LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 45

Search options

  1. Article: Transmembrane 163 (TMEM163) Protein: A New Member of the Zinc Efflux Transporter Family.

    Styrpejko, Daniel J / Cuajungco, Math P

    Biomedicines

    2021  Volume 9, Issue 2

    Abstract: A growing body of evidence continues to demonstrate the vital roles that zinc and its transporters play on human health. The mammalian solute carrier 30 (SLC30) family, with ten current members, controls zinc efflux transport in cells. TMEM163, a ... ...

    Abstract A growing body of evidence continues to demonstrate the vital roles that zinc and its transporters play on human health. The mammalian solute carrier 30 (SLC30) family, with ten current members, controls zinc efflux transport in cells. TMEM163, a recently reported zinc transporter, has similar characteristics in both predicted transmembrane domain structure and function to the cation diffusion facilitator (CDF) protein superfamily. This review discusses past and present data indicating that TMEM163 is a zinc binding protein that transports zinc in cells. We provide a brief background on TMEM163's discovery, transport feature, protein interactome, and similarities, as well as differences, with known SLC30 (ZnT) protein family. We also examine recent reports that implicate TMEM163 directly or indirectly in various human diseases such as Parkinson's disease, Mucolipidosis type IV and diabetes. Overall, the role of TMEM163 protein in zinc metabolism is beginning to be realized, and based on current evidence, we propose that it is likely a new CDF member belonging to mammalian SLC30 (ZnT) zinc efflux transporter proteins.
    Language English
    Publishing date 2021-02-21
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2720867-9
    ISSN 2227-9059
    ISSN 2227-9059
    DOI 10.3390/biomedicines9020220
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article ; Online: Protocol for Quantifying Zinc Flux in Cultured Cells using Fluorescent Indicators.

    Ali, Saima / Cuajungco, Math P

    STAR protocols

    2020  Volume 1, Issue 2, Page(s) 100050

    Abstract: ... Zinc ( ... ...

    Abstract Zinc (Zn
    MeSH term(s) Cation Transport Proteins/metabolism ; Cells, Cultured ; Cytological Techniques/methods ; Fluorescent Dyes/analysis ; Fluorescent Dyes/metabolism ; HeLa Cells ; Humans ; Microscopy, Fluorescence/methods ; Zinc/analysis ; Zinc/metabolism
    Chemical Substances Cation Transport Proteins ; Fluorescent Dyes ; Zinc (J41CSQ7QDS)
    Language English
    Publishing date 2020-06-08
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 2666-1667
    ISSN (online) 2666-1667
    DOI 10.1016/j.xpro.2020.100050
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  3. Article ; Online: Protocol for Quantifying Zinc Flux in Cultured Cells using Fluorescent Indicators

    Saima Ali / Math P. Cuajungco

    STAR Protocols, Vol 1, Iss 2, Pp 100050- (2020)

    2020  

    Abstract: Summary: Zinc (Zn2+) plays a vital role in the functioning of the cell. Cells have influx and efflux zinc transporters to regulate the levels of Zn2+ in the cytoplasm and organellar compartments to maintain homeostasis. We present a protocol to measure ... ...

    Abstract Summary: Zinc (Zn2+) plays a vital role in the functioning of the cell. Cells have influx and efflux zinc transporters to regulate the levels of Zn2+ in the cytoplasm and organellar compartments to maintain homeostasis. We present a protocol to measure changes in cellular zinc concentrations using either a low-affinity membrane permeable or a high-affinity membrane impermeable fluorescent dye. Overall, zinc-specific fluorescent indicators using the assay can reliably detect the Zn2+ flux into or out of cultured cells.For complete details on the use and execution of this protocol, please refer to Sanchez et al. (2019).
    Keywords Science (General) ; Q1-390
    Language English
    Publishing date 2020-09-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

    More links

    Kategorien

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  4. Article: Zinc: Multidimensional Effects on Living Organisms.

