{"entity": "researcher", "timestamp": "2026-09-23T23:24:24.812Z", "family": "Fontana", "given": "Jacopo Maria", "initials": "JM", "orcid": "0000-0003-4784-4713", "affiliations": ["Science for Life Laboratory, Department of Applied Physics, Royal Institute of Technology, Stockholm, Sweden."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/6198b7e9db6e48bdbadbee573adbd997.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/6198b7e9db6e48bdbadbee573adbd997"}}, "publications": [{"entity": "publication", "iuid": "44056901db34455fbd66f9b9f2ee86da", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/44056901db34455fbd66f9b9f2ee86da.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/44056901db34455fbd66f9b9f2ee86da"}}, "title": "Ouabain-regulated phosphoproteome reveals molecular mechanisms for Na+, K+-ATPase control of cell adhesion, proliferation, and survival.", "authors": [{"family": "Panizza", "given": "Elena", "initials": "E"}, {"family": "Zhang", "given": "Liang", "initials": "L"}, {"family": "Fontana", "given": "Jacopo Maria", "initials": "JM", "orcid": "0000-0003-4784-4713", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/6198b7e9db6e48bdbadbee573adbd997.json"}}, {"family": "Hamada", "given": "Kozo", "initials": "K"}, {"family": "Svensson", "given": "Daniel", "initials": "D"}, {"family": "Akkuratov", "given": "Evgeny E", "initials": "EE", "orcid": "0000-0002-2552-9512", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/abd9e4662bb543eebb0451af868bc319.json"}}, {"family": "Scott", "given": "Lena", "initials": "L", "orcid": "0000-0002-4886-5084", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/87aad1a3faeb4470992c46bbfcccb873.json"}}, {"family": "Mikoshiba", "given": "Katsuhiko", "initials": "K"}, {"family": "Brismar", "given": "Hjalmar", "initials": "H", "orcid": "0000-0003-0578-4003", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/04321d9fb805493db538489927a42c8f.json"}}, {"family": "Lehti\u00f6", "given": "Janne", "initials": "J", "orcid": "0000-0002-8100-9562", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/561efcf32e2648c8a10fee692fc4e908.json"}}, {"family": "Aperia", "given": "Anita", "initials": "A"}], "type": "journal article", "published": "2019-09-00", "journal": {"title": "FASEB J.", "issn": "1530-6860", "volume": "33", "issue": "9", "pages": "10193-10206", "issn-l": "0892-6638"}, "abstract": "The ion pump Na+, K+-ATPase (NKA) is a receptor for the cardiotonic steroid ouabain. Subsaturating concentration of ouabain triggers intracellular calcium oscillations, stimulates cell proliferation and adhesion, and protects from apoptosis. However, it is controversial whether ouabain-bound NKA is considered a signal transducer. To address this question, we performed a global analysis of protein phosphorylation in COS-7 cells, identifying 2580 regulated phosphorylation events on 1242 proteins upon 10- and 20-min treatment with ouabain. Regulated phosphorylated proteins include the inositol triphosphate receptor and stromal interaction molecule, which are essential for initiating calcium oscillations. Hierarchical clustering revealed that ouabain triggers a structured phosphorylation response that occurs in a well-defined, time-dependent manner and affects specific cellular processes, including cell proliferation and cell-cell junctions. We additionally identify regulation of the phosphorylation of several calcium and calmodulin-dependent protein kinases (CAMKs), including 2 sites of CAMK type II-\u03b3 (CAMK2G), a protein known to regulate apoptosis. To verify the significance of this result, CAMK2G was knocked down in primary kidney cells. CAMK2G knockdown impaired ouabain-dependent protection from apoptosis upon treatment with high glucose or serum deprivation. In conclusion, we establish NKA as the coordinator of a broad, tightly regulated phosphorylation response in cells and define CAMK2G as a downstream effector of NKA.-Panizza, E., Zhang, L., Fontana, J. M., Hamada, K., Svensson, D., Akkuratov, E. E., Scott, L., Mikoshiba, K., Brismar, H., Lehti\u00f6, J., Aperia, A. Ouabain-regulated phosphoproteome reveals molecular mechanisms for Na+, K+-ATPase control of cell adhesion, proliferation, and survival.", "doi": "10.1096/fj.201900445R", "pmid": "31199885", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC6704450"}], "notes": [], "created": "2026-08-21T12:13:05.633Z", "modified": "2026-09-23T14:52:47.487Z"}, {"entity": "publication", "iuid": "71d1ef09b28e48a4a9e81d6ba6c37f5a", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/71d1ef09b28e48a4a9e81d6ba6c37f5a.