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  1. Article: Importance of the propeptide in the biosynthetic maturation of rat cathepsin C.

    Santilman, Virginie / Jadot, Michel / Mainferme, Francis

    European journal of cell biology

    2002  Volume 81, Issue 12, Page(s) 654–663

    Abstract: Cathepsin C is a cysteine dipeptidyl-aminopeptidase. Active cathepsin C is found in lysosomes as a 200-kDa multimeric enzyme. Subunits constituting this assembly all arise from the proteolytic cleavage of a single precursor giving rise to three peptides: ...

    Abstract Cathepsin C is a cysteine dipeptidyl-aminopeptidase. Active cathepsin C is found in lysosomes as a 200-kDa multimeric enzyme. Subunits constituting this assembly all arise from the proteolytic cleavage of a single precursor giving rise to three peptides: the propeptide, the alpha- and the beta-chains. Some features of the propeptide such as its length, its high level of glycosylation and its retention in the active lysosomal form of the enzyme suggest an important contribution of the proregion in the transport, maturation and expression of cathepsin C. In order to assess some aspects of this contribution, we transiently expressed mutant molecules of rat cathepsin C either lacking three of the four glycosylation sites, partially deleted in the proregion, or mutated at tryptophan 39 also located in the proregion, and studied their biosynthesis. Our results show that at least one of the three glycosylation sites in the propeptide must be glycosylated in order to obtain targeting and maturation of cathepsin C. We also show that a deletion of 14 amino acids and mutation W39S in the propeptide totally abolishes the biosynthetic processing of the enzyme. These results demonstrate that in addition to its role as a chaperone or in maintaining the latency of the enzymatic activity, the propeptide is required for proper transport and expression of newly synthesized cathepsin C.
    MeSH term(s) Amino Acid Sequence/genetics ; Animals ; COS Cells ; Cathepsin C/biosynthesis ; Cathepsin C/genetics ; Eukaryotic Cells/enzymology ; Glycosylation ; Lysosomes/enzymology ; Peptides/genetics ; Peptides/metabolism ; Point Mutation/genetics ; Protein Subunits/genetics ; Protein Subunits/metabolism ; Protein Transport/genetics ; Rats ; Tryptophan/metabolism
    Chemical Substances Peptides ; Protein Subunits ; Tryptophan (8DUH1N11BX) ; Cathepsin C (EC 3.4.14.1)
    Language English
    Publishing date 2002-12
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 391967-5
    ISSN 1618-1298 ; 0171-9335 ; 0070-2463
    ISSN (online) 1618-1298
    ISSN 0171-9335 ; 0070-2463
    DOI 10.1078/0171-9335-00291
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 667: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  2. Article: Caveolin-1 polarization in transmigrating endothelial cells requires binding to intermediate filaments.

    Santilman, Virginie / Baran, JoAnne / Anand-Apte, Bela / Evans, Robert M / Parat, Marie-Odile

    Angiogenesis

    2007  Volume 10, Issue 4, Page(s) 297–305

    Abstract: Caveolin-1 influences cell migration through multiple signaling pathways. In a previous report, we have shown that caveolin-1 is polarized in three-dimensional migrating endothelial cells (EC), and that caveolin-1 accumulation at the front of ... ...

    Abstract Caveolin-1 influences cell migration through multiple signaling pathways. In a previous report, we have shown that caveolin-1 is polarized in three-dimensional migrating endothelial cells (EC), and that caveolin-1 accumulation at the front of transmigrating cells requires the phosphorylatable Tyr(14) residue of caveolin-1. Immuno-electron microscopy further indicated that caveolin-1 was distributed along cytoskeletal structures in the anterior of transmigrating EC [Parat MO, Anand-Apte B, Fox PL (Mol Biol Cell 14:3156-3168, 2003)]. In the present study, we investigate whether caveolin-1 interacts with intermediate filaments (IF) and whether this interaction is required for caveolin-1 polarization in transmigrating cells. The distribution of vimentin is polarized in cells traversing a filter pore and overlaps with the distribution of caveolin-1, which accumulates in the cell front. In vivo sprouting EC also exhibit an anterior polarization of these two proteins. Furthermore, caveolin-1 co-purifies with intermediate filaments, suggesting an interaction between caveolin-1 and IF. Vimentin-deficient SW13 cells exhibit a dramatically altered polarization of caveolin-1-GFP, which no longer accumulates in the protruding cell extension. In addition, the Tyr(14) residue of caveolin-1 is required for co-purification of the protein with IF. Taken together, our results show that caveolin-1 Tyr(14) is necessary for binding to intermediate filaments, which in turn is required for anterior polarization of caveolin-1 in transmigrating cells.
    MeSH term(s) Animals ; Cattle ; Caveolin 1/physiology ; Cell Movement ; Cell Polarity ; Cells, Cultured ; Endothelium, Vascular/cytology ; Intermediate Filaments/physiology ; Vimentin/physiology
    Chemical Substances Caveolin 1 ; Vimentin
    Language English
    Publishing date 2007-10-23
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1484717-6
    ISSN 0969-6970
    ISSN 0969-6970
    DOI 10.1007/s10456-007-9083-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5094: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (2.OG)
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  3. Article: Caveolin-1 polarization in migrating endothelial cells is directed by substrate topology not chemoattractant gradient.

    Santilman, Virginie / Baran, JoAnne / Anand-Apte, Bela / Fox, Paul L / Parat, Marie-Odile

    Cell motility and the cytoskeleton

    2006  Volume 63, Issue 11, Page(s) 673–680

    Abstract: Polarization is a hallmark of migrating cells, and an asymmetric distribution of proteins is essential to the migration process. Caveolin-1 is highly polarized in migrating endothelial cells (EC). Several studies have shown caveolin-1 accumulation in the ...

    Abstract Polarization is a hallmark of migrating cells, and an asymmetric distribution of proteins is essential to the migration process. Caveolin-1 is highly polarized in migrating endothelial cells (EC). Several studies have shown caveolin-1 accumulation in the front of migrating EC while others report its accumulation in the EC rear. In this paper we address these conflicting results on polarized localization of caveolin-1. We find evidence for the hypothesis that different modes of locomotion lead to differences in protein polarization. In particular, we show that caveolin-1 is primarily localized in the rear of cells migrating on a planar substrate, but in the front of cells traversing a three-dimensional pore. We also show that a chemoattractant, present either as a gradient or ubiquitously in the medium, does not alter caveolin-1 localization in cells in either mode of locomotion. Thus we conclude that substrate topology, and not the presence of a chemoattractant, directs the polarization of caveolin-1 in motile ECs.
    MeSH term(s) Animals ; Aorta/physiology ; Cattle ; Caveolin 1/physiology ; Cell Movement/physiology ; Cell Polarity/physiology ; Chemotaxis/physiology ; Endothelial Cells/physiology ; Humans ; Vascular Endothelial Growth Factors/physiology
    Chemical Substances CAV1 protein, human ; Caveolin 1 ; Vascular Endothelial Growth Factors
    Language English
    Publishing date 2006-11
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 283774-2
    ISSN 1097-0169 ; 0886-1544
    ISSN (online) 1097-0169
    ISSN 0886-1544
    DOI 10.1002/cm.20153
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1840: Show issues Location:
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