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Eriksson, Ida
Publications (5 of 5) Show all publications
Wäster, P., Eriksson, I., Vainikka, L., Rosdahl, I. & Öllinger, K. (2016). Extracellular vesicles are transferred from melanocytes to keratinocytes after UVA irradiation. Scientific Reports, 6(27890)
Open this publication in new window or tab >>Extracellular vesicles are transferred from melanocytes to keratinocytes after UVA irradiation
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2016 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 6, no 27890Article in journal (Refereed) Published
Abstract [en]

Ultraviolet (UV) irradiation induces skin pigmentation, which relies on the intercellular crosstalk of melanin between melanocytes to keratinocytes. However, studying the separate effects of UVA and UVB irradiation reveals differences in cellular response. Herein, we show an immediate shedding of extracellular vesicles (EVs) from the plasma membrane when exposing human melanocytes to UVA, but not UVB. The EV-shedding is preceded by UVA-induced plasma membrane damage, which is rapidly repaired by Ca2+-dependent lysosomal exocytosis. Using co-cultures of melanocytes and keratinocytes, we show that EVs are preferably endocytosed by keratinocytes. Importantly, EV-formation is prevented by the inhibition of exocytosis and increased lysosomal pH but is not affected by actin and microtubule inhibitors. Melanosome transfer from melanocytes to keratinocytes is equally stimulated by UVA and UVB and depends on a functional cytoskeleton. In conclusion, we show a novel cell response after UVA irradiation, resulting in transfer of lysosome-derived EVs from melanocytes to keratinocytes.

Place, publisher, year, edition, pages
NATURE PUBLISHING GROUP, 2016
National Category
Cell Biology
Identifiers
urn:nbn:se:liu:diva-130287 (URN)10.1038/srep27890 (DOI)000378036300001 ()27293048 (PubMedID)
Note

Funding Agencies|Swedish Research Council; Swedish Cancer Society; Welander-Finsen Foundation; County Council of Ostergotland; Stiftelsen Olle Engkvist Byggmastare; Konung Gustav V och Drottning Victorias Frimurarestiftelse; Ostgotaregionens Cancerfond

Available from: 2016-08-01 Created: 2016-07-28 Last updated: 2017-11-28
Wäster, P., Eriksson, I., Vainikka, L. & Öllinger, K. (2014). Sunbathing: What’ve lysosomes got to do with it?. Communicative & Integrative Biology, 7(1), e28723-1-e28723-5
Open this publication in new window or tab >>Sunbathing: What’ve lysosomes got to do with it?
2014 (English)In: Communicative & Integrative Biology, ISSN 1942-0889, E-ISSN 1942-0889, Vol. 7, no 1, p. e28723-1-e28723-5Article in journal (Refereed) Published
Abstract [en]

Solar radiation is an important risk factor for skin cancer, the incidence of which is increasing, especially in the fair-skinned populations of the world. While the ultraviolet (UV)B component has direct DNA damaging ability, UVA-induced effects are currently mainly attributed to the production of reactive oxygen species. In our recent study, we compared the effects of UVA and UVB radiation on human keratinocytes and found that UVA-induced plasma membrane damage was rapidly repaired by lysosomal exocytosis, which was detected based on the expression of lysosomal membrane associated protein-1 (LAMP-1) on the plasma membrane of non-permeabilized cells. Later, the keratinocytes died through caspase-8 mediated apoptosis. In contrast, the plasma membranes of keratinocytes exposed to UVB showed no LAMP-1 expression, and, although the cells died by apoptosis, no initial caspase-8 activity was detected. We have also demonstrated the occurrence of UVA-induced lysosomal exocytosis in reconstructed skin and shown the relocation of lysosomes from the center of cells to the vicinity of the plasma membrane. Thus, we suggest that lysosomal exocytosis also occurs in keratinocytes covered by the stratum corneum following exposure to UVA. Our findings provide new insight into the mechanism of UVA-induced skin damage.