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/71d1ef09b28e48a4a9e81d6ba6c37f5a"}}, "title": "Transport and release of colloidal 3-mercaptopropionic acid-coated CdSe-CdS/ZnS core-multishell quantum dots in human umbilical vein endothelial cells.", "authors": [{"family": "Fontana", "given": "Jacopo M", "initials": "JM", "orcid": "0000-0003-4784-4713", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/6198b7e9db6e48bdbadbee573adbd997.json"}}, {"family": "Yin", "given": "Huijuan", "initials": "H", "orcid": "0000-0002-4821-7562", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/fd77510493cc4a58b47a357d5bfba513.json"}}, {"family": "Chen", "given": "Yun", "initials": "Y"}, {"family": "Florez", "given": "Ricardo", "initials": "R"}, {"family": "Brismar", "given": "Hjalmar", "initials": "H", "orcid": "0000-0003-0578-4003", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/04321d9fb805493db538489927a42c8f.json"}}, {"family": "Fu", "given": "Ying", "initials": "Y", "orcid": "0000-0002-2442-1809", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/6f01cde4dbdd49b6bc997b22d0726e25.json"}}], "type": "journal article", "published": "2017-12-04", "journal": {"title": "Int J Nanomedicine", "issn": "1178-2013", "volume": "12", "issue": null, "pages": "8615-8629", "issn-l": "1176-9114"}, "abstract": "Colloidal semiconductor quantum dots (QDs) have been extensively researched and developed for biomedical applications, including drug delivery and biosensing assays. Hence, it is pivotal to understand their behavior in terms of intracellular transport and toxicological effects. In this study, we focused on 3-mercaptopropionic acid-coated CdSe-CdS/ZnS core-multishell quantum dots (3MPA-QDs) converted from the as-grown octadecylamine-coated quantum dots (ODA-QDs) and their direct and dynamic interactions with human umbilical vein endothelial cells (HUVECs). Live cell imaging using confocal fluorescence microscopy showed that 3MPA-QDs first attached to and subsequently aggregated on HUVEC plasma membrane ~25 min after QD deposition. The aggregated QDs started being internalized at ~2 h and reached their highest internalization degree at ~24 h. They were released from HUVECs after ~48 h. During the 48 h period, the HUVECs responded normally to external stimulations, grew, proliferated and wound healed without any perceptible apoptosis. Furthermore, 1) 3MPA-QDs were internalized in newly formed LysoTracker-stained early endosomes; 2) adenosine 5'-triphosphate-induced [Ca2+]i modulation caused a transient decrease in the fluorescence of 3MPA-QDs that were attached to the plasma membrane but a transient increase in the internalized 3MPA-QDs; and 3) fluorescence signal modulations of co-stained LysoTracker and QDs induced by the lysosomotropic agent Gly-Phe-\u03b2-naphthylamide were spatially co-localized and temporally synchronized. Our findings suggest that 3MPA-QDs converted from ODA-QDs are a potential nontoxic fluorescent probe for future use in clinical applications. Moreover, the photophysical strategy and techniques reported in this work are easily applicable to study of direct interactions between other nanoparticles and live cells; contributing to awareness and implementation of the safe applications of nanoparticles.", "doi": "10.2147/IJN.S145608", "pmid": "29270011", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC5720035"}, {"db": "pii", "key": "ijn-12-8615"}], "notes": [], "created": "2018-12-05T12:52:56.234Z", "modified": "2026-09-23T14:53:35.426Z"}, {"entity": "publication", "iuid": "e2072f5e86504a778720d387ab2ac60a", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/e2072f5e86504a778720d387ab2ac60a.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/e2072f5e86504a778720d387ab2ac60a"}}, "title": "Na+-K+-ATPase, a new class of plasma membrane receptors.", "authors": [{"family": "Aperia", "given": "Anita", "initials": "A"}, {"family": "Akkuratov", "given": "Evgeny E", "initials": "EE"}, {"family": "Fontana", "given": "Jacopo Maria", "initials": "JM", "orcid": "0000-0003-4784-4713", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/6198b7e9db6e48bdbadbee573adbd997.json"}}, {"family": "Brismar", "given": "Hjalmar", "initials": "H"}], "type": "journal article", "published": "2016-04-01", "journal": {"title": "Am. J. Physiol., Cell Physiol.", "issn": "1522-1563", "volume": "310", "issue": "7", "pages": "C491-C495", "issn-l": "0363-6143"}, "abstract": "The Na(+)-K(+)-ATPase (NKA) differs from most other ion transporters, not only in its capacity to maintain a steep electrochemical gradient across the plasma membrane, but also as a receptor for a family of cardiotonic steroids, to which ouabain belongs. Studies from many groups, performed during the last 15 years, have demonstrated that ouabain, a member of the cardiotonic steroid family, can activate a network of signaling molecules, and that NKA will also serve as a signal transducer that can provide a feedback loop between NKA and the mitochondria. This brief review summarizes the current knowledge and controversies with regard to the understanding of NKA signaling.", "doi": "10.1152/ajpcell.00359.2015", "pmid": "26791490", "labels": [], "xrefs": [{"db": "pii", "key": "ajpcell.00359.2015"}], "notes": [], "created": "2018-12-05T09:19:09.743Z", "modified": "2026-09-23T07:36:43.621Z"}]}