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  1. Article ; Online: Cathepsin E (EC 3.4.23.34) — a review

    Anna Worowska / Marek Gacko / Michał Chlabicz / Radosław Łapiński

    Folia Histochemica et Cytobiologica, Vol 49, Iss 4, Pp 547-

    2012  Volume 557

    Abstract: Cathepsin E belongs to the third class of enzymes — hydrolases, a subclass of peptide bond hydrolases and a sub-subclass of endopeptidases with aspartic catalytic sites. Cathepsin E is an endopeptidase with substrate specificity similar to that of ... ...

    Abstract Cathepsin E belongs to the third class of enzymes — hydrolases, a subclass of peptide bond hydrolases and a sub-subclass of endopeptidases with aspartic catalytic sites. Cathepsin E is an endopeptidase with substrate specificity similar to that of cathepsin D. In a human organism, cathepsin E occurs in: erythrocytes, thymus, dendritic cells, epithelial M cells, microglia cells, Langerhans cells, lymphocytes, epithelium of gastrointestinal tract, urinary bladder, lungs, osteoclasts, spleen and lymphatic nodes. In human cells, loci of the gene of pre-procathepsin E are located on chromosome 1 in the region 1231-32. The catalytic site of cathepsin E is two residues of aspartic acid — Asp96 and Asn281, occurring in amino acid triads with sequences DTG96-98 and DTG281-283. To date, no particular role of cathepsin E in the metabolism of proteins in normal tissues has been found. However, it is known that there are many documented pathological conditions in which overexpression of cathepsin E occurs. ( Folia Histochemica et Cytobiologica 2011; Vol. 49, No. 4, pp. 547–557 )
    Keywords cathepsin E ; cathepsin D ; Biology (General) ; QH301-705.5 ; Science ; Q ; DOAJ:Biology ; DOAJ:Biology and Life Sciences
    Subject code 570
    Language English
    Publishing date 2012-01-01T00:00:00Z
    Publisher Polish Histochemical and Cytochemical Society
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Effect of heavy metal cations on the activity of cathepsin D (in vitro study) Effect of heavy metal cations on the activity of cathepsin D (in vitro study)

    Alicja Karwowska / Radosław Łapiński / Marek Gacko / Ewa Grzegorczyk / Joanna Żurawska / Jan K. Karczewski

    Folia Histochemica et Cytobiologica, Vol 50, Iss 3, Pp 432-

    2012  Volume 435

    Abstract: We studied the effect of heavy metal cations: Fe 2+, Cu2+, Zn2+, Cd2+, Hg2+, Pb2+ on the activity of cathepsin D in human aorta homogenate and blood serum. The concentration of cations was 1 mmol/l. Hemoglobin was the cathepsin D substrate. The activity ... ...

    Abstract We studied the effect of heavy metal cations: Fe 2+, Cu2+, Zn2+, Cd2+, Hg2+, Pb2+ on the activity of cathepsin D in human aorta homogenate and blood serum. The concentration of cations was 1 mmol/l. Hemoglobin was the cathepsin D substrate. The activity of cathepsin D was determined at pH 3.5. Only Hg2+ cations inhibit the activity of cathepsin D. Cations Hg2+ damage lysosomes and release cathepsin D from these organelles. We studied the effect of heavy metal cations: Fe 2+, Cu2+, Zn2+, Cd2+, Hg2+, Pb2+ on the activity of cathepsin D in human aorta homogenate and blood serum. The concentration of cations was 1 mmol/l. Hemoglobin was the cathepsin D substrate. The activity of cathepsin D was determined at pH 3.5. Only Hg2+ cations inhibit the activity of cathepsin D. Cations Hg2+ damage lysosomes and release cathepsin D from these organelles.
    Keywords Biology (General) ; QH301-705.5 ; Science ; Q ; DOAJ:Biology ; DOAJ:Biology and Life Sciences
    Subject code 690
    Language English
    Publishing date 2012-10-01T00:00:00Z
    Publisher Polish Histochemical and Cytochemical Society
    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.

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