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Article ; Online: Functional Analysis of Connexin Channels in Cultured Cells by Neurobiotin Injection and Visualization.

Wörsdörfer, Philipp / Willecke, Klaus

2017 Volume 7, Issue 11, Page(s) e2325

Abstract: Functional gap junction channels between neighboring cells can be assessed by microinjection of low molecular weight tracer substances into cultured cells. The extent of direct intercellular communication can be precisely quantified by this method. This ... ...

Abstract	Functional gap junction channels between neighboring cells can be assessed by microinjection of low molecular weight tracer substances into cultured cells. The extent of direct intercellular communication can be precisely quantified by this method. This protocol describes the iontophoretic injection and visualisation of Neurobiotin into cultured cells.
Language	English
Publishing date	2017-06-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	2833269-6
ISSN	2331-8325 ; 2331-8325
ISSN (online)	2331-8325
ISSN	2331-8325
DOI	10.21769/BioProtoc.2325
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Article ; Online: Connexin-caused genetic diseases and corresponding mouse models.

Dobrowolski, Radoslaw / Willecke, Klaus

Antioxidants & redox signaling

2009 Volume 11, Issue 2, Page(s) 283–295

Abstract: The human and mouse genomes contain 21 and 20 connexin genes, respectively. During the last 10-year period, genetic research on connexins has been stimulated by two parallel approaches: first, the characterization of genetic diseases that are caused by ... ...

Abstract	The human and mouse genomes contain 21 and 20 connexin genes, respectively. During the last 10-year period, genetic research on connexins has been stimulated by two parallel approaches: first, the characterization of genetic diseases that are caused by connexin mutations and, second, the generation and characterization of connexin knockout (null) mutated mice in which the coding region of nearly all connexin genes has been deleted. We summarize the current results of each of these two approaches. More recently, first results have been published in which connexin point mutations in human connexin genes were inserted at the corresponding position of the orthologous mouse gene. Under these conditions, the mutated connexin protein is expressed, in contrast to a connexin null mutation, and its interaction with other connexin isoforms or other connexin-binding proteins can be maintained. In this review, we discuss advantages and problems of such an approach and possible implications regarding the mechanism of the disease. The long-term goal is to understand the biologic function of each connexin isoform and the contribution of these proteins to the physiology of the corresponding organs in health and disease.
MeSH term(s)	Animals ; Connexins/genetics ; Connexins/physiology ; Disease Models, Animal ; Gap Junctions/genetics ; Gap Junctions/physiology ; Genetic Diseases, Inborn/etiology ; Genetic Diseases, Inborn/genetics ; Humans ; Mice ; Models, Biological ; Mutation ; Point Mutation ; Protein Isoforms/genetics ; Protein Isoforms/physiology
Chemical Substances	Connexins ; Protein Isoforms
Language	English
Publishing date	2009-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1483836-9
ISSN	1557-7716 ; 1523-0864
ISSN (online)	1557-7716
ISSN	1523-0864
DOI	10.1089/ars.2008.2128
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Zs.A 5488: Show issues

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Article ; Online: Connexin47 protein phosphorylation and stability in oligodendrocytes depend on expression of Connexin43 protein in astrocytes.

May, Dennis / Tress, Oliver / Seifert, Gerald / Willecke, Klaus

The Journal of neuroscience : the official journal of the Society for Neuroscience

2013 Volume 33, Issue 18, Page(s) 7985–7996

Abstract: Panglial networks are essential for normal physiology in the CNS, and the function of distinct connexins participating in these networks is not well understood. We generated Connexin32 (Cx32)-deficient mice with additional deletion of astrocytic Cx43 to ... ...

