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  1. Article: Glycobiology of Head and Neck Squamous Epithelia and Carcinomas

    Plzák, Jan / Smetana Jr., Karel / Chovanec, Martin / Betka, Jan

    ORL

    2005  Volume 67, Issue 2, Page(s) 61–69

    Abstract: An impressive variety of regulatory processes including cell adhesion and migration, proliferation, apoptosis and differentiation folding and routing of glycoproteins have been found to be mediated by specific lectin-carbohydrate interactions. This ... ...

    Institution Department of Otorhinolaryngology and Head and Neck Surgery and Institute of Anatomy, 1st Faculty of Medicine, and Center of Cell Therapy and Tissue Repair, 2nd Faculty of Medicine, Charles University, Prague, Czech Republic
    Abstract An impressive variety of regulatory processes including cell adhesion and migration, proliferation, apoptosis and differentiation folding and routing of glycoproteins have been found to be mediated by specific lectin-carbohydrate interactions. This article summarizes the data on glycobiological aspects of differentiation of squamous epithelia in the head and neck region under physiological conditions and in cancer. The possible function of lectins in tumor development and invasiveness is debated. Introduction of labeled endogenous lectins as a tool for the study of functional glycomics at the cellular level in head and neck squamous epithelia and carcinomas enables a complex interpretation of studied data because these lectins are normally occurring in these tissues. The lectinology of Langerhans cells in head and neck squamous epithelia and carcinoma is also mentioned. Finally, the use of the described data in the diagnosis and prospectively in the treatment of head and neck squamous cell carcinoma is shown.
    Keywords Squamous epithelium ; Head and neck squamous cell carcinoma ; Lectin-carbohydrate interactions
    Language English
    Publishing date 2005-05-20
    Publisher S. Karger AG
    Publishing place Basel, Switzerland
    Document type Article
    Note Review
    ZDB-ID 121482-2
    ISSN 1423-0275 ; 0301-1569
    ISSN (online) 1423-0275
    ISSN 0301-1569
    DOI 10.1159/000084994
    Database Karger publisher's database

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  2. Article: Human Galectins Induce Conversion of Dermal Fibroblasts into Myofibroblasts and Production of Extracellular Matrix: Potential Application in Tissue Engineering and Wound Repair

    Dvořánková, Barbora / Szabo, Pavol / Lacina, Lukas / Gal, Peter / Uhrova, Jana / Zima, Tomas / Kaltner, Herbert / André, Sabine / Gabius, Hans-Joachim / Sykova, Eva / Smetana, Jr., Karel

    Cells Tissues Organs

    2011  Volume 194, Issue 6, Page(s) 469–480

    Abstract: Members of the galectin family of endogenous lectins are potent adhesion/growth-regulatory effectors. Their multifunctionality opens possibilities for their use in bioapplications. We studied whether human galectins induce the conversion of human dermal ... ...

    Institution Institute of Anatomy Department of Dermatovenerology Institute of Clinical Biochemistry and Laboratory Diagnostics, 1st Faculty of Medicine Center of Cell Therapy and Tissue Repair, 2nd Faculty of Medicine, Charles University, and Institute of Experimental Medicine, Academy of Sciences of the Czech Republic, Prague, Czech Republic Department for Biomedical Research, East-Slovak Institute of Cardiovascular Diseases Department of Pathological Anatomy, University of Veterinary Medicine and Pharmacy, Košice, Slovak Republic Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Munich, Germany
    Abstract Members of the galectin family of endogenous lectins are potent adhesion/growth-regulatory effectors. Their multifunctionality opens possibilities for their use in bioapplications. We studied whether human galectins induce the conversion of human dermal fibroblasts into myofibroblasts (MFBs) and the production of a bioactive extracellular matrix scaffold is suitable for cell culture. Testing a panel of galectins of all three subgroups, including natural and engineered variants, we detected activity for the proto-type galectin-1 and galectin-7, the chimera-type galectin-3 and the tandem-repeat-type galectin-4. The activity of galectin-1 required the integrity of the carbohydrate recognition domain. It was independent of the presence of TGF-β1, but it yielded an additive effect. The resulting MFBs, relevant, for example, for tumor progression, generated a matrix scaffold rich in fibronectin and galectin-1 that supported keratinocyte culture without feeder cells. Of note, keratinocytes cultured on this substratum presented a stem-like cell phenotype with small size and keratin-19 expression. In vivo in rats, galectin-1 had a positive effect on skin wound closure 21 days after surgery. In conclusion, we describe the differential potential of certain human galectins to induce the conversion of dermal fibroblasts into MFBs and the generation of a bioactive cell culture substratum.
    Keywords Extracellular matrix ; Fibronectin ; Keratinocyte ; Lectin ; Tissue engineering
    Language English
    Publishing date 2011-04-14
    Publisher S. Karger AG
    Publishing place Basel, Switzerland
    Document type Article
    Note Original Paper
    ZDB-ID 1468141-9
    ISSN 1422-6421 ; 1422-6405
    ISSN (online) 1422-6421
    ISSN 1422-6405
    DOI 10.1159/000324864
    Database Karger publisher's database

