Change search
Link to record
Permanent link

Direct link
BETA
Alternative names
Publications (10 of 30) Show all publications
Uematsu, K., Heiman, M., Zelenina, M., Padovan, J., Chait, B. T., Aperia, A., . . . Greengard, P. (2015). Protein kinase A directly phosphorylates metabotropic glutamate receptor 5 to modulate its function. Journal of Neurochemistry, 132(6), 677-686.
Open this publication in new window or tab >>Protein kinase A directly phosphorylates metabotropic glutamate receptor 5 to modulate its function
Show others...
2015 (English)In: Journal of Neurochemistry, ISSN 0022-3042, E-ISSN 1471-4159, Vol. 132, no 6, 677-686 p.Article in journal (Refereed) Published
Abstract [en]

Metabotropic glutamate receptor 5 (mGluR5) regulates excitatory post-synaptic signaling in the central nervous system (CNS) and is implicated in various CNS disorders. Protein kinase A (PKA) signaling is known to play a critical role in neuropsychiatric disorders such as Parkinson's disease, schizophrenia, and addiction. Dopamine signaling is known to modulate the properties of mGluR5 in a cAMP-and PKA-dependent manner, suggesting that mGluR5 may be a direct target for PKA. Our study identifies mGluR5 at Ser870 as a direct substrate for PKA phosphorylation and demonstrates that this phosphorylation plays a critical role in the PKA-mediated modulation of mGluR5 functions such as extracellular signal-regulated kinase phosphorylation and intracellular Ca2+ oscillations. The identification of the molecular mechanism by which PKA signaling modulates mGluR5-mediated cellular responses contributes to the understanding of the interaction between dopaminergic and glutamatergic neuronal signaling.

National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:kth:diva-164471 (URN)10.1111/jnc.13038 (DOI)000351392800006 ()25639954 (PubMedID)2-s2.0-84924586659 (Scopus ID)
Note

QC 20150422

Available from: 2015-04-22 Created: 2015-04-17 Last updated: 2017-12-04Bibliographically approved
Errando-Herranz, C., Vastesson, A., Zelenina, M., Pardon, G., Bergström, G., Wijngaart, W. v., . . . Gylfason, K. B. (2013). Biocompatibility of OSTE polymers studied by cell growth experiments. In: Proceedings of the 17th Int. Conf. on Miniaturized Systems for Chemistry  and Life Sciences (microTAS): . Paper presented at The 17th International Conference on Miniaturized Systems for Chemistry and Life Sciences (MicroTAS 2013), Freiburg, 27-31 October 2013. Freiburg, Germany.
Open this publication in new window or tab >>Biocompatibility of OSTE polymers studied by cell growth experiments
Show others...
2013 (English)In: Proceedings of the 17th Int. Conf. on Miniaturized Systems for Chemistry  and Life Sciences (microTAS), Freiburg, Germany, 2013Conference paper, Published paper (Refereed)
Abstract [en]

The recently introduced OSTE polymer technology has shown very useful features for microfluidics for lab-on-a-chip applications. However, no data has yet been published on cell viability on OSTE. In this work, we study the biocompatibility of three OSTE formulations by cell growth experiments. Moreover, we investigate the effect of varying thiol excess on cell viability on OSTE surfaces. The results show poor cell viability on one OSTE formulation, and viability comparable with polystyrene on a second formulation with thiol excess below 60%. In the third formulation, we observe cell proliferation. These results are promising for cell-based assays in OSTE microfluidic devices.

Place, publisher, year, edition, pages
Freiburg, Germany: , 2013
Keyword
loc OSTE lab-on-chip biocompatibility
National Category
Medical Materials
Identifiers
urn:nbn:se:kth:diva-129546 (URN)2-s2.0-84907370206 (Scopus ID)
Conference
The 17th International Conference on Miniaturized Systems for Chemistry and Life Sciences (MicroTAS 2013), Freiburg, 27-31 October 2013
Projects
CellRing
Funder
Swedish Research Council, B0460801EU, European Research Council, 267528
Note