    Cuajungco, Math P / Ramirez, Maria Soledad / Tolmasky, Marcelo E

    Biomedicines

    2021  Volume 9, Issue 2

    Abstract: Zinc is a redox-inert trace element that is second only to iron in abundance in biological systems. In cells, zinc is typically buffered and bound to metalloproteins, but it may also exist in a labile or chelatable (free ion) form. Zinc plays a critical ... ...

    Abstract Zinc is a redox-inert trace element that is second only to iron in abundance in biological systems. In cells, zinc is typically buffered and bound to metalloproteins, but it may also exist in a labile or chelatable (free ion) form. Zinc plays a critical role in prokaryotes and eukaryotes, ranging from structural to catalytic to replication to demise. This review discusses the influential properties of zinc on various mechanisms of bacterial proliferation and synergistic action as an antimicrobial element. We also touch upon the significance of zinc among eukaryotic cells and how it may modulate their survival and death through its inhibitory or modulatory effect on certain receptors, enzymes, and signaling proteins. A brief discussion on zinc chelators is also presented, and chelating agents may be used with or against zinc to affect therapeutics against human diseases. Overall, the multidimensional effects of zinc in cells attest to the growing number of scientific research that reveal the consequential prominence of this remarkable transition metal in human health and disease.
    Language English
    Publishing date 2021-02-22
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2720867-9
    ISSN 2227-9059
    ISSN 2227-9059
    DOI 10.3390/biomedicines9020208
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article ; Online: Transmembrane 163 (TMEM163) protein interacts with specific mammalian SLC30 zinc efflux transporter family members.

    Escobar, Adrian / Styrpejko, Daniel J / Ali, Saima / Cuajungco, Math P

    Biochemistry and biophysics reports

    2022  Volume 32, Page(s) 101362

    Abstract: Recently, we reported that TMEM163 is a zinc efflux transporter that likely belongs to the mammalian solute carrier 30 (Slc30/ZnT) subfamily of the cation diffusion facilitator (CDF) protein superfamily. We hypothesized that human TMEM163 forms ... ...

    Abstract Recently, we reported that TMEM163 is a zinc efflux transporter that likely belongs to the mammalian solute carrier 30 (Slc30/ZnT) subfamily of the cation diffusion facilitator (CDF) protein superfamily. We hypothesized that human TMEM163 forms functional heterodimers with certain ZNT proteins based on their overlapping subcellular localization with TMEM163 and previous reports that some ZNT monomers interact with each other. In this study, we heterologously expressed individual constructs with a unique peptide tag containing TMEM163, ZNT1, ZNT2, ZNT3, and ZNT4 (negative control) or co-expressed TMEM163 with each ZNT in cultured cells for co-immunoprecipitation (co-IP) experiments. We also co-expressed TMEM163 with two different peptide tags as a positive co-IP control. Western blot analyses revealed that TMEM163 dimerizes with itself but that it also heterodimerizes with ZNT1, ZNT2, ZNT3, and ZNT4 proteins. Confocal microscopy revealed that TMEM163 and ZNT proteins partially co-localize in cells, suggesting that they exist as homodimers and heterodimers in their respective subcellular sites. Functional zinc flux assays using Fluozin-3 and Newport Green dyes show that TMEM163/ZNT heterodimers exhibit similar efflux function as TMEM163 homodimers. Cell surface biotinylation revealed that the plasma membrane localization of TMEM163 is not markedly influenced by ZNT co-expression. Overall, our results show that the interaction between TMEM163 and distinct ZNT proteins is physiologically relevant and that their heterodimerization may serve to increase the functional diversity of zinc effluxers within specific tissues or cell types.
    Language English
    Publishing date 2022-10-01
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 2831046-9
    ISSN 2405-5808 ; 2405-5808
    ISSN (online) 2405-5808
    ISSN 2405-5808
    DOI 10.1016/j.bbrep.2022.101362
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  6. Article ; Online: Transmembrane 163 (TMEM163) Protein

    Daniel J. Styrpejko / Math P. Cuajungco

    Biomedicines, Vol 9, Iss 2, p

    A New Member of the Zinc Efflux Transporter Family

    2021  Volume 220

    Abstract: A growing body of evidence continues to demonstrate the vital roles that zinc and its transporters play on human health. The mammalian solute carrier 30 (SLC30) family, with ten current members, controls zinc efflux transport in cells. TMEM163, a ... ...