Abstract	Panglial networks are essential for normal physiology in the CNS, and the function of distinct connexins participating in these networks is not well understood. We generated Connexin32 (Cx32)-deficient mice with additional deletion of astrocytic Cx43 to explore the role of both connexins in panglial networks. Cx43/Cx32 double knock-out (dKO) mice revealed strong microglial activation in corpus callosum and cingulum along with severe astrogliosis and scar formation. In addition, most of the fine myelinated fibers projecting from the corpus callosum into the cortex were lost. Myelin loss was caused by a strong decrease of oligodendrocytes in the cingulum of Cx43/Cx32dKO mice. Immunoblot analyses using newly generated specific Cx47 antibodies revealed that oligodendrocytic Cx47 is phosphorylated in vivo depending on astrocytic Cx43 expression. In Cx43-deficient mice, Cx47 protein levels were strongly decreased, whereas Cx47 mRNA levels were not altered. Using Cx43G138R/Cx30KO mice, we show that Cx47 expression depends on the presence of astrocytic Cx43 protein and that its gap junctional channel function is not necessary for Cx47 stabilization. In consequence, Cx43/Cx32dKO mice additionally lack Cx47 expression and therefore cannot form oligodendrocytic gap junctions, which explains the phenotypic similarities to Cx32/Cx47dKO mice. Our findings provide strong evidence that phosphorylation and stability of oligodendrocytic Cx47 proteins is dependent on astrocytic Cx43 expression. These results further unravel the complexity of panglial networks and show that results of previous studies using astrocytic Cx43-deficient mice have to be reconsidered.
MeSH term(s)	Age Factors ; Animals ; Astrocytes/physiology ; Basic Helix-Loop-Helix Transcription Factors/metabolism ; Central Nervous System/cytology ; Connexin 43/genetics ; Connexin 43/metabolism ; Connexins/genetics ; Connexins/metabolism ; Gene Expression Regulation/genetics ; Glial Fibrillary Acidic Protein/metabolism ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Intermediate Filament Proteins/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Myelin Sheath/metabolism ; Nerve Tissue Proteins/metabolism ; Nestin ; Oligodendrocyte Transcription Factor 2 ; Oligodendroglia/physiology ; Phosphorylation ; RNA, Messenger/metabolism ; Gap Junction beta-1 Protein
Chemical Substances	Basic Helix-Loop-Helix Transcription Factors ; Connexin 43 ; Connexins ; Glial Fibrillary Acidic Protein ; Intermediate Filament Proteins ; Nerve Tissue Proteins ; Nes protein, mouse ; Nestin ; Olig2 protein, mouse ; Oligodendrocyte Transcription Factor 2 ; RNA, Messenger ; connexin 47 ; Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2013-04-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	604637-x
ISSN	1529-2401 ; 0270-6474
ISSN (online)	1529-2401
ISSN	0270-6474
DOI	10.1523/JNEUROSCI.5874-12.2013
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Article ; Online: Expression of connexin genes in the human retina

Joussen Antonia / Söhl Goran / Kociok Norbert / Willecke Klaus

BMC Ophthalmology, Vol 10, Iss 1, p

2010 Volume 27

Abstract: Abstract Background Gap junction channels allow direct metabolically and electrical coupling between adjacent cells in various mammalian tissues. Each channel is composed of 12 protein subunits, termed connexins (Cx). In the mouse retina, Cx43 could be ... ...

Abstract	Abstract Background Gap junction channels allow direct metabolically and electrical coupling between adjacent cells in various mammalian tissues. Each channel is composed of 12 protein subunits, termed connexins (Cx). In the mouse retina, Cx43 could be localized mostly between astroglial cells whereas expression of Cx36, Cx45 and Cx57 genes has been detected in different neuronal subtypes. In the human retina, however, the expression pattern of connexin genes is largely unknown. Methods Northern blot hybridizations, RT-PCR as well as immunofluorescence analyses helped to explore at least partially the expression pattern of the following human connexin genes GJD2 (hCx36), GJC1 (hCx45), GJA9 (hCx59) and GJA10 (hCx62) in the human retina. Results Here we report that Northern blot hybridization signals of the orthologuous hCx36 and hCx45 were found in human retinal RNA. Immunofluorescence signals for both connexins could be located in both inner and outer plexiform layer (IPL, OPL). Expression of a third connexin gene denoted as GJA10 (Cx62) was also detected after Northern blot hybridization in the human retina. Interestingly, its gene structure is similar to that of Gja10 (mCx57) being expressed in mouse horizontal cells. RT-PCR analysis suggested that an additional exon of about 25 kb further downstream, coding for 12 amino acid residues, is spliced to the nearly complete reading frame on exon2 of GJA10 (Cx62). Cx59 mRNA, however, with high sequence identity to zebrafish Cx55.5 was only weakly detectable by RT-PCR in cDNA of human retina. Conclusion In contrast to the neuron-expressed connexin genes Gjd2 coding for mCx36, Gjc1 coding for mCx45 and Gja10 coding for mCx57 in the mouse, a subset of 4 connexin genes, including the unique GJA9 (Cx59) and GJA10 (Cx62), could be detected at least as transcript isoforms in the human retina. First immunofluorescence analyses revealed a staining pattern of hCx36 and hCx45 expression both in the IPL and OPL, partially reminiscent to that in the mouse, although additional post-mortem material is needed to further explore their sublamina-specific distribution. Appropriate antibodies against Cx59 and Cx62 protein will clarify expression of these proteins in future studies.
Keywords	Ophthalmology ; RE1-994 ; Medicine ; R ; DOAJ:Ophthalmology ; DOAJ:Medicine (General) ; DOAJ:Health Sciences
Subject code	616
Language	English
Publishing date	2010-10-01T00:00:00Z
Publisher	BioMed Central
Document type	Article ; Online
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Article ; Online: Correction to: Disease-linked connexin26 S17F promotes volar skin abnormalities and mild wound healing defects in mice.