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  3. Article ; Online: Differentiation-Dependent Glycosylation of Cells in Squamous Cell Epithelia Detected by a Mammalian Lectin

    Plzák, Jan / Holíková, Zuzana / Smetana, Jr., Karel / Dvořánková, Barbora / Hercogová, Jana / Kaltner, Herbert / Motlík, Jan / Gabius, Hans-Joachim

    Cells Tissues Organs - in vivo, in vitro

    2002  Volume 171, Issue 2-3, Page(s) 135–144

    Abstract: The squamous stratified epithelia contain a proliferative (harboring mitotic activity) and a differentiating compartment. Due to the potential of protein-carbohydrate interactions to regulate cellular activities we introduced a mammalian lectin to cyto- ... ...

    Abstract The squamous stratified epithelia contain a proliferative (harboring mitotic activity) and a differentiating compartment. Due to the potential of protein-carbohydrate interactions to regulate cellular activities we introduced a mammalian lectin to cyto- and histochemical analysis. We answer the questions of whether and to what extent this new probe can pinpoint differentiation-dependent glycosylation changes in sections and in culture of keratinocytes. Material and Methods: Purification and labeling enabled monitoring of galectin-3 reactivity in frozen sections of human and pig epidermis and basal cell carcinomas as well as in culture of keratinocytes. The staining pattern of the lectin was correlated with the staining profile of other cell markers including desmosomal proteins, β1 integrin, and the proliferation marker Ki-67. The Dolichos biflorus agglutinin (DBA) sharing binding reactivity of galectin-3 to the A type histoblood group epitope was used for comparison. Results: Both lectins exhibit suprabasal binding. However, their profiles were not identical, substantiated by lack of coinhibition. Strong DBA reactivity was also observed in a limited number of basal layer cells, namely in cells without the expression of the proliferation marker Ki-67. Cultured mitotic epidermal cells have no reactivity for DBA. Presence of ligands for this plant lectin was connected with decreased positivity of nuclei for Ki-67 and the occurrence of ring-shaped nucleoli, micronucleoli or absence of nucleoli. Considering colocalization the pattern of galectin-3-binding sites coincided with the presence of desmosomal proteins such as desmoplakin-1 and desmoglein but not β1 integrin, a potential ligand. Interestingly, studied basal cell carcinomas expressed no binding sites for galectin-3, while a limited number of cells were DBA-reactive. Conclusion: The expression of galectin-3-binding sites and also DBA-reactive glycoligands correlates with an increased level of differentiation and/or cessation of proliferation in the examined squamous stratified epithelia. Further application of tissue lectins for characterizing ligand expression and its modulation is an important step to reveal functional relevance.
    Keywords Carcinoma, basal cell ; Cell differentiation ; Galectin-3 ; Lectin ; Squamous epithelia
    Language English
    Publisher S. Karger AG
    Publishing place Basel
    Publishing country Switzerland
    Document type Article ; Online
    ZDB-ID 1468141-9
    ISSN 1422-6421 ; 1422-6405 ; 1422-6405
    ISSN (online) 1422-6421
    ISSN 1422-6405
    DOI 10.1159/000063707
    Database Karger publisher's database

