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  1. Article ; Online: Peptidases: Role and Function in Health and Disease.

    Kos, Janko

    International journal of molecular sciences

    2023  Volume 24, Issue 9

    Abstract: Peptidases represent a large family of hydrolases present in all living organisms, which catalyze the degradation of peptide bonds in different biological processes. ...

    Abstract Peptidases represent a large family of hydrolases present in all living organisms, which catalyze the degradation of peptide bonds in different biological processes.
    MeSH term(s) Peptide Hydrolases/metabolism
    Chemical Substances Peptide Hydrolases (EC 3.4.-)
    Language English
    Publishing date 2023-04-25
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms24097823
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  2. Article ; Online: Proteases: Role and Function in Cancer.

    Kos, Janko

    International journal of molecular sciences

    2022  Volume 23, Issue 9

    Abstract: The Special Issue "Proteases: Role and Function in Cancer" aimed to focus on basic and translational research to highlight the role of peptidases in tumor development and to assess their potential in cancer diagnosis and therapy [ ... ]. ...

    Abstract The Special Issue "Proteases: Role and Function in Cancer" aimed to focus on basic and translational research to highlight the role of peptidases in tumor development and to assess their potential in cancer diagnosis and therapy [...].
    MeSH term(s) Endopeptidases ; Humans ; Neoplasms ; Peptide Hydrolases ; Translational Research, Biomedical
    Chemical Substances Endopeptidases (EC 3.4.-) ; Peptide Hydrolases (EC 3.4.-)
    Language English
    Publishing date 2022-04-22
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms23094632
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Compensational role between cathepsins.

    Pečar Fonović, Urša / Kos, Janko / Mitrović, Ana

    Biochimie

    2024  

    Abstract: Cathepsins, a family of lysosomal peptidases, play a crucial role in maintaining cellular homeostasis by regulating protein turnover and degradation as well as many specific regulatory actions that are important for proper cell function and human health. ...

    Abstract Cathepsins, a family of lysosomal peptidases, play a crucial role in maintaining cellular homeostasis by regulating protein turnover and degradation as well as many specific regulatory actions that are important for proper cell function and human health. Alterations in the activity and expression of cathepsins have been observed in many diseases such as cancer, inflammation, neurodegenerative disorders, bone remodelling-related conditions and others. These changes are not exclusively harmful, but rather appear to be a compensatory response on the lack of one cathepsin in order to maintain tissue integrity. The upregulation of specific cathepsins in response to the inhibition or dysfunction of other cathepsins suggests a fine-tuned system of proteolytic balance and understanding the compensatory role of cathepsins may improve therapeutic potential of cathepsin's inhibitors. Selectively targeting one cathepsin or modulating their activity could offer new treatment strategies for a number of diseases. This review emphasises the need for comprehensive research into cathepsin biology in the context of disease. The identification of the specific cathepsins involved in compensatory responses, the elucidation of the underlying molecular mechanisms and the development of targeted interventions could lead to innovative therapeutic approaches.
    Language English
    Publishing date 2024-04-23
    Publishing country France
    Document type Journal Article ; Review
    ZDB-ID 120345-9
    ISSN 1638-6183 ; 0300-9084
    ISSN (online) 1638-6183
    ISSN 0300-9084
    DOI 10.1016/j.biochi.2024.04.010
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    In stock of ZB MED Cologne/Königswinter

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  4. Article: Multifunctional roles of γ-enolase in the central nervous system: more than a neuronal marker.

    Horvat, Selena / Kos, Janko / Pišlar, Anja

    Cell & bioscience

    2024  Volume 14, Issue 1, Page(s) 61

    Abstract: Enolase, a multifunctional protein with diverse isoforms, has generally been recognized for its primary roles in glycolysis and gluconeogenesis. The shift in isoform expression from α-enolase to neuron-specific γ-enolase extends beyond its enzymatic role. ...

    Abstract Enolase, a multifunctional protein with diverse isoforms, has generally been recognized for its primary roles in glycolysis and gluconeogenesis. The shift in isoform expression from α-enolase to neuron-specific γ-enolase extends beyond its enzymatic role. Enolase is essential for neuronal survival, differentiation, and the maturation of neurons and glial cells in the central nervous system. Neuron-specific γ-enolase is a critical biomarker for neurodegenerative pathologies and neurological conditions, not only indicating disease but also participating in nerve cell formation and neuroprotection and exhibiting neurotrophic-like properties. These properties are precisely regulated by cysteine peptidase cathepsin X and scaffold protein γ
    Language English
    Publishing date 2024-05-12
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2593367-X
    ISSN 2045-3701
    ISSN 2045-3701
    DOI 10.1186/s13578-024-01240-6
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  5. Article: Cysteine Cathepsins as Therapeutic Targets in Immune Regulation and Immune Disorders.

