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Article ; Online: Prof. Hans-Joachim Gabius (1955-2021) A Tribute to an Outstanding Glycobiologist, Mentor and Friend.

Kaltner, Herbert / Mayo, Kevin H

2022 Volume 32, Issue 1, Page(s) 2–5

MeSH term(s)	Glycomics ; History, 20th Century ; Humans ; Mentors
Language	English
Publishing date	2022-02-03
Publishing country	England
Document type	Biography ; Historical Article ; Letter
ZDB-ID	1067689-2
ISSN	1460-2423 ; 0959-6658
ISSN (online)	1460-2423
ISSN	0959-6658
DOI	10.1093/glycob/cwab099
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Article ; Online: The sweet side of wound healing: galectins as promising therapeutic targets in hemostasis, inflammation, proliferation, and maturation/remodeling.

Čoma, Matúš / Manning, Joachim C / Kaltner, Herbert / Gál, Peter

Expert opinion on therapeutic targets

2023 Volume 27, Issue 1, Page(s) 41–53

Abstract: Introduction: Understanding the molecular and cellular processes involved in skin wound healing may pave the way for the development of innovative approaches to transforming the identified natural effectors into therapeutic tools. Based on the extensive ...

Abstract	Introduction: Understanding the molecular and cellular processes involved in skin wound healing may pave the way for the development of innovative approaches to transforming the identified natural effectors into therapeutic tools. Based on the extensive involvement of the ga(lactoside-binding)lectin family in (patho)physiological processes, it has been well established that galectins are involved in a wide range of cell-cell and cell-matrix interactions. Areas covered: In the present paper, we provide an overview of the biological role of galectins in repair and regeneration, focusing on four main phases (hemostasis, inflammation, proliferation, and maturation/remodeling) of skin repair using basic wound models (open excision vs. sutured incision). Expert opinion: The reported data make a strong case for directing further efforts to treat excisional and incisional wounds differently. Functions of galectins essentially result from their modular presentation. In fact, Gal-1 seems to play a role in the early phases of healing (anti-inflammatory) and wound contraction, Gal-3 accelerates re-epithelization and increases tensile strength (scar inductor). Galectins have also become subject of redesigning by engineering to optimize the activity. Clinically relevant, these new tools derived from the carbohydrate recognition domain platform may also prove helpful for other purposes, such as potent antibacterial agglutinins and opsonins.
MeSH term(s)	Humans ; Wound Healing ; Galectins ; Hemostasis ; Cell Proliferation ; Inflammation
Chemical Substances	Galectins
Language	English
Publishing date	2023-02-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2055208-7
ISSN	1744-7631 ; 1472-8222
ISSN (online)	1744-7631
ISSN	1472-8222
DOI	10.1080/14728222.2023.2175318
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Article ; Online: Examining Galectin Gene Regulation by Reporter Assays.

Schmidt, Sebastian / Kaltner, Herbert / Gabius, Hans-Joachim

Methods in molecular biology (Clifton, N.J.)

2022 Volume 2442, Page(s) 445–462

Abstract: Matching their role as potent and versatile effectors in cellular homeostasis and disease processes, galectins are subject to a fine-tuned transcriptional regulation of gene expression. It can apparently even involve coregulation with certain elements of ...

Abstract	Matching their role as potent and versatile effectors in cellular homeostasis and disease processes, galectins are subject to a fine-tuned transcriptional regulation of gene expression. It can apparently even involve coregulation with certain elements of the enzymatic machinery for glycan biosynthesis/remodeling and/or functional carriers of galectin-binding glycans such as the α
MeSH term(s)	Galectins/genetics ; Gene Expression Regulation ; Luciferases/genetics ; Promoter Regions, Genetic
Chemical Substances	Galectins ; Luciferases (EC 1.13.12.-)
Language	English
Publishing date	2022-03-23
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-2055-7_24
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Article ; Online: Sensing Glycans as Biochemical Messages by Tissue Lectins: The Sugar Code at Work in Vascular Biology.

Kaltner, Herbert / Gabius, Hans-Joachim

Thrombosis and haemostasis

2019 Volume 119, Issue 4, Page(s) 517–533

Abstract: Although a plethora of players has already been revealed to be engaged in the haemostatic system, a fundamental consideration of the molecular nature of information coding can give further explorations of the mechanisms of blood clotting, platelet ... ...