QC 20131122

Available from: 2013-10-02 Created: 2013-10-02 Last updated: 2017-10-02Bibliographically approved
Dånmark, S., Gladnikoff, M., Frisk, T., Zelenina, M., Mustafa, K., Russom, A. & Finne-Wistrand, A. (2012). Development of a novel microfluidic device for long-term in situ monitoring of live cells in 3-dimensional matrices. Biomedical microdevices (Print), 14(5), 885-893.
Open this publication in new window or tab >>Development of a novel microfluidic device for long-term in situ monitoring of live cells in 3-dimensional matrices
Show others...
2012 (English)In: Biomedical microdevices (Print), ISSN 1387-2176, E-ISSN 1572-8781, Vol. 14, no 5, 885-893 p.Article in journal (Refereed) Published
Abstract [en]

Using the latest innovations in microfabrication technology, 3-dimensional microfluidic cell culture systems have been developed as an attractive alternative to traditional 2-dimensional culturing systems as a model for long-term microscale cell-based research. Most microfluidic systems are based on the embedding of cells in hydrogels. However, physiologically realistic conditions based on hydrogels are difficult to obtain and the systems are often too complicated. We have developed a microfluidic cell culture device that incorporates a biodegradable rigid 3D polymer scaffold using standard soft lithography methods. The device permits repeated high-resolution fluorescent imaging of live cell populations within the matrix over a 4 week period. It was also possible to track cell development at the same spatial location throughout this time. In addition, human primary periodontal ligament cells were induced to produce quantifiable calcium deposits within the system. This simple and versatile device should be readily applicable for cell-based studies that require long-term culture and high-resolution bioimaging.

Keyword
Microfabrication, Soft lithography, Live cell imaging, 3-dimensional cell culture
National Category
Other Medical Engineering
Identifiers
urn:nbn:se:kth:diva-103760 (URN)10.1007/s10544-012-9668-1 (DOI)000308963200009 ()2-s2.0-84870298439 (Scopus ID)
Funder
EU, FP7, Seventh Framework Programme, 242175-VascuBoneScience for Life Laboratory - a national resource center for high-throughput molecular bioscience
Note

QC 20121029

Available from: 2012-10-29 Created: 2012-10-19 Last updated: 2017-12-07Bibliographically approved
Ringman Uggla, A., von Schewelov, K., Zelenina, M., Aperia, A. & Frenckner, B. (2011). Low pulmonary expression of epithelial Na(+) channel and Na(+), K(+)-ATPase in newborn infants with congenital diaphragmatic hernia. Neonatology, 99(1), 14-22.
Open this publication in new window or tab >>Low pulmonary expression of epithelial Na(+) channel and Na(+), K(+)-ATPase in newborn infants with congenital diaphragmatic hernia
Show others...
2011 (English)In: Neonatology, ISSN 1661-7800, E-ISSN 1661-7819, Vol. 99, no 1, 14-22 p.Article in journal (Refereed) Published
Abstract [en]

BACKGROUND: It has been suggested from several animal studies and clinical observations that congenital diaphragmatic hernia (CDH) with pulmonary hypoplasia is accompanied by a disturbed perinatal ion transport. This could lead to respiratory distress due to slower clearance of fetal lung fluid at birth.

OBJECTIVES: The purpose of this study was to determine whether CDH is related to changes in the expression of three rate-limiting transporter proteins in lung epithelium at birth.

METHODS: Tracheal aspirate was collected from 12 newborn infants with CDH and from 8 newborn control patients. Sampling was performed at postnatal age 18 and at 43 h in the CDH group and at 18 h in the control group. The protein abundance of α-, β- and γ-epithelial Na(+) channel (ENaC), aquaporin 5 and Na(+), K(+)-ATPase α(1) was analyzed using semiquantitative immunoblotting.

RESULTS: The levels of β-ENaC, γ-ENaC and Na(+), K(+)-ATPase α(1) collected at 18 h postnatally were significantly lower in CDH infants compared to control infants. In the CDH group, no significant difference in the expression of the ENaC subunits, Na(+), K(+)-ATPase α(1) or aquaporin 5 could be detected between the two sampling time points.

CONCLUSIONS: This downregulation may result in an abnormal lung fluid absorption which could be an important mechanism behind the respiratory distress seen in newborn CDH patients.