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  4. Article: Differentiation-Dependent Glycosylation of Cells in Squamous Cell Epithelia Detected by a Mammalian Lectin

    Plzák, Jan / Holíková, Zuzana / Smetana Jr., Karel / Dvořánková, Barbora / Hercogová, Jana / Kaltner, Herbert / Motlík, Jan / Gabius, Hans-Joachim

    Cells Tissues Organs

    2002  Volume 171, Issue 2-3, Page(s) 135–144

    Abstract: The squamous stratified epithelia contain a proliferative (harboring mitotic activity) and a differentiating compartment. Due to the potential of protein-carbohydrate interactions to regulate cellular activities we introduced a mammalian lectin to cyto- ... ...

    Institution Institute of Anatomy, 1st Faculty of Medicine Department of Otorhinolaryngology and Head and Neck Surgery, 1st Faculty of Medicine Center for Cell Therapy and Tissue Repair, 2nd Faculty of Medicine Department of Dermatology, 2nd Faculty of Medicine, and Department of Burn Surgery, 3rd Faculty of Medicine, Charles University, Prague, and Institute of Animal Physiology and Genetics, Academy of Sciences of the Czech Republic, Liběchov, Czech Republic Faculty of Veterinary Medicine, Institute of Physiological Chemistry, Ludwig Maximilians University, Munich, Germany
    Abstract The squamous stratified epithelia contain a proliferative (harboring mitotic activity) and a differentiating compartment. Due to the potential of protein-carbohydrate interactions to regulate cellular activities we introduced a mammalian lectin to cyto- and histochemical analysis. We answer the questions of whether and to what extent this new probe can pinpoint differentiation-dependent glycosylation changes in sections and in culture of keratinocytes. Material and Methods: Purification and labeling enabled monitoring of galectin-3 reactivity in frozen sections of human and pig epidermis and basal cell carcinomas as well as in culture of keratinocytes. The staining pattern of the lectin was correlated with the staining profile of other cell markers including desmosomal proteins, β1 integrin, and the proliferation marker Ki-67. The Dolichos biflorus agglutinin (DBA) sharing binding reactivity of galectin-3 to the A type histoblood group epitope was used for comparison. Results: Both lectins exhibit suprabasal binding. However, their profiles were not identical, substantiated by lack of coinhibition. Strong DBA reactivity was also observed in a limited number of basal layer cells, namely in cells without the expression of the proliferation marker Ki-67. Cultured mitotic epidermal cells have no reactivity for DBA. Presence of ligands for this plant lectin was connected with decreased positivity of nuclei for Ki-67 and the occurrence of ring-shaped nucleoli, micronucleoli or absence of nucleoli. Considering colocalization the pattern of galectin-3-binding sites coincided with the presence of desmosomal proteins such as desmoplakin-1 and desmoglein but not β1 integrin, a potential ligand. Interestingly, studied basal cell carcinomas expressed no binding sites for galectin-3, while a limited number of cells were DBA-reactive. Conclusion: The expression of galectin-3-binding sites and also DBA-reactive glycoligands correlates with an increased level of differentiation and/or cessation of proliferation in the examined squamous stratified epithelia. Further application of tissue lectins for characterizing ligand expression and its modulation is an important step to reveal functional relevance.
    Keywords Cell differentiation ; Squamous epithelia ; Galectin-3 ; Lectin ; Carcinoma, basal cell
    Language English
    Publishing date 2002-06-28
    Publisher S. Karger AG
    Publishing place Basel, Switzerland
    Document type Article
    Note Original Paper
    ZDB-ID 1468141-9
    ISSN 1422-6421 ; 1422-6405
    ISSN (online) 1422-6421
    ISSN 1422-6405
    DOI 10.1159/000063707
    Database Karger publisher's database

    Full text online

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    In stock of ZB MED Cologne/Königswinter

    Ub I Zs.150: Show issues Location:
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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
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