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Bernhem, Kristoffer
Publications (7 of 7) Show all publications
Parmryd, I., Adler, J. & Bernhem, K. (2018). Membrane Topography can Cause Apparent Clustering - Identification and Differentiation from Genuine Clustering. Paper presented at 62nd Annual Meeting of the Biophysical-Society, FEB 17-21, 2018, San Francisco, CA. Biophysical Journal, 114(3), 165A-165A
Open this publication in new window or tab >>Membrane Topography can Cause Apparent Clustering - Identification and Differentiation from Genuine Clustering
2018 (English)In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 114, no 3, p. 165A-165AArticle in journal, Meeting abstract (Other academic) Published
Place, publisher, year, edition, pages
CELL PRESS, 2018
National Category
Biophysics
Identifiers
urn:nbn:se:kth:diva-228288 (URN)000430439600076 ()
Conference
62nd Annual Meeting of the Biophysical-Society, FEB 17-21, 2018, San Francisco, CA
Note

QC 20180521

Available from: 2018-05-21 Created: 2018-05-21 Last updated: 2018-05-21Bibliographically approved
Bernhem, K., Blom, H. & Brismar, H. (2018). Quantification of endogenous and exogenous protein expressions of Na,K-ATPase with super-resolution PALM/STORM imaging. PLoS ONE, 13(4), Article ID e0195825.
Open this publication in new window or tab >>Quantification of endogenous and exogenous protein expressions of Na,K-ATPase with super-resolution PALM/STORM imaging
2018 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 13, no 4, article id e0195825Article in journal (Refereed) Published
Abstract [en]

Transient transfection of fluorescent fusion proteins is a key enabling technology in fluorescent microscopy to spatio-temporally map cellular protein distributions. Transient transfection of proteins may however bypass normal regulation of expression, leading to overexpression artefacts like misallocations and excess amounts. In this study we investigate the use of STORM and PALM microscopy to quantitatively monitor endogenous and exogenous protein expression. Through incorporation of an N-terminal hemagglutinin epitope to a mMaple3 fused Na,K-ATPase (α1 isoform), we analyze the spatial and quantitative changes of plasma membrane Na,K-ATPase localization during competitive transient expression. Quantification of plasma membrane protein density revealed a time dependent increase of Na,K-ATPase, but no increase in size of protein clusters. Results show that after 41h transfection, the total plasma membrane density of Na,K-ATPase increased by 63% while the endogenous contribution was reduced by 16%. © 2018 Bernhem et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Place, publisher, year, edition, pages
Public Library of Science, 2018
National Category
Physical Sciences
Identifiers
urn:nbn:se:kth:diva-227364 (URN)10.1371/journal.pone.0195825 (DOI)000430802400044 ()2-s2.0-85045925649 (Scopus ID)
Note

Export Date: 9 May 2018; Article; CODEN: POLNC; Correspondence Address: Brismar, H.; Science for Life Laboratory, Department of Applied Physics, Royal Institute of TechnologySweden; email: brismar@kth.se. QC 20180604

Available from: 2018-06-04 Created: 2018-06-04 Last updated: 2018-06-04Bibliographically approved
Bernhem, K., Blom, H. & Brismar, H. (2018). Quantification of endogenous and exogenous protein expressions of Na,K-ATPase with super-resolution PALM/STORM imaging [Letter to the editor]. PLoS ONE
Open this publication in new window or tab >>Quantification of endogenous and exogenous protein expressions of Na,K-ATPase with super-resolution PALM/STORM imaging
2018 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203Article in journal, Letter (Refereed) Published
Abstract [en]

Transient transfection of fluorescent fusion proteins is a key enabling technology in fluorescent microscopy to spatio-temporally map cellular protein distributions. Transient transfection of proteins may however bypass normal regulation of expression, leading to overexpression artefacts like misallocations and excess amounts. In this study we investigate the use of STORM and PALM microscopy to quantitatively monitor endogenous and exogenous protein expression. Through incorporation of an N-terminal hemagglutinin epitope to a mMaple3 fused Na,K-ATPase (α1 isoform), we analyze the spatial and quantitative changes of plasma membrane Na,K-ATPase localization during competitive transient expression. Quantification of plasma membrane protein density revealed a time dependent increase of Na,K-ATPase, but no increase in size of protein clusters. Results show that after 41h transfection, the total plasma membrane density of Na,K-ATPase increased by 63% while the endogenous contribution was reduced by 16%.

National Category
Nano Technology
Research subject
Biological Physics
Identifiers
urn:nbn:se:kth:diva-258007 (URN)10.1371/journal. pone.0195825 (DOI)
Funder
Swedish Research Council, 2013-6041Swedish Research Council, 2015-4198Swedish Foundation for Strategic Research , RIF14-0091
Note

QC 20190916

Available from: 2019-09-09 Created: 2019-09-09 Last updated: 2019-09-16Bibliographically approved
Agostinho, A., Kouznetsova, A., Hernández-Hernández, A., Bernhem, K., Blom, H., Brismar, H. & Höög, C. (2018). Sexual dimorphism in the width of the mouse synaptonemal complex. Journal of Cell Science, 131(5), Article ID jcs212548.
Open this publication in new window or tab >>Sexual dimorphism in the width of the mouse synaptonemal complex
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2018 (English)In: Journal of Cell Science, ISSN 0021-9533, E-ISSN 1477-9137, Vol. 131, no 5, article id jcs212548Article in journal (Refereed) Published
Abstract [en]

Sexual dimorphism has been used to describe morphological differences between the sexes, but can be extended to any biologically related process that varies between males and females. The synaptonemal complex (SC) is a tripartite structure that connects homologous chromosomes in meiosis. Here, aided by superresolution microscopy techniques, we show that the SC is subject to sexual dimorphism, in mouse germ cells. We have identified a significantly narrower SC in oocytes and have established that this difference does not arise from a different organization of the lateral elements nor from a different isoform of transverse filament protein SYCP1. Instead, we provide evidence for the existence of a narrower central element and a different integration site for the C-termini of SYCP1, in females. In addition to these female-specific features, we speculate that post-translation modifications affecting the SYCP1 coiled-coil region could render a more compact conformation, thus contributing to the narrower SC observed in females.

