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Svensson, Samuel P.S.
Alternative names
Publications (10 of 48) Show all publications
Boman, A., Svensson, S., Boxer, A., Rojas, J. C., Seeley, W. W., Karydas, A., . . . Svenningsson, P. (2016). Distinct lysosomal network protein profiles in parkinsonian syndrome cerebrospinal fluid. Journal of Parkinson's Disease, 6(2), 307-315
Open this publication in new window or tab >>Distinct lysosomal network protein profiles in parkinsonian syndrome cerebrospinal fluid
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2016 (English)In: Journal of Parkinson's Disease, ISSN 1877-7171, E-ISSN 1877-718X, Vol. 6, no 2, p. 307-315Article in journal (Refereed) Published
Abstract [en]

Introduction: Clinical diagnosis of parkinsonian syndromes like Parkinson’s disease, corticobasal degeneration and progressive supranuclear palsy is hampered by overlapping symptomatology and lack of biomarkers for diagnosis, and definitive diagnosis is only possible post-mortem. Since impaired protein degradation plays an important role in many neurodegenerative disorders, we hypothesized that levels and profiles of lysosomal network proteins in cerebrospinal fluid could be changed in these parkinsonian syndromes.

Methods: Cerebrospinal fluid samples were collected from Parkinson’s disease patients (n=18), clinically diagnosed 4-repeat tauopathy patients, corticobasal syndrome (n=6) and progressive supranuclear palsy (n=5), pathologically diagnosed progressive supranuclear palsy (n=8) and corticobasal degeneration patients (n=7). Each patient set was compared to its appropriate control group consisting of the same number of age and gender matched individuals. Lysosomal network protein levels were detected via Western blotting.

Results: Lysosomal network proteins have markedly different cerebrospinal fluid protein levels and profiles in Parkinson’s disease, corticobasal degeneration and progressive supranuclear palsy. Lysosomal-associated membrane proteins 1 and 2 were significantly decreased in Parkinson´s disease; early endosomal antigen 1 was decreased and lysozyme increased in progressive supranuclear palsy; and lysosomal-associated membrane proteins 1 and 2, microtubule-associated protein 1 light chain 3 and lysozyme were increased in corticobasal degeneration.

Conclusions: Lysosomal network proteins hold promise of being interesting novel candidates for biomarker studies and for elucidating disease mechanisms of Parkinson’s disease, corticobasal degeneration and progressive supranuclear palsy, but further validation studies will be needed to assess the specificity and the predictive value of these proteins in CSF.

Place, publisher, year, edition, pages
IOS Press, 2016
National Category
Cell and Molecular Biology Chemical Sciences
Identifiers
urn:nbn:se:liu:diva-122342 (URN)10.3233/JPD-150759 (DOI)000378352200004 ()
Note

Funding agencies:This work was supported by the Swedish Alzheimer foundation, the Swedish Dementia foundation, Linkoping University Neurobiology Center, Karin & Sten CBD Solutions AB, AZ-KI TSC, ALF, US National Institutes of Health R01AG038791 and U54NS092089, the Tau Consortium, the Hellman Family Foundation.

Vid tiden för disputationen förelåg publikationen endast som manuskript

Available from: 2015-10-29 Created: 2015-10-29 Last updated: 2018-01-10Bibliographically approved
Adolfsson, P. I., Bloth, B., Hägg, S. & Svensson, S. P. (2015). Zinc Induces a Bell-shaped Proliferative Dose-response Effect in Cultured Smooth Muscle Cells From Benign Prostatic Hyperplasia.. Urology, 85(3), 704.e15-704.e19
Open this publication in new window or tab >>Zinc Induces a Bell-shaped Proliferative Dose-response Effect in Cultured Smooth Muscle Cells From Benign Prostatic Hyperplasia.
2015 (English)In: Urology, ISSN 0090-4295, E-ISSN 1527-9995, Vol. 85, no 3, p. 704.e15-704.e19Article in journal (Refereed) Published
Abstract [en]

OBJECTIVE: To investigate the effects of zinc (Zn(2+)) concentrations on cultured benign prostatic hyperplasia (BPH) smooth muscle cell (SMC) proliferation.