Keyword
Aquaporin, Pulmonary hypoplasia, Ion transport, Tracheal aspirate fluid, Perinatal clearance of lung fluid
National Category
Cell Biology Respiratory Medicine and Allergy Pediatrics
Identifiers
urn:nbn:se:kth:diva-80458 (URN)10.1159/000292503 (DOI)000282172800003 ()20588066 (PubMedID)2-s2.0-77953930731 (Scopus ID)
Note
QC 20120210Available from: 2012-02-09 Created: 2012-02-09 Last updated: 2017-12-07Bibliographically approved
Li, Y., Zelenina, M., Plat-Willson, G., Marcoux, M.-O., Aperia, A. & Casper, C. (2011). Urinary aquaporin-2 excretion during ibuprofen or indomethacin treatment in preterm infants with patent ductus arteriosus. Acta Paediatrica, 100(1), 59-66.
Open this publication in new window or tab >>Urinary aquaporin-2 excretion during ibuprofen or indomethacin treatment in preterm infants with patent ductus arteriosus
Show others...
2011 (English)In: Acta Paediatrica, ISSN 0803-5253, E-ISSN 1651-2227, Vol. 100, no 1, 59-66 p.Article in journal (Refereed) Published
Abstract [en]

Aim: Water channel AQP2 is the target for vasopressin (AVP) and a major determinant of urinary concentrating capacity. In mature kidneys, prostaglandins counteract the effect of AVP on AQP2 expression at functional sites. We investigated whether disturbances in water homeostasis in infants with patent ductus arteriosus (PDA) treated with prostaglandin inhibitors can be attributed to activation of AQP2. Methods: In 53 infants with symptomatic PDA (gestational age 24-33 weeks), 30 receiving ibuprofen and 23 indomethacin starting at 2-15 days of life, clinical and biochemical data were collected before treatment and after each dose of the drugs. Urinary AQP2 was determined by dot immunoblotting. Results: Urinary AQP2 level and osmolality were decreased in both groups. Urinary osmolality was overall low and correlated inversely with fluid uptake. In ibuprofen group, there was no correlation of AQP2 level with urinary osmolality. Conclusion: There was no AQP2 upregulation in the infants. The low urinary osmolality and dissociation between urinary osmolality and urinary AQP2 level indicate that the fluid retention sometimes observed in PDA infants treated with prostaglandin inhibitors is not caused by increased levels of functional AQP2. Thus, knowledge about the renal physiology of the adult cannot always be transferred to the infant kidney.

Place, publisher, year, edition, pages
Wiley-Blackwell, 2011
Keyword
Aquaporin-2, Ibuprofen, Indomethacin, Patent ductus arteriosus, Preterm infants
National Category
Pediatrics Cell and Molecular Biology Urology and Nephrology Cardiac and Cardiovascular Systems
Identifiers
urn:nbn:se:kth:diva-29541 (URN)10.1111/j.1651-2227.2010.01943.x (DOI)000285101100016 ()2-s2.0-78650136543 (Scopus ID)
Funder
Swedish Research Council
Note

QC 20110207

Available from: 2011-02-07 Created: 2011-02-07 Last updated: 2018-01-12Bibliographically approved
Fenton, R. A., Moeller, H. B., Zelenina, M., Snaebjornsson, M. T., Holen, T. & MacAulay, N. (2010). Differential water permeability and regulation of three aquaporin 4 isoforms. Cellular and Molecular Life Sciences (CMLS), 67(5), 829-840.
Open this publication in new window or tab >>Differential water permeability and regulation of three aquaporin 4 isoforms
Show others...
2010 (English)In: Cellular and Molecular Life Sciences (CMLS), ISSN 1420-682X, E-ISSN 1420-9071, Vol. 67, no 5, 829-840 p.Article in journal (Refereed) Published
Abstract [en]

Aquaporin 4 (AQP4) is expressed in the perivascular glial endfeet and is an important pathway for water during formation and resolution of brain edema. In this study, we examined the functional properties and relative unit water permeability of three functional isoforms of AQP4 expressed in the brain (M1, M23, Mz). The M23 isoform gave rise to square arrays when expressed in Xenopus laevis oocytes. The relative unit water permeability differed significantly between the isoforms in the order of M1 > Mz > M23. None of the three isoforms were permeable to small osmolytes nor were they affected by changes in external K+ concentration. Upon protein kinase C (PKC) activation, oocytes expressing the three isoforms demonstrated rapid reduction of water permeability, which correlated with AQP4 internalization. The M23 isoform was more sensitive to PKC regulation than the longer isoforms and was internalized significantly faster. Our results suggest a specific role for square array formation.