    Senjor, Emanuela / Kos, Janko / Nanut, Milica Perišić

    Biomedicines

    2023  Volume 11, Issue 2

    Abstract: Cysteine cathepsins, as the most abundant proteases found in the lysosomes, play a vital role in several processes-such as protein degradation, changes in cell signaling, cell morphology, migration and proliferation, and energy metabolism. In addition to ...

    Abstract Cysteine cathepsins, as the most abundant proteases found in the lysosomes, play a vital role in several processes-such as protein degradation, changes in cell signaling, cell morphology, migration and proliferation, and energy metabolism. In addition to their lysosomal function, they are also secreted and may remain functional in the extracellular space. Upregulation of cathepsin expression is associated with several pathological conditions including cancer, neurodegeneration, and immune-system dysregulation. In this review, we present an overview of cysteine-cathepsin involvement and possible targeting options for mitigation of aberrant function in immune disorders such as inflammation, autoimmune diseases, and immune response in cancer.
    Language English
    Publishing date 2023-02-07
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2720867-9
    ISSN 2227-9059
    ISSN 2227-9059
    DOI 10.3390/biomedicines11020476
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  6. Article ; Online: γ-Enolase enhances Trk endosomal trafficking and promotes neurite outgrowth in differentiated SH-SY5Y cells.

    Pišlar, Anja / Kos, Janko

    Cell communication and signaling : CCS

    2021  Volume 19, Issue 1, Page(s) 118

    Abstract: Background: Neurotrophins can activate multiple signalling pathways in neuronal cells through binding to their cognate receptors, leading to neurotrophic processes such as cell survival and differentiation. γ-Enolase has been shown to have a ... ...

    Abstract Background: Neurotrophins can activate multiple signalling pathways in neuronal cells through binding to their cognate receptors, leading to neurotrophic processes such as cell survival and differentiation. γ-Enolase has been shown to have a neurotrophic activity that depends on its translocation towards the plasma membrane by the scaffold protein γ1-syntrophin. The association of γ-enolase with its membrane receptor or other binding partners at the plasma membrane remains unknown.
    Methods: In the present study, we used immunoprecipitation and immunofluorescence to show that γ-enolase associates with the intracellular domain of the tropomyosin receptor kinase (Trk) family of tyrosine kinase receptors at the plasma membrane of differentiated SH-SY5Y cells.
    Results: In differentiated SH-SY5Y cells with reduced expression of γ1-syntrophin, the association of γ-enolase with the Trk receptor was diminished due to impaired translocation of γ-enolase towards the plasma membrane or impaired Trk activity. Treatment of differentiated SH-SY5Y cells with a γ-Eno peptide that mimics γ-enolase neurotrophic activity promoted Trk receptor internalisation and endosomal trafficking, as defined by reduced levels of Trk in clathrin-coated vesicles and increased levels in late endosomes. In this way, γ-enolase triggers Rap1 activation, which is required for neurotrophic activity of γ-enolase. Additionally, the inhibition of Trk kinase activity by K252a revealed that increased SH-SY5Y cell survival and neurite outgrowth mediated by the γ-Eno peptide through activation of signalling cascade depends on Trk kinase activity.
    Conclusions: These data therefore establish the Trk receptor as a binding partner of γ-enolase, whereby Trk endosomal trafficking is promoted by γ-Eno peptide to mediate its neurotrophic signalling. Video abstract.
    MeSH term(s) Cell Differentiation ; Cell Line, Tumor ; Humans ; Neurites/physiology ; Phosphopyruvate Hydratase/metabolism ; Receptor, trkA/metabolism
    Chemical Substances Receptor, trkA (EC 2.7.10.1) ; Phosphopyruvate Hydratase (EC 4.2.1.11)
    Language English
    Publishing date 2021-12-11
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2126315-2
    ISSN 1478-811X ; 1478-811X
    ISSN (online) 1478-811X
    ISSN 1478-811X
    DOI 10.1186/s12964-021-00784-1
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  7. Article ; Online: Lysosomal peptidases-intriguing roles in cancer progression and neurodegeneration.