Place, publisher, year, edition, pages
Austin, Texas, USA: Landes Biosciences, 2014
Keywords
UV irradiation, keratinocytes, lysosomes, exocytosis, plasma membrane repair, lysosomal, associated membrane protein
National Category
Basic Medicine Cell and Molecular Biology
Identifiers
urn:nbn:se:liu:diva-107147 (URN)10.4161/cib.28723 (DOI)25346791 (PubMedID)2-s2.0-84902664460 (Scopus ID)
Note

Article Addendum to: H Appelqvist, P Waster, I Eriksson, I Rosdahl, K Ollinger. Lysosomal exocytosis and caspase-8-mediated apoptosis in UVA-irradiated keratinocytes. Journal of Cell Science 2013; 126: 5578- 5584. DOI: 10.1242/jcs.130633

Available from: 2014-06-05 Created: 2014-06-05 Last updated: 2018-01-11Bibliographically approved
Appelqvist, H., Wäster, P., Eriksson, I., Rosdahl, I. & Öllinger, K. (2013). Lysosomal exocytosis and caspase-8-mediated apoptosis in UVA-irradiated keratinocytes. Journal of Cell Science, 126(24), 5578-5584
Open this publication in new window or tab >>Lysosomal exocytosis and caspase-8-mediated apoptosis in UVA-irradiated keratinocytes
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2013 (English)In: Journal of Cell Science, ISSN 0021-9533, E-ISSN 1477-9137, Vol. 126, no 24, p. 5578-5584Article in journal (Refereed) Published
Abstract [en]

Ultraviolet (UV) irradiation is a major environmental carcinogen involved in the development of skin cancer. To elucidate the initial signaling during UV-induced damage in human keratinocytes, we investigated lysosomal exocytosis and apoptosis induction. UVA, but not UVB, induced plasma membrane damage, which was repaired by Ca2+-dependent lysosomal exocytosis. The lysosomal exocytosis resulted in extracellular release of cathepsin D and acid sphingomyelinase (aSMase). Two hours after UVA irradiation, we detected activation of caspase-8, which was reduced by addition of anti-aSMAse. Furthermore, caspase-8 activation and apoptosis was reduced by prevention of endocytosis and by the use of cathepsin inhibitors. We conclude that lysosomal exocytosis is part of the keratinocyte response to UVA and is followed by cathepsin-dependent activation of caspase-8. The findings have implications for the understanding of UV-induced skin damage and emphasize that UVA and UVB initiate apoptosis through different signaling pathways in keratinocytes.

Place, publisher, year, edition, pages
Company of Biologists, 2013
Keywords
Keratinocyte; UV irradiation; Lysosome; Cathepsin; Endocytosis; Apoptosis
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-103290 (URN)10.1242/jcs.130633 (DOI)000328686600005 ()
Note

The previous status of this article was manuscript with the title Lysosomal exocytosis repairs the plasma membrane after UVA and is followed by caspase-8 induced apoptosis.

Available from: 2014-01-17 Created: 2014-01-16 Last updated: 2017-08-30
Eriksson, I., Joosten, M., Roberg, K. & Öllinger, K. (2013). The histone deacetylase inhibitor trichostatin A reduces lysosomal pH and enhances cisplatin-induced apoptosis. Experimental Cell Research, 319(1), 12-20
Open this publication in new window or tab >>The histone deacetylase inhibitor trichostatin A reduces lysosomal pH and enhances cisplatin-induced apoptosis
2013 (English)In: Experimental Cell Research, ISSN 0014-4827, E-ISSN 1090-2422, Vol. 319, no 1, p. 12-20Article in journal (Refereed) Published
Abstract [en]

