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Article: Epidermal Stem Cells.

Lenkiewicz, Anna M

Advances in experimental medicine and biology

2020 Volume 1201, Page(s) 239–259

Abstract: A multilayered epithelium to fulfil its function must be replaced throughout the lifespan. This is possible due to the presence of multipotent, self-renewing epidermal stem cells that give rise to differentiated cell lineages: keratinocytes, hairs, as ... ...

Abstract	A multilayered epithelium to fulfil its function must be replaced throughout the lifespan. This is possible due to the presence of multipotent, self-renewing epidermal stem cells that give rise to differentiated cell lineages: keratinocytes, hairs, as well as sebocytes. Till now the molecular mechanisms responsible for stem cell quiescent, proliferation, and differentiation have not been fully established. It is suggested that epidermal stem cells might change their fate, both due to intrinsic events and as a result of niche-dependent extrinsic signals; however other yet unknown factors may also be involved in this process. Given the increasing excitement evoked by self-renewing epidermal stem cells, as one of the sources of adult stem cells, it seems important to reveal the mechanisms that govern their fate. In this chapter, we describe recent advances in the characterisation of the epidermal stem cells and their compartments. Furthermore, we focus on the interplay between epidermal stem cells and extrinsic signals and their role in quiescence, proliferation, and differentiation of appropriate epidermal stem cell lineages.
MeSH term(s)	Cell Differentiation ; Cell Division ; Cell Lineage ; Epidermal Cells/cytology ; Stem Cells/cytology
Language	English
Publishing date	2020-01-03
Publishing country	United States
Document type	Journal Article ; Review
ISSN	2214-8019 ; 0065-2598
ISSN (online)	2214-8019
ISSN	0065-2598
DOI	10.1007/978-3-030-31206-0_12
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Article: The Interplay of Tumor Vessels and Immune Cells Affects Immunotherapy of Glioblastoma.

Ghosh, Mitrajit / Lenkiewicz, Anna M / Kaminska, Bozena

Biomedicines

2022 Volume 10, Issue 9

Abstract: Immunotherapies with immune checkpoint inhibitors or adoptive cell transfer have become powerful tools to treat cancer. These treatments act via overcoming or alleviating tumor-induced immunosuppression, thereby enabling effective tumor clearance. ... ...

Abstract	Immunotherapies with immune checkpoint inhibitors or adoptive cell transfer have become powerful tools to treat cancer. These treatments act via overcoming or alleviating tumor-induced immunosuppression, thereby enabling effective tumor clearance. Glioblastoma (GBM) represents the most aggressive, primary brain tumor that remains refractory to the benefits of immunotherapy. The immunosuppressive immune tumor microenvironment (TME), genetic and cellular heterogeneity, and disorganized vasculature hinder drug delivery and block effector immune cell trafficking and activation, consequently rendering immunotherapy ineffective. Within the TME, the mutual interactions between tumor, immune and endothelial cells result in the generation of positive feedback loops, which intensify immunosuppression and support tumor progression. We focus here on the role of aberrant tumor vasculature and how it can mediate hypoxia and immunosuppression. We discuss how immune cells use immunosuppressive signaling for tumor progression and contribute to the development of resistance to immunotherapy. Finally, we assess how a positive feedback loop between vascular normalization and immune cells, including myeloid cells, could be targeted by combinatorial therapies with immune checkpoint blockers and sensitize the tumor to immunotherapy.
Language	English
Publishing date	2022-09-15
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2720867-9
ISSN	2227-9059
ISSN	2227-9059
DOI	10.3390/biomedicines10092292
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Article ; Online: Cytosolic Quality Control of Mitochondrial Protein Precursors-The Early Stages of the Organelle Biogenesis.

Lenkiewicz, Anna M / Krakowczyk, Magda / Bragoszewski, Piotr

International journal of molecular sciences

2021 Volume 23, Issue 1

Abstract: With few exceptions, proteins that constitute the proteome of mitochondria originate outside of this organelle in precursor forms. Such protein precursors follow dedicated transportation paths to reach specific parts of mitochondria, where they complete ... ...