    Kos, Janko / Mitrović, Ana / Perišić Nanut, Milica / Pišlar, Anja

    FEBS open bio

    2022  Volume 12, Issue 4, Page(s) 708–738

    Abstract: Lysosomal peptidases are hydrolytic enzymes capable of digesting waste proteins that are targeted to lysosomes via endocytosis and autophagy. Besides intracellular protein catabolism, they play more specific roles in several other cellular processes and ... ...

    Abstract Lysosomal peptidases are hydrolytic enzymes capable of digesting waste proteins that are targeted to lysosomes via endocytosis and autophagy. Besides intracellular protein catabolism, they play more specific roles in several other cellular processes and pathologies, either within lysosomes, upon secretion into the cell cytoplasm or extracellular space, or bound to the plasma membrane. In cancer, lysosomal peptidases are generally associated with disease progression, as they participate in crucial processes leading to changes in cell morphology, signaling, migration, and invasion, and finally metastasis. However, they can also enhance the mechanisms resulting in cancer regression, such as apoptosis of tumor cells or antitumor immune responses. Lysosomal peptidases have also been identified as hallmarks of aging and neurodegeneration, playing roles in oxidative stress, mitochondrial dysfunction, abnormal intercellular communication, dysregulated trafficking, and the deposition of protein aggregates in neuronal cells. Furthermore, deficiencies in lysosomal peptidases may result in other pathological states, such as lysosomal storage disease. The aim of this review was to highlight the role of lysosomal peptidases in particular pathological processes of cancer and neurodegeneration and to address the potential of lysosomal peptidases in diagnosing and treating patients.
    MeSH term(s) Apoptosis/physiology ; Humans ; Lysosomes/metabolism ; Neoplasms ; Neoplastic Processes ; Peptide Hydrolases/metabolism
    Chemical Substances Peptide Hydrolases (EC 3.4.-)
    Language English
    Publishing date 2022-02-03
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2651702-4
    ISSN 2211-5463 ; 2211-5463
    ISSN (online) 2211-5463
    ISSN 2211-5463
    DOI 10.1002/2211-5463.13372
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  8. Article ; Online: Cell models for Alzheimer's and Parkinson's disease: At the interface of biology and drug discovery.

    Cetin, Sandra / Knez, Damijan / Gobec, Stanislav / Kos, Janko / Pišlar, Anja

    Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie

    2022  Volume 149, Page(s) 112924

    Abstract: Neurodegenerative diseases are severely debilitating conditions characterized primarily by progressive neuronal loss and impairment of the nervous system. Alzheimer's and Parkinson's diseases are the most common neurodegenerative disorders, and their ... ...

    Abstract Neurodegenerative diseases are severely debilitating conditions characterized primarily by progressive neuronal loss and impairment of the nervous system. Alzheimer's and Parkinson's diseases are the most common neurodegenerative disorders, and their impact is increasing as average life expectancy increases worldwide. Although the underlying mechanisms of both progressive diseases have been extensively studied, we still lack a comprehensive understanding of the molecular basis of both diseases. Current therapeutic options do not slow the progression of the diseases and only provide symptom relief. Cell models that resemble the characteristics of the disease in question are important in drug discovery projects because they provide information about the therapeutic benefits of drugs under development. Here, we review current in vitro cell models used to study the molecular basis of Alzheimer's and Parkinson's disease focusing on their potential for discovering of disease-modifying therapeutics to combat neurodegenerative diseases. We discuss phenotypic screening as an important approach for identifying novel therapeutic molecules. Advances in the development of cell-based assays for drug discovery are discussed, ranging from simple monoculture cell models to high-throughput three-dimensional cell models. Finally, we critically present the limitations of cell models and the caveats encountered in drug discovery to find effective treatment for neurodegenerative diseases.
    MeSH term(s) Alzheimer Disease/drug therapy ; Biology ; Drug Discovery ; Humans ; Neurodegenerative Diseases/drug therapy ; Parkinson Disease/drug therapy
    Language English
    Publishing date 2022-04-08
    Publishing country France
    Document type Journal Article ; Review
    ZDB-ID 392415-4
    ISSN 1950-6007 ; 0753-3322 ; 0300-0893
    ISSN (online) 1950-6007
    ISSN 0753-3322 ; 0300-0893
    DOI 10.1016/j.biopha.2022.112924
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    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.198: Show issues Location:
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  9. Article ; Online: ?-Trefoil Protease Inhibitors Unique to Higher Fungi.