High activity of histone deacetylases (HDACs) has been documented in several types of cancer and may be associated with survival advantage. In a head and neck squamous cell carcinoma cell line, cisplatin-induced apoptosis was augmented by pretreatment with the HDAC inhibitor trichostatin Apoptosis was accompanied by lysosomal membrane permeabilization (LMP), as shown by immunoblotting of the lysosomal marker protease cathepsin B in extracted cytosol and by immunofluorescence. Moreover, LAMP-2 (lysosomal associated membrane protein-2) was translocated from lysosomal membranes and found in a digitonin extractable fraction together with cytosolic proteins and pretreatment with trichostatin A potentiated the release. Overall, protein level of LAMP-2 was decreased during cell death and, interestingly, inhibition of cysteine cathepsins, by the pan-cysteine cathepsin inhibitor zFA-FMK, prevented loss of LAMP-2. The importance of LAMP-2 for lysosomal membrane stability, was confirmed by showing that LAMP-2 knockout MEFs (mouse embryonic fibroblasts) were more sensitive to cisplatin as compared to the corresponding wildtype cells. Trichostatin A reduced lysosomal pH from 4.46 to 4.25 and cell death was prevented when lysosomal pH was increased by NH4Cl, or when inhibiting the activity of lysosomal proteases. We conclude that trichostatin A enhances cisplatin induced cell death by decreasing lysosomal pH, which augments cathepsin activity resulting in reduced LAMP-2 level, and might promote LMP.

Place, publisher, year, edition, pages
Elsevier, 2013
Keywords
Histone deacetylase inhibitor; Lysosome; LAMP-2; Cathepsin; LMP
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-87194 (URN)10.1016/j.yexcr.2012.10.004 (DOI)000311712900002 ()
Available from: 2013-01-14 Created: 2013-01-14 Last updated: 2017-12-06
Persson, H. L., Vainikka, L., Eriksson, I. & Wennerstrom, U. (2013). TNF-alpha-stimulated macrophages protect A549 lung cells against iron and oxidation. Experimental and Toxicological Pathology, 65(1-2), 81-89
Open this publication in new window or tab >>TNF-alpha-stimulated macrophages protect A549 lung cells against iron and oxidation
2013 (English)In: Experimental and Toxicological Pathology, ISSN 0940-2993, E-ISSN 1618-1433, Vol. 65, no 1-2, p. 81-89Article in journal (Refereed) Published
Abstract [en]

Previously, we have shown that TNF-alpha protects iron-exposed J774 macrophages against iron-catalyzed oxidative lysosomal disruption and cell death by increasing reduced glutathione and H-ferritin in cells. Because J774 cells are able to harbor large amounts of iron, which is potentially harmful in a redox-active state, we hypothesized that TNF-alpha-stimulated J774 macrophages will prevent iron-driven oxidative killing of alveolar epithelial A549 cells in co-culture. In the present study, iron trichloride (which is endocytosed by cells as hydrated iron-phosphate complexes) was mainly deposited inside the lysosomes of J774 macrophages, while A549 cells, equally iron exposed, accumulated much less iron. When challenged by oxidants, however, reactive lysosomal iron in A549 cells promoted lysosomal disruption and cell death, particularly in the presence of TNF-alpha. This effect resulted from an elevation in ROS generation by TNF-alpha, while a compensatory upregulation of protective molecules (H-ferritin and/or reduced glutathione) by TNF-alpha was absent. A549 cell death was particularly pronounced when iron and TNF-alpha were present in the conditioned medium during oxidant challenge; thus, iron-driven oxidative reactions in the culture medium were a much greater hazard to A549 cells than those taking place inside their lysosomes. Consequently, the iron chelator, deferoxamine, efficiently prevented A549 cell death when added to the culture medium during an oxidant challenge. In co-cultures of TNF-alpha-stimulated lung cells, J774 macrophages sequestered iron inside their lysosomes and protected A549 cells from oxidative reactions and cell death. Thus, the collective effect of TNF-alpha on co-cultured lung cells was mainly cytoprotective.

Place, publisher, year, edition, pages
Elsevier, 2013
Keywords
Apoptosis, Ferritin, Fibrosis, Lysosomes, Macrophages, Oxidative stress
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-89525 (URN)10.1016/j.etp.2011.06.004 (DOI)000314006000014 ()
Note

Funding Agencies|County Council of Ostergotland (ALF)||Medical Research Council of Southeast Sweden (FORSS)||Swedish Medical Society||Linkoping Medical Society||Olle Engkvist, Apotekare Hedberg and LiO (Ostergotland, Sweden)||

Available from: 2013-02-26 Created: 2013-02-26 Last updated: 2017-12-06
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