Abstract	Although a plethora of players has already been revealed to be engaged in the haemostatic system, a fundamental consideration of the molecular nature of information coding can give further explorations of the mechanisms of blood clotting, platelet functionality and vascular trafficking direction. By any measures, looking at ranges of occurrence and of potential for structural versatility, at strategic positioning to influence protein and cell sociology as well as at dynamics of processing and restructuring for phenotypic variability, using sugars as an alphabet of life for generating the glycan part of glycoconjugates is a success story. The handiwork by the complex system for glycan biosynthesis renders biochemical messages of exceptionally high coding capacity available. They are read and translated into cellular effects by receptors termed lectins. The different levels of regulation on both sides, that is, glycan and lectin, establish an intriguingly fine-tuned capacity for functional pairing. The emerging insights into the highly branched routes of glycosylation, into lectin structures up to complete characterization in solution and the shape of lectin networks, first obtained for the three selectins, now extended to considering many other C-type lectins, galectins and siglecs, as well as into intra- and inter-family cross-talk and cooperations are sure to push boundaries in our understanding of the molecular basis of haemostasis.
MeSH term(s)	Alternative Splicing ; Animals ; Blood Vessels/physiology ; Carbohydrates/chemistry ; Cardiovascular System ; Cell Membrane/chemistry ; Epitopes/chemistry ; Galectins/chemistry ; Glycosylation ; Hemostasis ; Humans ; Inflammation ; Lectins/chemistry ; Molecular Conformation ; Phenotype ; Polysaccharides/chemistry ; Sialic Acid Binding Immunoglobulin-like Lectins/chemistry ; Signal Transduction
Chemical Substances	Carbohydrates ; Epitopes ; Galectins ; Lectins ; Polysaccharides ; Sialic Acid Binding Immunoglobulin-like Lectins
Language	English
Publishing date	2019-01-08
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	518294-3
ISSN	2567-689X ; 0340-6245
ISSN (online)	2567-689X
ISSN	0340-6245
DOI	10.1055/s-0038-1676968
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Book ; Thesis: Die Entwicklung des Embryos der Japanischen Wachtel unter In-vitro-Bedingungen

Kaltner, Herbert

1989

Keywords	Japanische Wachtel ; Embryonalentwicklung ; In vitro
Subject	In-vitro-Methode ; Embryo ; Embryogenese ; Keimesentwicklung ; Coturnix coturnix japonica ; Japanwachtel ; Coturnix quail
Size	104 S. : graph. Darst.
Document type	Book ; Thesis
Thesis / German Habilitation thesis	München, Univ., Diss., 1989
HBZ-ID	HT003635014
Database	Catalogue ZB MED Nutrition, Environment, Agriculture

In stock of ZB MED Bonn / Germany

Shelf mark	Loan status	Location
AY 14197	order for loan	Geschlossenes Magazin (U2)

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Article ; Online: Combining Recombinase-Mediated Cassette Exchange Strategy with Quantitative Proteomic and Phosphoproteomic Analyses to Inspect Intracellular Functions of the Tumor Suppressor Galectin-4 in Colorectal Cancer Cells.

Michalak, Malwina / Golde, Viola / Helm, Dominik / Kaltner, Herbert / Gebert, Johannes / Kopitz, Jürgen

International journal of molecular sciences

2022 Volume 23, Issue 12

Abstract: Galectin-4 (Gal4) has been suggested to function as a tumor suppressor in colorectal cancer (CRC). In order to systematically explore its function in CRC, we established a CRC cell line where Gal4 expression can be regulated via the doxycycline (dox)- ... ...

Abstract	Galectin-4 (Gal4) has been suggested to function as a tumor suppressor in colorectal cancer (CRC). In order to systematically explore its function in CRC, we established a CRC cell line where Gal4 expression can be regulated via the doxycycline (dox)-inducible expression of a single copy wildtype
MeSH term(s)	Cell Line, Tumor ; Colorectal Neoplasms/pathology ; DNA-Binding Proteins ; Forkhead Transcription Factors ; Galectin 4 ; Humans ; Intracellular Space/metabolism ; Proteomics/methods ; Recombinases ; Transcription Factors
Chemical Substances	DNA-Binding Proteins ; FOXK1 protein, human ; Forkhead Transcription Factors ; Galectin 4 ; Recombinases ; Transcription Factors ; ZBTB7A protein, human
Language	English
Publishing date	2022-06-08
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms23126414
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Article ; Online: Altering the Modular Architecture of Galectins Affects its Binding with Synthetic α-Dystroglycan O-Mannosylated Core M1 Glycoconjugates In situ.