Press, Eric / Alaga, Katanya C / Barr, Kevin / Shao, Qing / Bosen, Felicitas / Willecke, Klaus / Laird, Dale W

Cell death & disease

2018 Volume 9, Issue 6, Page(s) 630

Abstract: Correction to: NPG Asia Materials (2018) https://doi.org/10.1038/s41427-018-0014-9 published online on 16 April 2018. ...

Abstract	Correction to: NPG Asia Materials (2018) https://doi.org/10.1038/s41427-018-0014-9 published online on 16 April 2018.
Language	English
Publishing date	2018-05-24
Publishing country	England
Document type	Published Erratum
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/s41419-018-0639-1
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Article ; Online: Synopsis of the International Gap Junction Conference in Elsinore, Denmark August 5-9, 2007.

Willecke, Klaus / Nielsen, Morten Schak

Cell communication & adhesion

2007 Volume 14, Issue 6, Page(s) 251–257

Abstract: This synopsis covers the main results and conclusions from the platform presentations during the International Gap Junction Conference. More detailed information is provided in the mini reviews on controversial scientific issues, short reports of ... ...

Abstract	This synopsis covers the main results and conclusions from the platform presentations during the International Gap Junction Conference. More detailed information is provided in the mini reviews on controversial scientific issues, short reports of research results and conference abstracts published in this issue of Cell Communication and Adhesion.
MeSH term(s)	Cell Communication ; Gap Junctions ; Humans
Language	English
Publishing date	2007-11
Publishing country	England
Document type	Journal Article
ZDB-ID	2065474-1
ISSN	1543-5180 ; 1061-5385 ; 1541-9061
ISSN (online)	1543-5180
ISSN	1061-5385 ; 1541-9061
DOI	10.1080/15419060801891000
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Zs.A 4377: Show issues

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Article: Epidermal 1‐O‐acylceramides appear with the establishment of the water permeability barrier in mice and are produced by maturating keratinocytes

Lipids. 2022 May, v. 57, no. 3

2022

Abstract: 1‐O‐Acylceramides (1‐OACs) have a fatty acid esterified to the 1‐hydroxyl of the sphingosine head group of the ceramide, and recently we identified these lipids as natural components of human and mouse epidermis. Here we show epidermal 1‐OACs arise ... ...

Abstract	1‐O‐Acylceramides (1‐OACs) have a fatty acid esterified to the 1‐hydroxyl of the sphingosine head group of the ceramide, and recently we identified these lipids as natural components of human and mouse epidermis. Here we show epidermal 1‐OACs arise shortly before birth during the establishment of the water permeability barrier in mice. Fractionation of human epidermis indicates 1‐OACs concentrate in the stratum corneum. During in vitro maturation into reconstructed human epidermis, human keratinocytes dramatically increase 1‐OAC levels indicating they are one source of epidermal 1‐OACs. In search of potential enzymes responsible for 1‐OAC synthesis in vivo, we analyzed mutant mice with deficiencies of ceramide synthases (Cers2, Cers3, or Cers4), diacylglycerol acyltransferases (Dgat1 or Dgat2), elongase of very long fatty acids 3 (Elovl3), lecithin cholesterol acyltransferase (Lcat), stearoyl‐CoA desaturase 1 (Scd1), or acidic ceramidase (Asah1). Overall levels of 1‐OACs did not decrease in any mouse model. In Cers3 and Dgat2‐deficient epidermis they even increased in correlation with deficient skin barrier function. Dagt2 deficiency reshapes 1‐OAC synthesis with an increase in 1‐OACs with N‐linked non‐hydroxylated fatty acids and a 60% decrease compared to control in levels of 1‐OACs with N‐linked hydroxylated palmitate. As none of the single enzyme deficiencies we examined resulted in a lack of 1‐OACs, we conclude that either there is functional redundancy in forming 1‐OAC and more than one enzyme is involved, and/or an unknown acyltransferase of the epidermis performs the final step of 1‐OAC synthesis, the implications of which are discussed.
Keywords	artificial skin ; ceramides ; cholesterol acyltransferase ; diacylglycerol acyltransferase ; esterification ; fatty acids ; fractionation ; humans ; hydroxylation ; keratinocytes ; lecithins ; mice ; mutants ; palmitates ; permeability ; sphingosine ; stearoyl-CoA desaturase
Language	English
Dates of publication	2022-05
Size	p. 183-195.
Publishing place	John Wiley & Sons, Inc.
Document type	Article
Note	JOURNAL ARTICLE
ZDB-ID	241539-2
ISSN	1558-9307 ; 0024-4201
ISSN (online)	1558-9307
ISSN	0024-4201
DOI	10.1002/lipd.12342
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Article ; Online: Epidermal 1-O-acylceramides appear with the establishment of the water permeability barrier in mice and are produced by maturating keratinocytes.