Keyword
Aquaporin, Glial cells, Water permeability, Regulation, Protein kinase, C, Isoforms, xenopus-laevis oocytes, retinal muller cells, orthogonal arrays, subcellular-distribution, cultured astrocytes, circulatory arrest, plasma-membranes, epithelial-cells, high-resolution, square arrays
National Category
Cell Biology Biochemistry and Molecular Biology Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:kth:diva-19226 (URN)10.1007/s00018-009-0218-9 (DOI)000274655600012 ()2-s2.0-77949910179 (Scopus ID)
Note
QC 20110210Available from: 2010-08-05 Created: 2010-08-05 Last updated: 2017-12-12Bibliographically approved
Zelenina, M. (2010). Regulation of brain aquaporins. Neurochemistry International, 57(4), 468-488.
Open this publication in new window or tab >>Regulation of brain aquaporins
2010 (English)In: Neurochemistry International, ISSN 0197-0186, E-ISSN 1872-9754, Vol. 57, no 4, 468-488 p.Article in journal (Refereed) Published
Abstract [en]

Three aquaporins are expressed in the brain. AQP4, the predominant brain water channel, is expressed in astrocyte endfeet facing brain capillaries, perisynaptic spaces, and nodes of Ranvier. It is implicated in brain edema formation and resolution. It is also believed to assist clearance of K+. released during neuronal activity. AQP1 is expressed in epithelial cells of choroid plexus and is implicated in cerebrospinal fluid formation. AQP9, which has been reported to be present in astrocytes and in subpopulations of neurons, is implicated in the brain energy metabolism. All three brain AQPs are strongly upregulated in brain tumors and in injured brain tissue. Water and solute transport via AQPs depends on concentration gradients across the membrane, but the magnitude of the transport is to a large extent determined by the single channel permeability of AQPs and by their abundance in the cell membrane. The future therapies will have to address not only the forces driving the water and solute transport (e.g. as mannitol infusion does in the treatment of brain edema), but also the regulation of AQPs, which provide the means for water entry to the brain, for water exit from the brain, and for redistribution of water and solutes within the brain compartments. This review summarizes the data concerning structure, permeability, role in the brain, short-term and long-term regulation of the three AQPs.

Keyword
Water channel, Astrocyte, Regulation, Phosphorylation, Permeability, Expression
National Category
Neurosciences Cell and Molecular Biology Cell Biology
Identifiers
urn:nbn:se:kth:diva-29208 (URN)10.1016/j.neuint.2010.03.022 (DOI)000282472300018 ()2-s2.0-77956212144 (Scopus ID)
Note

QC 20110131

Available from: 2011-01-31 Created: 2011-01-27 Last updated: 2018-01-12Bibliographically approved
Vieux, R., Zelenina, M., Aperia, A. & Hascoët, J.-M. (2010). The renal adverse effects of ibuprofen are not mediated by AQP2 water channels. Pediatric nephrology (Berlin, West), 25(7), 1277-1284.
Open this publication in new window or tab >>The renal adverse effects of ibuprofen are not mediated by AQP2 water channels
2010 (English)In: Pediatric nephrology (Berlin, West), ISSN 0931-041X, E-ISSN 1432-198X, Vol. 25, no 7, 1277-1284 p.Article in journal (Refereed) Published
Abstract [en]

The aim of this study was to determine (1) whether ibuprofen treatment in very preterm infants causes an increase in the renal water channel aquaporin-2 (AQP2) activity in the collecting duct via prostaglandin synthesis inhibition and (2) whether AQP2 activity remains disturbed long after ibuprofen treatment has ended. This was a prospective study involving premature infants with a gestation age of 27-31 weeks who received treatment between December 2005 and August 2006 in a tertiary Neonatal Intensive Care Unit. Each ibuprofen-treated infant was matched to two controls. Renal glomerular and tubular function were evaluated weekly for 1 month, and urinary AQP2 was measured by immuno-dotting. In total, 166 longitudinal samples were analyzed in 36 infants. Median [interquartile range] gestational age and birthweight were 28 [27.0-29.5] weeks and 1160 [1041-1242] g, respectively. Perinatal factors were similar in both groups. Urine output was significantly decreased in the ibuprofen-treated infants during the treatment. The urinary AQP2 level decreased significantly from day 2 to day 7 in both groups and was similar thereafter for the first month of life in ibuprofen-treated and control groups. Based on our results, we conclude that ibuprofen-induced oligo-anuria is not associated with a change in AQP2 activity and that ibuprofen does not affect AQP2 activity during the first month of life in very preterm neonates.

