1-phosphate (S 1-P), was added to the cells, similar calcium signals were induced, which were dependent on a pertussis toxin sensitive G-protein activity. Finally, addition of S 1-P to the cells prior to stimulation with IFN-gamma partly mimicked the priming effect of fibronectin. In conclusion, fibronectin contact evokes by itself a calcium signal in PMN and further promotes calcium signalling by IFN-gamma. We suggest that fibronectin might activate sphingosine kinase and the sphingosine 1-phosphate, thereby generated, induce a calcium signal via a G-protein dependent mechanism. Apparently, sphingosine kinase activity is also involved in IFN-gamma induced calcium signals.
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Benestad, Haakon Breien; Sand, Kristin Larsen & Bruusgaard, Jo C.
(2018).
Less than recommended training of aerobic fitness and muscle strength: What to expect?
Acta Physiologica.
ISSN 1748-1708.
224(4).
doi:
10.1111/apha.13104.
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Melien, Øyvind; Nilssen, Laila Sortvik; Dajani, Olav Faial; Sand, Kristin Larsen; Iversen, Jens Gustav & Sandnes, Dagny Lise
[Show all 7 contributors for this article]
(2000).
A Role for Calmodulin and Src Kinases in Ca2+ - dependent activation of ERK in Hepatocytes by Norepinephrine and Prostaglandine F2Aalfa.
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Aas, Vigdis; Algerøy, Siri; Sand, Kristin Larsen & Iversen, Jens Gustav
(2000).
Fibronectin elicits a cytosolic calcium signal dependent on sphingosine kinase activity.
Show summary
Fibronectin elicits a cytosolic calcium signal dependent on sphingosine kinase activity in neutrophils
Vigdis Aas*, Siri Algerøy*, Kristin Larsen# and Jens-Gustav Iversen#
*Department of pharmacology, School of pharmacy, University of Oslo, #Department of physiology, Institute of basic medical sciences, University of Oslo.
Migration of neutrophils (PMN) towards inflammatory sites involves cell contact with extracellular matrix proteins like fibronectin (FN). The interaction with fibronectin has been reported to be a co-stimulatory signal that supports PMN activation. We have recently shown that the cytokine interferon-g (IFN-g) induces cytosolic calcium signals in human neutrophils adherent to fibronectin coated surfaces, but not in PMN adherent to uncoated glass surfaces. In an attempt to understand how adhesion to FN promote calcium signalling by IFN-g, we have investigated the effects of FN on PMN calcium metabolism. Registration of cytosolic calcium concentration in single fura-2 loaded cells was performed with a digital imaging technique.
Baseline cytosolic calcium concentration in cells adherent to FN did not differ from cells adherent to glass or plasma. As assessed by store depletion with thapsigargin, there were no indications that adhesion to FN affected PMN calcium storage. However, when cells adherent to uncoated surfaces were stimulated with a FN- or a RGD-solution, transient calcium signals were evoked in 32 % and 62 % of the cells, respectively. In addition, PMN falling down onto FN-coated coverslips showed marked intracellular calcium signals when establishing contact with the FN-surface. Falling down onto FN-coating 85 % of the cells responded with an increase in cytosolic calcium concentration > 100 nM, average 309 ± 9 nM, compared to 57 % on plasma-coating and 32 % on uncoated coverslips.
The FN-induced calcium signals were partly dependent on a pertussis-toxin sensitive G-protein, while they were totally abolished by the sphingosine kinase inhibitors N,N-dimethylsphingosine (DMS) and N-acetyl-D-sphingosine (N-Ac-Sp). Stimulation of PMN with the product of sphingosine kinase, sphingosine-1-phosphate, also induced transient cytosolic calcium signals which were dependent on a pertussis toxin sensitive G-protein.
These data suggest that FN-attachment induces calcium signals in PMN, presumably by sphingosine kinase mediated generation of sphingosine-1-phosphate.
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Published
Apr. 13, 2011 11:00 AM
- Last modified
Nov. 29, 2023 11:27 AM