Lipids

2022 Volume 57, Issue 3, Page(s) 183–195

Abstract: 1-O-Acylceramides (1-OACs) have a fatty acid esterified to the 1-hydroxyl of the sphingosine head group of the ceramide, and recently we identified these lipids as natural components of human and mouse epidermis. Here we show epidermal 1-OACs arise ... ...

Abstract	1-O-Acylceramides (1-OACs) have a fatty acid esterified to the 1-hydroxyl of the sphingosine head group of the ceramide, and recently we identified these lipids as natural components of human and mouse epidermis. Here we show epidermal 1-OACs arise shortly before birth during the establishment of the water permeability barrier in mice. Fractionation of human epidermis indicates 1-OACs concentrate in the stratum corneum. During in vitro maturation into reconstructed human epidermis, human keratinocytes dramatically increase 1-OAC levels indicating they are one source of epidermal 1-OACs. In search of potential enzymes responsible for 1-OAC synthesis in vivo, we analyzed mutant mice with deficiencies of ceramide synthases (Cers2, Cers3, or Cers4), diacylglycerol acyltransferases (Dgat1 or Dgat2), elongase of very long fatty acids 3 (Elovl3), lecithin cholesterol acyltransferase (Lcat), stearoyl-CoA desaturase 1 (Scd1), or acidic ceramidase (Asah1). Overall levels of 1-OACs did not decrease in any mouse model. In Cers3 and Dgat2-deficient epidermis they even increased in correlation with deficient skin barrier function. Dagt2 deficiency reshapes 1-OAC synthesis with an increase in 1-OACs with N-linked non-hydroxylated fatty acids and a 60% decrease compared to control in levels of 1-OACs with N-linked hydroxylated palmitate. As none of the single enzyme deficiencies we examined resulted in a lack of 1-OACs, we conclude that either there is functional redundancy in forming 1-OAC and more than one enzyme is involved, and/or an unknown acyltransferase of the epidermis performs the final step of 1-OAC synthesis, the implications of which are discussed.
MeSH term(s)	Animals ; Ceramides ; Epidermis ; Fatty Acids ; Keratinocytes ; Mice ; Permeability ; Sphingosine N-Acyltransferase ; Water
Chemical Substances	Ceramides ; Fatty Acids ; Water (059QF0KO0R) ; CERS4 protein, mouse (EC 2.3.1.24) ; Sphingosine N-Acyltransferase (EC 2.3.1.24)
Language	English
Publishing date	2022-03-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	241539-2
ISSN	1558-9307 ; 0024-4201
ISSN (online)	1558-9307
ISSN	0024-4201
DOI	10.1002/lipd.12342
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Article ; Online: Expression of connexin genes in the human retina.

Söhl, Goran / Joussen, Antonia / Kociok, Norbert / Willecke, Klaus

BMC ophthalmology

2010 Volume 10, Page(s) 27

Abstract: Background: Gap junction channels allow direct metabolically and electrical coupling between adjacent cells in various mammalian tissues. Each channel is composed of 12 protein subunits, termed connexins (Cx). In the mouse retina, Cx43 could be ... ...