Villones, Lareno L / Ludwig, Anna-Kristin / Kikuchi, Seiya / Ochi, Rika / Nishimura, Shin-Ichiro / Gabius, Hans-Joachim / Kaltner, Herbert / Hinou, Hiroshi

Chembiochem : a European journal of chemical biology

2023 Volume 24, Issue 14, Page(s) e202200783

Abstract: The multifunctionality of galectins helps regulate a broad range of fundamental cellular processes via cis-binding and trans-bridging activities and has gained widespread attention with respect to the importance of the natural specificity/selectivity of ... ...

Abstract	The multifunctionality of galectins helps regulate a broad range of fundamental cellular processes via cis-binding and trans-bridging activities and has gained widespread attention with respect to the importance of the natural specificity/selectivity of this lectin family to its glycoconjugate receptors. Combining galectin (Gal)-1, -3, -4, and -9 variant test panels, achieved via rational protein engineering, and a synthetic α-dystroglycan (DG) O-Mannosylated core M1 glycopeptide library, a detailed comparative analysis was performed, utilizing microarray experiments to delineate the design-functionality relationships within this lectin family. Enhancement of prototype Gal-1 and chimera-type Gal-3 cis-binding toward the prepared ligands is possible by transforming these lectins into tandem-repeat type and prototypes, respectively. Furthermore, Gal-1 variants demonstrated improved trans-bridging capabilities between core M1 α-DG glycopeptides and laminins in microarray, suggesting the possible translational applications of these galectin variants in the treatment of some forms of α-dystroglycanopathy.
MeSH term(s)	Dystroglycans ; Galectins/metabolism ; Glycoconjugates/metabolism ; Glycopeptides
Chemical Substances	Dystroglycans (146888-27-9) ; 1-nitrohydroxyphenyl-N-benzoylalanine (59921-69-6) ; Galectins ; Glycoconjugates ; Glycopeptides
Language	English
Publishing date	2023-05-16
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2020469-3
ISSN	1439-7633 ; 1439-4227
ISSN (online)	1439-7633
ISSN	1439-4227
DOI	10.1002/cbic.202200783
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Article: Sensing Glycans as Biochemical Messages by Tissue Lectins: The Sugar Code at Work in Vascular Biology

Kaltner, Herbert / Gabius, Hans-Joachim

Thrombosis and Haemostasis

2019 Volume 119, Issue 04, Page(s) 517–533

Abstract	Although a plethora of players has already been revealed to be engaged in the haemostatic system, a fundamental consideration of the molecular nature of information coding can give further explorations of the mechanisms of blood clotting, platelet functionality and vascular trafficking direction. By any measures, looking at ranges of occurrence and of potential for structural versatility, at strategic positioning to influence protein and cell sociology as well as at dynamics of processing and restructuring for phenotypic variability, using sugars as an alphabet of life for generating the glycan part of glycoconjugates is a success story. The handiwork by the complex system for glycan biosynthesis renders biochemical messages of exceptionally high coding capacity available. They are read and translated into cellular effects by receptors termed lectins. The different levels of regulation on both sides, that is, glycan and lectin, establish an intriguingly fine-tuned capacity for functional pairing. The emerging insights into the highly branched routes of glycosylation, into lectin structures up to complete characterization in solution and the shape of lectin networks, first obtained for the three selectins, now extended to considering many other C-type lectins, galectins and siglecs, as well as into intra- and inter-family cross-talk and cooperations are sure to push boundaries in our understanding of the molecular basis of haemostasis.
Keywords	C-type lectin ; galectin ; mucin ; selectin ; siglec ; von Willebrand factor
Language	English
Publishing date	2019-01-08
Publisher	Georg Thieme Verlag KG
Publishing place	Stuttgart ; New York
Document type	Article
ZDB-ID	518294-3
ISSN	2567-689X ; 0340-6245
ISSN (online)	2567-689X
ISSN	0340-6245
DOI	10.1055/s-0038-1676968
Database	Thieme publisher's database

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Uh III Zs.192: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Lectinology 4.0: Altering modular (ga)lectin display for functional analysis and biomedical applications.