    Sabotič, Jerica / Renko, Miha / Kos, Janko

    Acta chimica Slovenica

    2021  Volume 66, Issue 1, Page(s) 28–36

    Abstract: The cysteine protease inhibitors, clitocypin and macrocypins, from higher fungi (mycocypins), together with the serine protease inhibitors highly specific for trypsin cospin and cnispin from higher fungi (mycospins), display several characteristics that ... ...

    Abstract The cysteine protease inhibitors, clitocypin and macrocypins, from higher fungi (mycocypins), together with the serine protease inhibitors highly specific for trypsin cospin and cnispin from higher fungi (mycospins), display several characteristics that distinguish them from protease inhibitors from other sources. Their high genetic heterogeneity affects their functionality and/or stability and results in numerous protein variants with slightly different inhibitory profiles that influence the type of protease inhibited and/or the strength of inhibition. They possess the μ-trefoil fold that shows high plasticity in their utilization of the 11 diverse loops for the inhibition of various families of proteases through different mechanisms of inhibition. Their high versatility is also seen in their regulatory and defence functions and in their potential applications in biotechnology, crop protection and medicine.
    Language English
    Publishing date 2021-04-14
    Publishing country Slovenia
    Document type Journal Article
    ZDB-ID 2029709-9
    ISSN 1580-3155 ; 1318-0207
    ISSN (online) 1580-3155
    ISSN 1318-0207
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  10. Article ; Online: Human CD4+ T-Cell Clone Expansion Leads to the Expression of the Cysteine Peptidase Inhibitor Cystatin F.

    Perišić Nanut, Milica / Pawelec, Graham / Kos, Janko

    International journal of molecular sciences

    2021  Volume 22, Issue 16

    Abstract: The existence of CD4+ cytotoxic T cells (CTLs) at relatively high levels under different pathological conditions in vivo suggests their role in protective and/or pathogenic immune functions. CD4+ CTLs utilize the fundamental cytotoxic effector mechanisms ...

    Abstract The existence of CD4+ cytotoxic T cells (CTLs) at relatively high levels under different pathological conditions in vivo suggests their role in protective and/or pathogenic immune functions. CD4+ CTLs utilize the fundamental cytotoxic effector mechanisms also utilized by CD8+ CTLs and natural killer cells. During long-term cultivation, CD4+ T cells were also shown to acquire cytotoxic functions. In this study, CD4+ human T-cell clones derived from activated peripheral blood lymphocytes of healthy young adults were examined for the expression of cytotoxic machinery components. Cystatin F is a protein inhibitor of cysteine cathepsins, synthesized by CD8+ CTLs and natural killer cells. Cystatin F affects the cytotoxic efficacy of these cells by inhibiting the major progranzyme convertases cathepsins C and H as well as cathepsin L, which is involved in perforin activation. Here, we show that human CD4+ T-cell clones express the cysteine cathepsins that are involved in the activation of granzymes and perforin. CD4+ T-cell clones contained both the inactive, dimeric form as well as the active, monomeric form of cystatin F. As in CD8+ CTLs, cysteine cathepsins C and H were the major targets of cystatin F in CD4+ T-cell clones. Furthermore, CD4+ T-cell clones expressed the active forms of perforin and granzymes A and B. The levels of the cystatin F decreased with time in culture concomitantly with an increase in the activities of granzymes A and B. Therefore, our results suggest that cystatin F plays a role in regulating CD4+ T cell cytotoxicity. Since cystatin F can be secreted and taken up by bystander cells, our results suggest that CD4+ CTLs may also be involved in regulating immune responses through cystatin F secretion.
    MeSH term(s) CD4-Positive T-Lymphocytes/metabolism ; CD8-Positive T-Lymphocytes/metabolism ; Cathepsin C/metabolism ; Cathepsin L/metabolism ; Cell Line, Tumor ; Clone Cells ; Cysteine/metabolism ; Granzymes/metabolism ; Humans ; Jurkat Cells ; Killer Cells, Natural/metabolism ; Lymphocyte Activation/physiology ; Protease Inhibitors/metabolism ; T-Lymphocytes, Cytotoxic/metabolism
    Chemical Substances Protease Inhibitors ; Cathepsin C (EC 3.4.14.1) ; Granzymes (EC 3.4.21.-) ; Cathepsin L (EC 3.4.22.15) ; Cysteine (K848JZ4886)
    Language English
    Publishing date 2021-08-05
    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/ijms22168408
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