METHODS: The effects of Zn(2+) were studied in primary cultures of human BPH SMC, stimulated with either 10-μM lysophosphatidic acid (LPA) or LPA in combination with 100-nM testosterone. Deoxyribonucleic acid replication and protein synthesis using [(3)H]-thymidine and [(35)S]-methionine incorporation were measured. Furthermore, studies were performed to evaluate if Zn(2+) could potentiate the inhibitory effect of phosphodiesterase-5 blockers, on BPH SMC proliferation.

RESULTS: Zn(2+) generated a bell-shaped concentration response, both regarding deoxyribonucleic acid replication and protein synthesis in cultured BPH SMC. Below a threshold value (approximately 200 μM), a significant mitogenic effect was seen, whereas higher concentrations inhibited SMC proliferation after stimulation with LPA. This effect was even more pronounced after stimulation of LPA in combination with testosterone. Moreover, phosphodiesterase-5 inhibitors, that is, sildenafil blocked LPA-stimulated BPH SMC proliferation. This antiproliferative effect, was significantly potentiated by coincubation with Zn(2+) in an additative manner.

CONCLUSION: The bell-shaped concentration response of Zn(2+) on cultured BPH SMC proliferation suggests that changes in prostate Zn(2+) concentrations, during aging, diet, or inflammatory conditions, may be of importance in the pathogenesis of BPH.

National Category
Cell and Molecular Biology
Identifiers
urn:nbn:se:liu:diva-115751 (URN)10.1016/j.urology.2014.11.026 (DOI)000351942400059 ()25733304 (PubMedID)
Available from: 2015-03-18 Created: 2015-03-18 Last updated: 2018-01-11
Borgegard, T., Gustavsson, S., Nilsson, C., Parpal, S., Klintenberg, R., Berg, A.-L., . . . Lundkvist, J. (2012). Alzheimers Disease: Presenilin 2-Sparing gamma-Secretase Inhibition Is a Tolerable A beta Peptide-Lowering Strategy. Journal of Neuroscience, 32(48), 17297-17305
Open this publication in new window or tab >>Alzheimers Disease: Presenilin 2-Sparing gamma-Secretase Inhibition Is a Tolerable A beta Peptide-Lowering Strategy
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2012 (English)In: Journal of Neuroscience, ISSN 0270-6474, E-ISSN 1529-2401, Vol. 32, no 48, p. 17297-17305Article in journal (Refereed) Published
Abstract [en]

gamma-Secretase inhibition represents a major therapeutic strategy for lowering amyloid beta (A beta) peptide production in Alzheimers disease (AD). Progress toward clinical use of gamma-secretase inhibitors has, however, been hampered due to mechanism-based adverse events, primarily related to impairment of Notch signaling. The gamma-secretase inhibitor MRK-560 represents an exception as it is largely tolerable in vivo despite displaying only a small selectivity between A beta production and Notch signaling in vitro. In exploring the molecular basis for the observed tolerability, we show that MRK-560 displays a strong preference for the presenilin 1(PS1) over PS2 subclass of gamma-secretases and is tolerable in wild-type mice but causes dose-dependent Notch-related side effect in PS2-deficient mice at drug exposure levels resulting in a substantial decrease in brain A beta levels. This demonstrates that PS2 plays an important role in mediating essential Notch signaling in several peripheral organs during pharmacological inhibition of PS1 and provide preclinical in vivo proof of concept for PS2-sparing inhibition as a novel, tolerable and efficacious gamma-secretase targeting strategy for AD.