Place, publisher, year, edition, pages
Company of Biologists Ltd, 2018
Keywords
Meiosis, SIM, STORM, Super-resolution microscopy, Synaptonemal complex
National Category
Biological Sciences
Identifiers
urn:nbn:se:kth:diva-224822 (URN)10.1242/jcs.212548 (DOI)000427877600011 ()2-s2.0-85043782610 (Scopus ID)
Funder
Science for Life Laboratory - a national resource center for high-throughput molecular bioscienceSwedish Cancer Society, 170226EU, Horizon 2020, 634113Swedish Research Council, K2013-54X-21397-04-5Swedish Foundation for Strategic Research , RIF14-0091
Note

QC 20180326

Available from: 2018-03-26 Created: 2018-03-26 Last updated: 2018-04-11Bibliographically approved
Bernhem, K., Zhang, L., Fontana, J. M., Nilsson, L., Scott, L., Brismar, H. & Aperia, A. (2017). Mapping the apoptotic process with super resolution microscopy in kidney cells challenged with high glucose. Paper presented at Annual Meeting of the American-Society-for-Pharmacology-and-Experimental-Therapeutics (ASPET) at Experimental Biology Meeting, APR 22-26, 2017, Chicago, IL. The FASEB Journal, 31
Open this publication in new window or tab >>Mapping the apoptotic process with super resolution microscopy in kidney cells challenged with high glucose
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2017 (English)In: The FASEB Journal, ISSN 0892-6638, E-ISSN 1530-6860, Vol. 31Article in journal, Meeting abstract (Other academic) Published
Place, publisher, year, edition, pages
FEDERATION AMER SOC EXP BIOL, 2017
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:kth:diva-214903 (URN)000405986502532 ()
Conference
Annual Meeting of the American-Society-for-Pharmacology-and-Experimental-Therapeutics (ASPET) at Experimental Biology Meeting, APR 22-26, 2017, Chicago, IL
Funder
Science for Life Laboratory - a national resource center for high-throughput molecular bioscience
Note

QC 20171023

Available from: 2017-10-23 Created: 2017-10-23 Last updated: 2018-02-21Bibliographically approved
Blom, H., Bernhem, K. & Brismar, H. (2016). Sodium pump organization in dendritic spines. NEUROPHOTONICS, 3(4), Article ID 041803.
Open this publication in new window or tab >>Sodium pump organization in dendritic spines
2016 (English)In: NEUROPHOTONICS, ISSN 2329-423X, Vol. 3, no 4, article id 041803Article in journal (Refereed) Published
Abstract [en]

Advancement in fluorescence imaging with the invention of several super-resolution microscopy modalities (e.g., PALM/STORM and STED) has opened up the possibility of deciphering molecular distributions on the nanoscale. In our quest to better elucidate postsynaptic protein distribution in dendritic spines, we have applied these nanoscopy methods, where generated results could help improve our understanding of neuronal functions. In particular, we have investigated the principal energy transformer in the brain, i.e., the Na+; K+-ATPase (or sodium pump), an essential protein responsible for maintaining resting membrane potential and a major controller of intracellular ion homeostasis. In these investigations, we have focused on estimates of protein amount, giving assessments of how variations may depend on labeling strategies, sample analysis, and choice of nanoscopic imaging method, concluding that all can be critical factors for quantification. We present a comparison of these results and discuss the influences this may have for homeostatic sodium regulation in neurons and energy consumption.

Place, publisher, year, edition, pages
SPIE - International Society for Optical Engineering, 2016
Keywords
dendritic spine, sodium pump, photoactivated localization microscopy, stimulated emission depletion microscopy
National Category
Neurosciences Neurology
Identifiers
urn:nbn:se:kth:diva-194264 (URN)10.1117/1.NPh.3.4.041803 (DOI)000384427300002 ()27175374 (PubMedID)2-s2.0-84979072971 (Scopus ID)
Note

QC 20161024

Available from: 2016-10-24 Created: 2016-10-21 Last updated: 2018-01-14Bibliographically approved
Fontana, J. M., Bernhem, K., Zhang, L., Nilsson, L., Blom, H., Brismar, H. & Aperia, A. (2015). Ouabain, a Na, K-ATPase ligand, intervenes with the onset of glucose-triggered apoptosis. Molecular Biology of the Cell, 26
Open this publication in new window or tab >>Ouabain, a Na, K-ATPase ligand, intervenes with the onset of glucose-triggered apoptosis
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2015 (English)In: Molecular Biology of the Cell, ISSN 1059-1524, E-ISSN 1939-4586, Vol. 26Article in journal, Meeting abstract (Other academic) Published
Place, publisher, year, edition, pages
AMER SOC CELL BIOLOGY, 2015
National Category
Cell and Molecular Biology
Identifiers
urn:nbn:se:kth:diva-242778 (URN)000209928500656 ()
Note

QC 20190211

Available from: 2019-02-11 Created: 2019-02-11 Last updated: 2019-02-11Bibliographically approved
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