Abstract	With few exceptions, proteins that constitute the proteome of mitochondria originate outside of this organelle in precursor forms. Such protein precursors follow dedicated transportation paths to reach specific parts of mitochondria, where they complete their maturation and perform their functions. Mitochondrial precursor targeting and import pathways are essential to maintain proper mitochondrial function and cell survival, thus are tightly controlled at each stage. Mechanisms that sustain protein homeostasis of the cytosol play a vital role in the quality control of proteins targeted to the organelle. Starting from their synthesis, precursors are constantly chaperoned and guided to reduce the risk of premature folding, erroneous interactions, or protein damage. The ubiquitin-proteasome system provides proteolytic control that is not restricted to defective proteins but also regulates the supply of precursors to the organelle. Recent discoveries provide evidence that stress caused by the mislocalization of mitochondrial proteins may contribute to disease development. Precursors are not only subject to regulation but also modulate cytosolic machinery. Here we provide an overview of the cellular pathways that are involved in precursor maintenance and guidance at the early cytosolic stages of mitochondrial biogenesis. Moreover, we follow the circumstances in which mitochondrial protein import deregulation disturbs the cellular balance, carefully looking for rescue paths that can restore proteostasis.
MeSH term(s)	Cell Survival ; Cytosol/metabolism ; Humans ; Mitochondria/physiology ; Mitochondrial Proteins/metabolism ; Organelle Biogenesis ; Protein Precursors/metabolism ; Protein Transport
Chemical Substances	Mitochondrial Proteins ; Protein Precursors
Language	English
Publishing date	2021-12-21
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms23010007
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Article ; Online: OMA1 protease eliminates arrested protein import intermediates upon mitochondrial depolarization.

Krakowczyk, Magda / Lenkiewicz, Anna M / Sitarz, Tomasz / Malinska, Dominika / Borrero, Mayra / Mussulini, Ben Hur Marins / Linke, Vanessa / Szczepankiewicz, Andrzej A / Biazik, Joanna M / Wydrych, Agata / Nieznanska, Hanna / Serwa, Remigiusz A / Chacinska, Agnieszka / Bragoszewski, Piotr

The Journal of cell biology

2024 Volume 223, Issue 5

Abstract: Most mitochondrial proteins originate from the cytosol and require transport into the organelle. Such precursor proteins must be unfolded to pass through translocation channels in mitochondrial membranes. Misfolding of transported proteins can result in ... ...

Abstract	Most mitochondrial proteins originate from the cytosol and require transport into the organelle. Such precursor proteins must be unfolded to pass through translocation channels in mitochondrial membranes. Misfolding of transported proteins can result in their arrest and translocation failure. Arrested proteins block further import, disturbing mitochondrial functions and cellular proteostasis. Cellular responses to translocation failure have been defined in yeast. We developed the cell line-based translocase clogging model to discover molecular mechanisms that resolve failed import events in humans. The mechanism we uncover differs significantly from these described in fungi, where ATPase-driven extraction of blocked protein is directly coupled with proteasomal processing. We found human cells to rely primarily on mitochondrial factors to clear translocation channel blockage. The mitochondrial membrane depolarization triggered proteolytic cleavage of the stalled protein, which involved mitochondrial protease OMA1. The cleavage allowed releasing the protein fragment that blocked the translocase. The released fragment was further cleared in the cytosol by VCP/p97 and the proteasome.
MeSH term(s)	Humans ; Endopeptidases ; Mitochondria/metabolism ; Proteasome Endopeptidase Complex ; Protein Transport ; Proteolysis ; Metalloendopeptidases/metabolism
Chemical Substances	Endopeptidases (EC 3.4.-) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; molecule metalloprotease-related protein-1, human (EC 3.4.24.-) ; Metalloendopeptidases (EC 3.4.24.-)
Language	English
Publishing date	2024-03-26
Publishing country	United States
Document type	Journal Article
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202306051
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Article ; Online: The interplay between parkin and alpha-synuclein; possible implications for the pathogenesis of Parkinson's disease.

Jęśko, Henryk / Lenkiewicz, Anna M / Wilkaniec, Anna / Adamczyk, Agata

Acta neurobiologiae experimentalis

2019 Volume 79, Issue 3, Page(s) 276–289

Abstract: Parkin and alpha-synuclein (α-syn) are two key proteins involved in the pathophysiology of Parkinson's disease (PD). Oligomerization/aggregation and excessive secretion of α-syn contributes to PD through free radical stress, mitochondrial impairment, and ...