Place, publisher, year, edition, pages
Society for Neuroscience, 2012
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-87214 (URN)10.1523/JNEUROSCI.1451-12.2012 (DOI)000311794700025 ()
Available from: 2013-01-14 Created: 2013-01-14 Last updated: 2017-12-06
Hammarström, P., Ali Malik, M., Mishra, R., Svensson, S., Tengvall, P. & Lundström, I. (2008). A catalytic surface for amyloid fibril formation. Journal of Physics, Conference Series, 100
Open this publication in new window or tab >>A catalytic surface for amyloid fibril formation
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2008 (English)In: Journal of Physics, Conference Series, ISSN 1742-6588, E-ISSN 1742-6596, Vol. 100Article in journal (Refereed) Published
Abstract [en]

A hydrophobic surface incubated in a solution of protein molecules (insulin monomers) was made into a catalytic surface for amyloid fibril formation by repeatedly incubate, rinse and dry the surface. The present contribution describes how this unexpected transformation occurred and its relation to rapid fibrillation of insulin solutions in contact with the surface. A tentative model of the properties of the catalytic surface is given, corroborated by ellipsometric measurements of the thickness of the organic layer on the surface and by atomic force microscopy. The surfaces used were spontaneously oxidized silicon made hydrophobic through treatment in dichlorodimethylsilane.

Place, publisher, year, edition, pages
Institute of Physics (IoP), 2008
National Category
Engineering and Technology
Identifiers
urn:nbn:se:liu:diva-58432 (URN)10.1088/1742-6596/100/5/052039 (DOI)000275655200135 ()
Available from: 2010-08-12 Created: 2010-08-11 Last updated: 2018-04-25
Eriksson, T., Svensson, S., Lundström, I., Persson, K., Andersson, T. & Andersson, R. (2008). Panax ginseng induces anterograde transport of pigment organelles in Xenopus melanophores. Journal of Ethnopharmacology, 119(1), 17-23
Open this publication in new window or tab >>Panax ginseng induces anterograde transport of pigment organelles in Xenopus melanophores
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2008 (English)In: Journal of Ethnopharmacology, ISSN 0378-8741, E-ISSN 1872-7573, Vol. 119, no 1, p. 17-23Article in journal (Refereed) Published
Abstract [en]

Melanophores from Xenopus laevis are pigmented cells, capable of quick colour changes through cyclic adenosine 3':5'-monophosphate (cAMP) coordinated transport of their intracellular pigment granules, melanosomes. In this study we use the melanophore cell line to evaluate the effects of Panax ginseng extract G115 on organelle transport. Absorbance readings of melanophore-coated microplates, Correlate-EIA direct cAMP enzyme immunoassay kit, and western blot were used to measure the melanosome movement and changes in intracellular signalling. We show that Panax ginseng induces a fast concentration-dependent anterograde transport of the melanosomes. No significant increase in the cAMP level was seen and pre-incubation of melanophores with the protein kinase C (PKC) inhibitor EGF-R Fragment 651-658 (M-EGF) only partly decreased the ginseng-induced dispersion. We also demonstrate that Panax ginseng, endothelin-3 (ET-3) and alpha-melanocyte stimulating hormone (MSH) stimulate an activation of mitogen activated protein kinase (MAPK). Pre-incubation with M-EGF decreased the MAPK activity induced by ET-3 and MSH, but again only marginally affected the response of Panax ginseng. Thus, in melanophores we suggest that Panax ginseng stimulates an anterograde transport of pigment organelles via a non-cAMP and mainly PKC-independent pathway.