Keyword
Aquaporin-2, Ibuprofen, Neonatal intensive care unit, Patent ductus arteriosus, Renal function
National Category
Cell Biology Urology and Nephrology Pediatrics
Identifiers
urn:nbn:se:kth:diva-80459 (URN)10.1007/s00467-010-1487-0 (DOI)000277940700011 ()20390303 (PubMedID)2-s2.0-77954537425 (Scopus ID)
Note
QC 20120210Available from: 2012-02-09 Created: 2012-02-09 Last updated: 2017-12-07Bibliographically approved
Zelenin, S., Zelenina, M., Li, Y., Kamali-Zare, P., Bondar, A., Brismar, H. & Aperia, A. (2009). AQP4 role in renal K+ transport. The FASEB Journal, 23, 867.2.
Open this publication in new window or tab >>AQP4 role in renal K+ transport
Show others...
2009 (English)In: The FASEB Journal, ISSN 0892-6638, E-ISSN 1530-6860, Vol. 23, 867.2- p.Article in journal, Meeting abstract (Other academic) Published
Abstract [en]

The collecting duct principle cells (PC) play a major role for concentration of urine and regulation of K+ homeostasis. Two water channels, AQP3 and AQP4, are expressed in the PC basolateral membrane (BLM). Here we present evidence that AQP4 participates in regulation of renal K+ transport. K+ enters the cell via Na+,K+-ATPase mediated transport in BLM. The presence of K+ channels in BLM, which is deeply infolded, thus providing a diffusion limited space, permits K+ recirculation, considered important for maintenance of membrane potential. Here we show with co-immunoprecipitation and GST pulldown assays, that in rat renal papilla, AQP4, but not AQP3, assembles with Na+,K+-ATPase and the K+ channel Kir7.1. This led us to hypothesize that AQP4, Na+,K+-ATPase and Kir7.1 form a K+ transporting microdomain, where AQP4 water transport maintains a favorable gradient for K+ efflux and stabilizes membrane potential. A mathematical model of K+ transport across an epithelial cells with a deeply infolded BLM supported the hypothesis and predicted an even higher impact of AQP water transport on K+ transport if AQP water permeability is sensitive to fluctuations in extracellular K+ concentration ([K+]o). To test this, AQP3 and AQP4 were expressed in MDCK cells, a cell line with much in common with PC. Water permeability was increased when [K+]o was 12mM in cells expressing AQP4 but not in cells expressing AQP3.

Place, publisher, year, edition, pages
American Societies for Experimental Biology, 2009
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:kth:diva-138116 (URN)000208621502239 ()
Note

QC 20131218. QC 20160209

Available from: 2013-12-18 Created: 2013-12-18 Last updated: 2017-12-06Bibliographically approved
Gunnarson, E., Zelenina, M., Song, Y., Illarionova, N., Brismar, H., Andersson, U., . . . Aperia, A. (2009). Effect of the brain protecting agent erythropoietin on astrocyte function. In: : . Paper presented at 9thEuropean Meeting on Glial Cells in Health and Disease, Paris, France, 2009 (pp. S70-S70). , 57(13).
Open this publication in new window or tab >>Effect of the brain protecting agent erythropoietin on astrocyte function
Show others...
2009 (English)Conference paper, Published paper (Refereed)
Series
GLIA, ISSN 0894-1491
National Category
Cell Biology Neurosciences
Identifiers
urn:nbn:se:kth:diva-18779 (URN)000270075500291 ()
Conference
9thEuropean Meeting on Glial Cells in Health and Disease, Paris, France, 2009
Note

QC 20100525

Available from: 2010-08-05 Created: 2010-08-05 Last updated: 2018-01-12Bibliographically approved
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0003-3402-9672

Search in DiVA

Show all publications