Abstract	Parkin and alpha-synuclein (α-syn) are two key proteins involved in the pathophysiology of Parkinson's disease (PD). Oligomerization/aggregation and excessive secretion of α-syn contributes to PD through free radical stress, mitochondrial impairment, and synaptic dysfunction. Parkin, an E3 ubiquitin ligase, is considered to be a pleiotropic, neuroprotective protein that modulates metabolic turnover and the accumulation of α-syn. This is in addition to parkin's role in counteracting the more distant effects of α-syn on cellular survival by altering proteasomal, autophagic, and calpain-mediated protein degradation pathways that can reduce α-syn levels. Moreover, parkin regulates mitochondrial turnover, cell survival, and immune phenomena - processes that are all known to be disturbed in PD. In addition, parkin might have an impact on the spreading and propagation of α-syn by controlling its post-translational modifications. On the other hand, recent research has shown that α-syn oligomers affect the expression, post-translational modification, and activity of parkin. This review focuses on the molecular mechanisms of cross-talk between parkin and α-syn in PD. The physical and functional interactions between α-syn and parkin, which have been incompletely characterized to-date, may present a new therapeutic avenue in PD and related synucleinopathies. The development of effective, clinically feasible modulators may offer great hopes for the the rapy of PD.
MeSH term(s)	Animals ; Brain/metabolism ; Humans ; Mutation/genetics ; Parkinson Disease/genetics ; Parkinson Disease/metabolism ; Phosphorylation ; Ubiquitin-Protein Ligases/genetics ; alpha-Synuclein/genetics ; alpha-Synuclein/metabolism
Chemical Substances	alpha-Synuclein ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; parkin protein (EC 2.3.2.27)
Language	English
Publishing date	2019-09-28
Publishing country	Poland
Document type	Journal Article ; Review
ZDB-ID	184409-x
ISSN	1689-0035 ; 0065-1400
ISSN (online)	1689-0035
ISSN	0065-1400
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Article ; Online: Treatments and compositions targeting α-synuclein: a patent review (2010-2016).

Jęśko, Henryk / Lenkiewicz, Anna M / Adamczyk, Agata

Expert opinion on therapeutic patents

2017 Volume 27, Issue 4, Page(s) 427–438

Abstract: Introduction: Abnormal deposition of α-synuclein (ASN) is a hallmark and possible central mechanism of Parkinson's disease and other synucleinopathies. Their therapy is currently hampered by the lack of early, screening-compatible diagnostic methods and ...

Abstract	Introduction: Abnormal deposition of α-synuclein (ASN) is a hallmark and possible central mechanism of Parkinson's disease and other synucleinopathies. Their therapy is currently hampered by the lack of early, screening-compatible diagnostic methods and efficient treatments. Areas covered: Patent applications related to synucleinopathies obtained from Patentscope and Espacenet databases are described against the background of current knowledge regarding the regulatory mechanisms of ASN behavior including alternative splicing, post-translational modifications, molecular interactions, aggregation, degradation, and changes in localization. Expert opinion: As the central pathological feature and possibly one of root causes in a number of neurodegenerative diseases, deregulation of ASN is a potentially optimal diagnostic and therapeutic target. Changes in total ASN may have diagnostic value, especially if non-invasive /peripheral tissue tests can be developed. Targeting the whole ASN pool for therapeutic purposes may be problematic, however. ASN mutations, truncation, and post-translational modifications have great potential value; therapeutic approaches selective towards aggregated or aggregation-prone ASN forms may lead to more successful and safe treatments. Numerous ASN interactions with signaling pathways, protein degradation and stress mechanisms widen its potential therapeutic significance dramatically. However, significant improvement in the basic knowledge on ASN is necessary to fully exploit these opportunities.
MeSH term(s)	Animals ; Antiparkinson Agents/pharmacology ; Drug Design ; Humans ; Neurodegenerative Diseases/diagnosis ; Neurodegenerative Diseases/drug therapy ; Neurodegenerative Diseases/physiopathology ; Parkinson Disease/diagnosis ; Parkinson Disease/drug therapy ; Parkinson Disease/physiopathology ; Patents as Topic ; Signal Transduction/drug effects ; alpha-Synuclein/metabolism
Chemical Substances	Antiparkinson Agents ; alpha-Synuclein
Language	English
Publishing date	2017-04
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1186201-4
ISSN	1744-7674 ; 0962-2594 ; 1354-3776
ISSN (online)	1744-7674
ISSN	0962-2594 ; 1354-3776
DOI	10.1080/13543776.2017.1261112
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Article: Exogenous Alpha-Synuclein Evoked Parkin Downregulation Promotes Mitochondrial Dysfunction in Neuronal Cells. Implications for Parkinson's Disease Pathology.

Wilkaniec, Anna / Lenkiewicz, Anna M / Babiec, Lidia / Murawska, Emilia / Jęśko, Henryk M / Cieślik, Magdalena / Culmsee, Carsten / Adamczyk, Agata

Frontiers in aging neuroscience

2021 Volume 13, Page(s) 591475

Abstract: Aberrant secretion and accumulation of α-synuclein (α-Syn) as well as the loss of parkin function are associated with the pathogenesis of Parkinson's disease (PD). Our previous study suggested a functional interaction between those two proteins, showing ... ...