    Abstract A growing body of evidence continues to demonstrate the vital roles that zinc and its transporters play on human health. The mammalian solute carrier 30 (SLC30) family, with ten current members, controls zinc efflux transport in cells. TMEM163, a recently reported zinc transporter, has similar characteristics in both predicted transmembrane domain structure and function to the cation diffusion facilitator (CDF) protein superfamily. This review discusses past and present data indicating that TMEM163 is a zinc binding protein that transports zinc in cells. We provide a brief background on TMEM163’s discovery, transport feature, protein interactome, and similarities, as well as differences, with known SLC30 (ZnT) protein family. We also examine recent reports that implicate TMEM163 directly or indirectly in various human diseases such as Parkinson’s disease, Mucolipidosis type IV and diabetes. Overall, the role of TMEM163 protein in zinc metabolism is beginning to be realized, and based on current evidence, we propose that it is likely a new CDF member belonging to mammalian SLC30 (ZnT) zinc efflux transporter proteins.
    Keywords zinc ; cation diffusion facilitator ; zinc transporter ; SV31 ; Biology (General) ; QH301-705.5
    Subject code 612
    Language English
    Publishing date 2021-02-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

    More links

    Kategorien

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  7. Article ; Online: The mucolipin-1 (TRPML1) ion channel, transmembrane-163 (TMEM163) protein, and lysosomal zinc handling.

    Cuajungco, Math P / Kiselyov, Kirill

    Frontiers in bioscience (Landmark edition)

    2017  Volume 22, Issue 8, Page(s) 1330–1343

    Abstract: Lysosomes are emerging as important players in cellular zinc ion ( ... ...

    Abstract Lysosomes are emerging as important players in cellular zinc ion (Zn
    MeSH term(s) Amino Acid Sequence ; Animals ; Humans ; Ion Transport ; Lysosomes/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Neurons/metabolism ; Transient Receptor Potential Channels/genetics ; Transient Receptor Potential Channels/metabolism ; Zinc/metabolism
    Chemical Substances MCOLN1 protein, human ; Membrane Proteins ; TMEM163 protein, human ; Transient Receptor Potential Channels ; Zinc (J41CSQ7QDS)
    Language English
    Publishing date 2017-03-01
    Publishing country Singapore
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, Non-U.S. Gov't
    ZDB-ID 2704569-9
    ISSN 2768-6698 ; 1093-9946
    ISSN (online) 2768-6698
    ISSN 1093-9946
    DOI 10.2741/4546
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  8. Article ; Online: Zinc

    Math P. Cuajungco / Maria Soledad Ramirez / Marcelo E. Tolmasky

    Biomedicines, Vol 9, Iss 2, p

    Multidimensional Effects on Living Organisms

    2021  Volume 208

    Abstract: Zinc is a redox-inert trace element that is second only to iron in abundance in biological systems. In cells, zinc is typically buffered and bound to metalloproteins, but it may also exist in a labile or chelatable (free ion) form. Zinc plays a critical ... ...

    Abstract Zinc is a redox-inert trace element that is second only to iron in abundance in biological systems. In cells, zinc is typically buffered and bound to metalloproteins, but it may also exist in a labile or chelatable (free ion) form. Zinc plays a critical role in prokaryotes and eukaryotes, ranging from structural to catalytic to replication to demise. This review discusses the influential properties of zinc on various mechanisms of bacterial proliferation and synergistic action as an antimicrobial element. We also touch upon the significance of zinc among eukaryotic cells and how it may modulate their survival and death through its inhibitory or modulatory effect on certain receptors, enzymes, and signaling proteins. A brief discussion on zinc chelators is also presented, and chelating agents may be used with or against zinc to affect therapeutics against human diseases. Overall, the multidimensional effects of zinc in cells attest to the growing number of scientific research that reveal the consequential prominence of this remarkable transition metal in human health and disease.
    Keywords metalloproteins ; zinc transporters ; metal chelators ; antibiotic resistance ; antimicrobials ; Biology (General) ; QH301-705.5
    Subject code 612
    Language English
    Publishing date 2021-02-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

    More links

    Kategorien

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  9. Article ; Online: ZnT3 expression levels are down-regulated in the brain of Mcoln1 knockout mice.