Place, publisher, year, edition, pages
Elsevier, 2008
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-19968 (URN)10.1016/j.jep.2008.05.024 (DOI)
Available from: 2009-08-21 Created: 2009-08-21 Last updated: 2017-12-13Bibliographically approved
Aifa, S., Miled, N., Frikha, F., Aniba, M., Svensson, S. & Rebai, A. (2006). Electrostatic interactions of peptides flanking the tyrosine kinase domain in the epidermal growth factor receptor provides a model for intracellular dimerization and autophosphorylation. Proteins: Structure, Function, and Bioinformatics, 62(4), 1036-1043
Open this publication in new window or tab >>Electrostatic interactions of peptides flanking the tyrosine kinase domain in the epidermal growth factor receptor provides a model for intracellular dimerization and autophosphorylation
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2006 (English)In: Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, E-ISSN 1097-0134, Vol. 62, no 4, p. 1036-1043Article in journal (Refereed) Published
Abstract [en]

The mechanism by which ligand-activated EGFR induces autophosphorylation via dimerization is not fully understood. Structural studies have revealed an extracellular loop mediated receptor dimerization. We have previously presented experimental data showing the involvement of a positive 13 amino acid peptide (R645-R657, P13+) from the intracellular juxtamembrane domain (JM) of EGFR important for intracellular dimerization and autophosphorylation. A model was presented that suggest that P13+ interacts with a negative peptide (D979-E991, P13-) positioned distal to the tyrosine kinase domain in the opposite EGFR monomer. The present work shows additional data strengthening this model. In fact, by analyzing protein sequences of 21 annotated ErbB proteins from 9 vertebrate genomes, we reveal the high conservation of peptides P13+ and P13- with regard to their sequence as well as their position relative to the tyrosine kinase (TK) domain. Moreover in silico structure modeling of these ErbB intracellular domains supports a general electrostatic P13+/P13- interaction, implying that the C-terminal of one receptor monomer is facing the TK domain of the other monomer in the receptor dimer and vice versa. This model provides new insights into the molecular mechanism of ErbB receptor activation and suggests a new strategy to pharmacologically interfering with ErbB receptor activity. © 2005 Wiley-Liss, Inc.

National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-33832 (URN)10.1002/prot.20780 (DOI)19902 (Local ID)19902 (Archive number)19902 (OAI)
Available from: 2009-10-09 Created: 2009-10-09 Last updated: 2018-01-26
Anderson, T., Filippini, D., Suska, A., Johansson, T., Svensson, S. & Lundström, I. (2005). Frog melanophores cultured on fluorescent microbeads: Biomimic-based biosensing. Biosensors & bioelectronics, 21(1), 111-120
Open this publication in new window or tab >>Frog melanophores cultured on fluorescent microbeads: Biomimic-based biosensing
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2005 (English)In: Biosensors & bioelectronics, ISSN 0956-5663, E-ISSN 1873-4235, Vol. 21, no 1, p. 111-120Article in journal (Refereed) Published
Abstract [en]

Melanophores are pigmented cells in lower vertebrates capable of quick color changes and thereby suitable as whole cell biosensors. In the frog dermis skin layer, the large and dark pigmented melanophore surrounds a core of other pigmented cells. Upon hormonal stimulation the black-brown pigment organelles will redistribute within the melanophore, and thereby cover or uncover the core, making complex color changes possible in the dermis. Previously, melanophores have only been cultured on flat surfaces. Here we mimic the three dimensional biological geometry in the frog dermis by culturing melanophores on fluorescent plastic microbeads. To demonstrate biosensing we use the hormones melatonin and α-melanocyte stimulating hormone (α-MSH) as lightening or darkening stimuli, respectively. Cellular responses were successfully demonstrated on single cell level by fluorescence microscopy, and in cell suspension by a fluorescence microplate reader and a previously demonstrated computer screen photo-assisted technique. The demonstrated principle is the first step towards "single well/multiple read-out" biosensor arrays based on suspensions of different selective-responding melanophores, each cultured on microbeads with distinctive spectral characteristics. By applying small amount of a clinical sample, or a candidate substance in early drug screening, to a single well containing combinations of melanophores on beads, multiple parameter read-outs will be possible. © 2004 Elsevier B.V. All rights reserved.