Abstract	Aberrant secretion and accumulation of α-synuclein (α-Syn) as well as the loss of parkin function are associated with the pathogenesis of Parkinson's disease (PD). Our previous study suggested a functional interaction between those two proteins, showing that the extracellular α-Syn evoked post-translational modifications of parkin, leading to its autoubiquitination and degradation. While parkin plays an important role in mitochondrial biogenesis and turnover, including mitochondrial fission/fusion as well as mitophagy, the involvement of parkin deregulation in α-Syn-induced mitochondrial damage is largely unknown. In the present study, we demonstrated that treatment with exogenous α-Syn triggers mitochondrial dysfunction, reflected by the depolarization of the mitochondrial membrane, elevated synthesis of the mitochondrial superoxide anion, and a decrease in cellular ATP level. At the same time, we observed a protective effect of parkin overexpression on α-Syn-induced mitochondrial dysfunction. α-Syn-dependent disturbances of mitophagy were also shown to be directly related to reduced parkin levels in mitochondria and decreased ubiquitination of mitochondrial proteins. Also, α-Syn impaired mitochondrial biosynthesis due to the parkin-dependent reduction of PGC-1α protein levels. Finally, loss of parkin function as a result of α-Syn treatment induced an overall breakdown of mitochondrial homeostasis that led to the accumulation of abnormal mitochondria. These findings may thus provide the first compelling evidence for the direct association of α-Syn-mediated parkin depletion to impaired mitochondrial function in PD. We suggest that improvement of parkin function may serve as a novel therapeutic strategy to prevent mitochondrial impairment and neurodegeneration in PD (thereby slowing the progression of the disease).
Language	English
Publishing date	2021-02-24
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2558898-9
ISSN	1663-4365
ISSN	1663-4365
DOI	10.3389/fnagi.2021.591475
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Article ; Online: Novel evidence that an alternative complement cascade pathway is involved in optimal mobilization of hematopoietic stem/progenitor cells in Nlrp3 inflammasome-dependent manner.

Adamiak, Mateusz / Lenkiewicz, Anna M / Cymer, Monika / Kucia, Magda / Ratajczak, Janina / Ratajczak, Mariusz Z

Leukemia

2019 Volume 33, Issue 12, Page(s) 2967–2970

MeSH term(s)	Animals ; Complement Activation/immunology ; Complement System Proteins/immunology ; Complement System Proteins/metabolism ; Hematopoietic Stem Cell Mobilization ; Hematopoietic Stem Cells/cytology ; Hematopoietic Stem Cells/immunology ; Hematopoietic Stem Cells/metabolism ; Humans ; Immunity, Innate ; Mice ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism
Chemical Substances	NLR Family, Pyrin Domain-Containing 3 Protein ; NLRP3 protein, human ; Complement System Proteins (9007-36-7)
Language	English
Publishing date	2019-07-26
Publishing country	England
Document type	Letter ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	807030-1
ISSN	1476-5551 ; 0887-6924
ISSN (online)	1476-5551
ISSN	0887-6924
DOI	10.1038/s41375-019-0530-9
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Article ; Online: NLRP3 inflammasome couples purinergic signaling with activation of the complement cascade for the optimal release of cells from bone marrow.

Ratajczak, Mariusz Z / Adamiak, Mateusz / Thapa, Arjun / Bujko, Kamila / Brzezniakiewicz-Janus, Katarzyna / Lenkiewicz, Anna M

Leukemia

2019 Volume 33, Issue 4, Page(s) 815–825

Abstract: The mechanisms that regulate egress of hematopoietic stem/progenitor cells (HSPCs) into peripheral blood (PB) in response to stress, inflammation, tissue/organ injury, or administration of mobilization-inducing drugs are still not well understood, and ... ...