    Chacon, Jonathan / Rosas, Lauren / Cuajungco, Math P

    Molecular brain

    2019  Volume 12, Issue 1, Page(s) 24

    Abstract: Aim: Zinc is a critical divalent cation in mammalian brain, but its concentration must be strictly-controlled. Within certain subsets of glutamatergic neurons, ZnT3 (encoded by the Slc30a3 gene) facilitates the transport and storage of zinc in synaptic ... ...

    Abstract Aim: Zinc is a critical divalent cation in mammalian brain, but its concentration must be strictly-controlled. Within certain subsets of glutamatergic neurons, ZnT3 (encoded by the Slc30a3 gene) facilitates the transport and storage of zinc in synaptic vesicles. It has been previously reported that Slc30a3 mRNA levels are perturbed in numerous neurodegenerative disorders. Given the growing evidence of zinc dysregulation in another neurodegenerative disease known as Mucolipidosis IV (MLIV), we hypothesized that abnormal ZnT3 expression would be observed in the brain of MLIV mouse model. Elucidating the link between abnormal ZnT3 and zinc levels could reveal the neuropathological correlates between MLIV and other age-related brain disorders.
    Methods: Total RNAs from cortical tissues of Mucolipin-1 knockout (Mcoln1
    Results: RNA-seq analysis showed a marked decrease in baseline levels of Slc30a3 mRNA in Mcoln1
    MeSH term(s) Animals ; Brain/metabolism ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Down-Regulation/genetics ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Membrane Transport Proteins ; Mice, Knockout ; Mucolipidoses/genetics ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Transient Receptor Potential Channels/metabolism
    Chemical Substances Carrier Proteins ; Mcoln1 protein, mouse ; Membrane Proteins ; Membrane Transport Proteins ; RNA, Messenger ; Slc30a3 protein, mouse ; Transient Receptor Potential Channels
    Language English
    Publishing date 2019-03-26
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2436057-0
    ISSN 1756-6606 ; 1756-6606
    ISSN (online) 1756-6606
    ISSN 1756-6606
    DOI 10.1186/s13041-019-0446-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  10. Article: Comparative De Novo Transcriptome Assembly of

    Chacon, Jonathan / Cuajungco, Math P

    Californian journal of health promotion

    2016  Volume 16, Issue 1, Page(s) 46–53

    Abstract: Background and purpose: The reduction of cost and ease of using core laboratories or commercial sequencing companies have allowed biomedical and health researchers alike to employ reference-based genomic or transcriptomic sequencing (RNA-seq) projects ... ...

    Abstract Background and purpose: The reduction of cost and ease of using core laboratories or commercial sequencing companies have allowed biomedical and health researchers alike to employ reference-based genomic or transcriptomic sequencing (RNA-seq) projects to expand their work. Non-reference based data analysis, in cases of inexperienced researchers, become more challenging despite the availability of many open source and commercial software programs.
    Methods: We performed de novo assembly of RNA-seq data obtained from a non-model organism (Eastern Newt skin) to compare data output of two commercially available software workflows.
    Results: Our results show that the software packages performed satisfactorily albeit with differences in how the annotated and novel transcripts were identified and listed.
    Conclusion: Overall, we conclude that the use of commercial software platforms has a clear advantage to that of open source programs because of convenience with data analysis workflows. One caveat is that users need to know the software's basic algorithm and technical approach, in order to determine the precision and validity of the data output. Thus, it is imperative that researchers fully evaluate the software according to their needs to determine their suitability.
    Language English
    Publishing date 2016-06-01
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2434589-1
    ISSN 1545-8725
    ISSN 1545-8725
    DOI 10.32398/cjhp_20181601
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top