Ludwig, Anna-Kristin / Kaltner, Herbert / Kopitz, Jürgen / Gabius, Hans-Joachim

Biochimica et biophysica acta. General subjects

2019 Volume 1863, Issue 5, Page(s) 935–940

Abstract: Background: Recognition of glycans by lectins is emerging as (patho)physiologically broadly used mode of cellular information transfer. Whereas the direct ligand-receptor contact is often already thoroughly characterized, the functional relevance of ... ...

Abstract	Background: Recognition of glycans by lectins is emerging as (patho)physiologically broadly used mode of cellular information transfer. Whereas the direct ligand-receptor contact is often already thoroughly characterized, the functional relevance of aspects of architecture such as modular design and valence of lectins is less well defined. Scope of review: Following an introduction to modular lectin design, three levels of methodology are then reviewed that delineate lectin structure-activity relationships beyond glycan binding, with emphasis on domain shuffling. Major conclusions: Engineering of variants by modular transplantation facilitates versatile Nature-inspired design switches and access to new combinations with translational potential, as exemplified for human adhesion/growth-regulatory galectins. General significance: To gain an understanding of the functional significance of natural variations in quaternary structure and modular design within a protein family is a current challenge. Strategic application of methods of the described phases is a means to respond to this challenge.
MeSH term(s)	Biomedical Research ; Galectins/chemistry ; Galectins/metabolism ; Humans ; Polysaccharides/chemistry ; Polysaccharides/metabolism ; Protein Engineering ; Structure-Activity Relationship
Chemical Substances	Galectins ; Polysaccharides
Language	English
Publishing date	2019-03-06
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	60-7
ISSN	1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagen.2019.03.005
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Article ; Online: Galectin-9 as a Potential Modulator of Lymphocyte Adhesion to Endothelium via Binding to Blood Group H Glycan.

Rapoport, Eugenia M / Ryzhov, Ivan M / Slivka, Ekaterina V / Korchagina, Elena Yu / Popova, Inna S / Khaidukov, Sergey V / André, Sabine / Kaltner, Herbert / Gabius, Hans-J / Henry, Stephen / Bovin, Nicolai V

Biomolecules

2023 Volume 13, Issue 8

Abstract: The recruitment of leukocytes from blood is one of the most important cellular processes in response to tissue damage and inflammation. This multi-step process includes rolling leukocytes and their adhesion to endothelial cells (EC), culminating in ... ...

Abstract	The recruitment of leukocytes from blood is one of the most important cellular processes in response to tissue damage and inflammation. This multi-step process includes rolling leukocytes and their adhesion to endothelial cells (EC), culminating in crossing the EC barrier to reach the inflamed tissue. Galectin-8 and galectin-9 expressed on the immune system cells are part of this process and can induce cell adhesion via binding to oligolactosamine glycans. Similarly, these galectins have an order of magnitude higher affinity towards glycans of the ABH blood group system, widely represented on ECs. However, the roles of gal-8 and gal-9 as mediators of adhesion to endothelial ABH antigens are practically unknown. In this work, we investigated whether H antigen-gal-9-mediated adhesion occurred between Jurkat cells (of lymphocytic origin and known to have gal-9) and EA.hy 926 cells (immortalized endothelial cells and known to have blood group H antigen). Baseline experiments showed that Jurkat cells adhered to EA.hy 926 cells; however when these EA.hy 926 cells were defucosylated (despite the unmasking of lactosamine chains), adherence was abolished. Restoration of fucosylation by insertion of synthetic glycolipids in the form of H (type 2) trisaccharide Fucα1-2Galβ1-4GlcNAc restored adhesion. The degree of lymphocyte adhesion to native and the "H-restored" (glycolipid-loaded) EA.hy 926 cells was comparable. If this gal-9/H (type 2) interaction is similar to processes that occur in vivo, this suggests that only the short (trisaccharide) H glycan on ECs is required.
MeSH term(s)	Humans ; Endothelial Cells ; ABO Blood-Group System ; Galectins ; Glycolipids ; Jurkat Cells ; Endothelium
Chemical Substances	ABO Blood-Group System ; Galectins ; Glycolipids
Language	English
Publishing date	2023-07-26
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom13081166
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