Abstract	The mechanisms that regulate egress of hematopoietic stem/progenitor cells (HSPCs) into peripheral blood (PB) in response to stress, inflammation, tissue/organ injury, or administration of mobilization-inducing drugs are still not well understood, and because of the importance of stem cell trafficking in maintaining organism homeostasis, several complementary pathways are believed to be involved. Our group proposes that mobilization of HSPCs is mainly a result of sterile inflammation in the bone marrow (BM) microenvironment in response to pro-mobilizing stimuli and that during the initiation phase of the mobilization process BM-residing cells belonging to the innate immunity system, including granulocytes and monocytes, release danger-associated molecular pattern molecules (DAMPs, also known as alarmins), reactive oxygen species (ROS), as well as proteolytic and lipolytic enzymes. These factors together orchestrate the release of HSPCs into PB. One of the most important DAMPs released in the initiation phase of mobilization is extracellular adenosine triphosphate, a potent activator of the inflammasome. As a result of its activation, IL-1β and IL-18 as well as other pro-mobilizing mediators, including DAMPs such as high molecular group box 1 (Hmgb1) and S100 calcium-binding protein A9 (S100a9), are released. These DAMPs are important activators of the complement cascade (ComC) in the mannan-binding lectin (MBL)-dependent pathway. Specifically, Hmgb1 and S100a9 bind to MBL, which leads to activation of MBL-associated proteases, which activate the ComC and in parallel also trigger activation of the coagulation cascade (CoaC). In this review, we will highlight the novel role of the innate immunity cell-expressed NLRP3 inflammasome, which, during the initiation phase of HSPC mobilization, couples purinergic signaling with the MBL-dependent pathway of the ComC and, in parallel, the CoaC for optimal release of HSPCs. These data are important to optimize the pharmacological mobilization of HSPCs.
MeSH term(s)	Animals ; Bone Marrow/immunology ; Bone Marrow/metabolism ; Bone Marrow/pathology ; Complement Activation/immunology ; Hematopoietic Stem Cell Mobilization ; Humans ; Immunity, Innate/immunology ; Inflammasomes/immunology ; Inflammasomes/metabolism ; Inflammation/immunology ; Inflammation/pathology ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism ; Purines/metabolism
Chemical Substances	Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein ; Purines
Language	English
Publishing date	2019-03-07
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	807030-1
ISSN	1476-5551 ; 0887-6924
ISSN (online)	1476-5551
ISSN	0887-6924
DOI	10.1038/s41375-019-0436-6
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Article ; Online: Selol, an organic selenium donor, prevents lipopolysaccharide-induced oxidative stress and inflammatory reaction in the rat brain.

Dominiak, Agnieszka / Wilkaniec, Anna / Jęśko, Henryk / Czapski, Grzegorz A / Lenkiewicz, Anna M / Kurek, Eliza / Wroczyński, Piotr / Adamczyk, Agata

Neurochemistry international

2017 Volume 108, Page(s) 66–77

Abstract: Neuroinflammation and oxidative stress are key intertwined pathological factors in many neurological, particularly neurodegenerative diseases, such as Alzheimer's and Parkinson's disorders as well as autism. The present study was conducted to evaluate ... ...

Abstract	Neuroinflammation and oxidative stress are key intertwined pathological factors in many neurological, particularly neurodegenerative diseases, such as Alzheimer's and Parkinson's disorders as well as autism. The present study was conducted to evaluate the protective effects of Selol, an organic selenium donor, against lipopolysaccharide (LPS)-mediated inflammation in rat brain. The results demonstrated that the peripheral administration of LPS in a dose of 100 μg/kg b.w. evoked typical pathological reaction known as systemic inflammatory response. Moreover, we observed elevated blood levels of thiobarbituric acid-reactive substances (TBARS), a marker of oxidative stress, as well as increased concentration of tumor necrosis factor-α (TNF-α) in LPS-treated animals. Selol significantly prevented these LPS-evoked changes. Subsequently, Selol protected against LPS-induced up-regulation of proinflammatory cytokines (Tnfa, Ifng, Il6) in rat brain cortex. The molecular mechanisms through which Selol prevented the neuroinflammation were associated with the inhibition of oxidized glutathione (GSSG) accumulation and with an increase of glutathione-associated enzymes: glutathione peroxidase (Se-GPx), glutathione reductase (GR) as well as thioredoxin reductase (TrxR) activity and expression. Finally, we observed that Selol administration effectively protected against LPS-induced changes in the expression of brain-derived neurotrophic factor (Bdnf). In conclusion, our studies indicated that Selol effectively protects against LPS-induced neuroinflammation by inhibiting pro-inflammatory cytokine release, by boosting antioxidant systems, and by augmenting BDNF level. Therefore, Selol could be a multi-potent and effective drug useful in the treatment and prevention of brain disorders associated with neuroinflammation.
Language	English
Publishing date	2017-09
Publishing country	England
Document type	Journal Article
ZDB-ID	283190-9
ISSN	1872-9754 ; 0197-0186
ISSN (online)	1872-9754
ISSN	0197-0186
DOI	10.1016/j.neuint.2017.02.014
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