Keywords
pigment cells, melanophores, fluorescent microbeads, biomimic, biosensing, computer screen photo-assisted technique
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-29564 (URN)10.1016/j.bios.2004.08.043 (DOI)14939 (Local ID)14939 (Archive number)14939 (OAI)
Available from: 2009-10-09 Created: 2009-10-09 Last updated: 2017-12-13
Johansson, F., Andersson, R., Lindström, E. & Svensson, S. (2004). An indomethacin-sensitive contraction induced by β-antagonists in guinea pig airways. Canadian Journal of Physiology and Pharmacology, 82(6), 393-401
Open this publication in new window or tab >>An indomethacin-sensitive contraction induced by β-antagonists in guinea pig airways
2004 (English)In: Canadian Journal of Physiology and Pharmacology, ISSN 0008-4212, E-ISSN 1205-7541, Vol. 82, no 6, p. 393-401Article in journal (Refereed) Published
Abstract [en]

β-adrenergic receptor (β-AR) antagonists have been associated with increased airway reactivity in asthmatics and potentiation of contractile stimuli in animal models. In the present study, using an in vitro model of tracheal preparations from guinea pigs, we show that the β-AR antagonists propranolol and pindolol induce a smooth muscle contraction. A prerequisite for this contraction is that the airway preparations have been pre-treated with an β-AR agonist. Our data show that the contractile effect of β-AR antagonists is not a simple consequence of reversing the agonist-induced relaxation. Furthermore, the effect seems to be mediated through interaction with β2-ARs since the response is stereo-selective, and the selective β1-AR receptor antagonist atenolol did not induce any contractile response. SQ 29,546, a thromboxane A2 antagonist; MK 886, a lipoxygenase inhibitor; and indomethacin, a cyclooxygenase inhibitor significantly inhibited the contractions of the tracheal preparations induced with propranolol or pindolol. We put forward the hypothesis that the contractile effect of the β-AR antagonist is a consequence of their inverse agonist activity, which is only evident when the receptor population have a higher basal activity. Our results indicate a novel additional explanation for the known side effect, bronchoconstriction, of β-AR antagonist.Key words: beta antagonist, guinea pig trachea, propranolol, formoterol, pindolol, indomethacin.

Keywords
beta antagonist, guinea pig trachea, propranolol, formoterol, pindolol, indomethacin
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-23707 (URN)10.1139/y04-039 (DOI)3208 (Local ID)3208 (Archive number)3208 (OAI)
Available from: 2009-10-07 Created: 2009-10-07 Last updated: 2017-12-13Bibliographically approved
Porter, A., Svensson, S., Stamer, W., Bahl, J., Richman, J. & Reagan, J. (2003). Alpha-2adrenergic receptors stimulate actin organization in developing fetal rat cardiac myocytes. Life Sciences, 72, 1455-1466
Open this publication in new window or tab >>Alpha-2adrenergic receptors stimulate actin organization in developing fetal rat cardiac myocytes
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2003 (English)In: Life Sciences, ISSN 0024-3205, E-ISSN 1879-0631, Vol. 72, p. 1455-1466Article in journal (Refereed) Published
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-27162 (URN)11811 (Local ID)11811 (Archive number)11811 (OAI)
Available from: 2009-10-08 Created: 2009-10-08 Last updated: 2017-12-13
Filippini, D., Svensson, S. & Lundström, I. (2003). Computer screen as a programmable light source for visible absorption characterization of (bio)chemical assays. , 9(2), 240-241
Open this publication in new window or tab >>Computer screen as a programmable light source for visible absorption characterization of (bio)chemical assays
2003 (English)Article in journal (Refereed) Published
Abstract [en]

Visible absorption features suitable for color recognition and micro-plate reading of a standard bioassay are performed by the combination of a computer screen used as a programmable light source and a web camera as detector. The method provides in this way a highly available platform for 'home tests' or 'self-tests', where the requirement is to monitor well defined assays and the use of economical instrumentation is advantageous.

National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-27163 (URN)10.1039/b210677a (DOI)11812 (Local ID)11812 (Archive number)11812 (OAI)
Available from: 2009-10-08 Created: 2009-10-08 Last updated: 2011-01-13
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