Abstract	Background: Gap junction channels allow direct metabolically and electrical coupling between adjacent cells in various mammalian tissues. Each channel is composed of 12 protein subunits, termed connexins (Cx). In the mouse retina, Cx43 could be localized mostly between astroglial cells whereas expression of Cx36, Cx45 and Cx57 genes has been detected in different neuronal subtypes. In the human retina, however, the expression pattern of connexin genes is largely unknown. Methods: Northern blot hybridizations, RT-PCR as well as immunofluorescence analyses helped to explore at least partially the expression pattern of the following human connexin genes GJD2 (hCx36), GJC1 (hCx45), GJA9 (hCx59) and GJA10 (hCx62) in the human retina. Results: Here we report that Northern blot hybridization signals of the orthologuous hCx36 and hCx45 were found in human retinal RNA. Immunofluorescence signals for both connexins could be located in both inner and outer plexiform layer (IPL, OPL). Expression of a third connexin gene denoted as GJA10 (Cx62) was also detected after Northern blot hybridization in the human retina. Interestingly, its gene structure is similar to that of Gja10 (mCx57) being expressed in mouse horizontal cells. RT-PCR analysis suggested that an additional exon of about 25 kb further downstream, coding for 12 amino acid residues, is spliced to the nearly complete reading frame on exon2 of GJA10 (Cx62). Cx59 mRNA, however, with high sequence identity to zebrafish Cx55.5 was only weakly detectable by RT-PCR in cDNA of human retina. Conclusion: In contrast to the neuron-expressed connexin genes Gjd2 coding for mCx36, Gjc1 coding for mCx45 and Gja10 coding for mCx57 in the mouse, a subset of 4 connexin genes, including the unique GJA9 (Cx59) and GJA10 (Cx62), could be detected at least as transcript isoforms in the human retina. First immunofluorescence analyses revealed a staining pattern of hCx36 and hCx45 expression both in the IPL and OPL, partially reminiscent to that in the mouse, although additional post-mortem material is needed to further explore their sublamina-specific distribution. Appropriate antibodies against Cx59 and Cx62 protein will clarify expression of these proteins in future studies.
MeSH term(s)	Animals ; Blotting, Northern ; Connexins/biosynthesis ; Connexins/genetics ; DNA/genetics ; Gene Expression Regulation ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; RNA, Messenger/genetics ; Retina/cytology ; Retina/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Gap Junction delta-2 Protein
Chemical Substances	Connexins ; Gja10 protein, mouse ; RNA, Messenger ; connexin 45 ; DNA (9007-49-2)
Language	English
Publishing date	2010-10-27
Publishing country	England
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2050436-6
ISSN	1471-2415 ; 1471-2415
ISSN (online)	1471-2415
ISSN	1471-2415
DOI	10.1186/1471-2415-10-27
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Article ; Online: Disease-linked connexin26 S17F promotes volar skin abnormalities and mild wound healing defects in mice.

Press, Eric / Alaga, Katanya C / Barr, Kevin / Shao, Qing / Bosen, Felicitas / Willecke, Klaus / Laird, Dale W

Cell death & disease

2017 Volume 8, Issue 6, Page(s) e2845

Abstract: Several mutant mice have been generated to model connexin (Cx)-linked skin diseases; however, the role of connexins in skin maintenance and during wound healing remains to be fully elucidated. Here we generated a novel, viable, and fertile mouse ( ... ...

Abstract	Several mutant mice have been generated to model connexin (Cx)-linked skin diseases; however, the role of connexins in skin maintenance and during wound healing remains to be fully elucidated. Here we generated a novel, viable, and fertile mouse (Cx26
MeSH term(s)	Animals ; Cell Differentiation ; Connexins/genetics ; Connexins/metabolism ; Deafness/genetics ; Deafness/metabolism ; Deafness/pathology ; Disease Models, Animal ; Epidermis/metabolism ; Epidermis/pathology ; Female ; Founder Effect ; Gap Junctions/metabolism ; Gap Junctions/pathology ; Gene Expression ; Humans ; Ichthyosis/genetics ; Ichthyosis/metabolism ; Ichthyosis/pathology ; Intermediate Filament Proteins/genetics ; Intermediate Filament Proteins/metabolism ; Keratin-14/genetics ; Keratin-14/metabolism ; Keratinocytes/metabolism ; Keratinocytes/pathology ; Keratoderma, Palmoplantar/genetics ; Keratoderma, Palmoplantar/metabolism ; Keratoderma, Palmoplantar/pathology ; Male ; Mice ; Mice, Transgenic ; Mutation ; Primary Cell Culture ; Promoter Regions, Genetic ; Wound Healing/genetics
Chemical Substances	Connexins ; GJB2 protein, human ; Intermediate Filament Proteins ; Keratin-14 ; filaggrin
Language	English
Publishing date	2017-06-01
Publishing country	England
Document type	Journal Article
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/cddis.2017.234
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