Localization of the Endogenous Cysteine Proteinase Inhibitor, Cystatin C, and the Cysteine Proteinase, Cathepsin B, to the Junctional Epithelium in Rat Gingiva

2005 ◽  
Vol 38 (2) ◽  
pp. 121-129 ◽  
Author(s):  
Takayoshi Yamaza ◽  
Satoya Mino ◽  
Ikiru Atsuta ◽  
Atsushi Danjo ◽  
Tadayoshi Kagiya ◽  
...  
Keyword(s):  
Cystatin C ◽  
Cathepsin B ◽  
Proteinase Inhibitor ◽  
Cysteine Proteinase ◽  
Cysteine Proteinase Inhibitor ◽  
Junctional Epithelium

scholarly journals Expression of Cysteine Proteinases Cathepsins B and K and of Cysteine Proteinase Inhibitor Cystatin C in Giant Cell Tumor of Tendon Sheath

2001 ◽  
Vol 14 (4) ◽  
pp. 318-324 ◽  
Author(s):  
Torsten Hansen ◽  
Peter K Petrow ◽  
Andreas Gaumann ◽  
Gernot M Keyszer ◽  
Mike Otto ◽  
...  
Keyword(s):  
Giant Cell Tumor ◽  
Giant Cell ◽  
Cystatin C ◽  
Proteinase Inhibitor ◽  
Cysteine Proteinase ◽  
Tendon Sheath ◽  
Cell Tumor ◽  
Cysteine Proteinase Inhibitor ◽  
Cysteine Proteinases

Production of the cysteine proteinase inhibitor cystatin C by rat Sertoli cells

FEBS Letters ◽  
1992 ◽  
Vol 300 (2) ◽  
pp. 131-135 ◽  
Author(s):  
Annick Esnard ◽  
Frédéric Esnard ◽  
Florian Guillou ◽  
Francis Gauthierxaa
Keyword(s):  
Cystatin C ◽  
Sertoli Cells ◽  
Proteinase Inhibitor ◽  
Cysteine Proteinase ◽  
Cysteine Proteinase Inhibitor

scholarly journals Structure and expression of the human cystatin C gene

1990 ◽  
Vol 268 (2) ◽  
pp. 287-294 ◽  
Author(s):  
M Abrahamson ◽  
I Olafsson ◽  
A Palsdottir ◽  
M Ulvsbäck ◽  
Å Lundwall ◽  
...  
Keyword(s):  
Cystatin C ◽  
Proteinase Inhibitor ◽  
Genomic Dna ◽  
Cysteine Proteinase ◽  
Housekeeping Genes ◽  
Genomic Region ◽  
Cysteine Proteinase Inhibitor ◽  
Specific Expression ◽  
Human Cystatin C ◽  
Human Cystatin

The structural organization of the gene for the human cysteine-proteinase inhibitor cystatin C was studied. Restriction-endonuclease digests of human genomic DNA hybridized with human cystatin C cDNA and genomic probes produced patterns consistent with a single cystatin C gene and, also, the presence of six closely related sequences in the human genome. A 30 kb restriction map covering the genomic region of the cystatin C gene was constructed. The positions of three polymorphic restriction sites, found at examination of digests of genomic DNA from 79 subjects, were localized in the flanking regions of the gene. The gene was cloned and the nucleotide sequence of a 7.3 kb genomic segment was determined, containing the three exons of the cystatin C structural gene as well as 1.0 kb of 5′-flanking and 2.0 kb of 3′-flanking sequences. Northern-blot experiments revealed that the cystatin C gene is expressed in every human tissue examined, including kidney, liver, pancreas, intestine, stomach, antrum, lung and placenta. The highest cystatin C expression was seen in seminal vesicles. The apparently non-tissue-specific expression of this cysteine-proteinase inhibitor gene is discussed with respect to the structure of its 5′-flanking region, which shares several features with those of housekeeping genes.

Effect of Cysteine Proteinase Inhibitors on Murine B16 Melanoma Cell Invasion in vitro

2002 ◽  
Vol 383 (5) ◽  
pp. 839-842 ◽  
Author(s):  
Natasa Sever ◽  
Metka Filipic ◽  
Joze Brzin ◽  
Tamara T. Lah
Keyword(s):  
Cell Invasion ◽  
Cathepsin B ◽  
Proteinase Inhibitor ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Cathepsin L ◽  
Cysteine Proteinase Inhibitor ◽  
Cysteine Proteinases ◽  
Cysteine Proteinase Inhibitors

Abstract Various types of proteinases are implicated in the malignant progression of human and animal tumors. Proteinase inhibitors may therefore be useful as therapeutic agents in antiinvasive and antimetastatic treatment. The aims of this study were (1) to estimate the relative importance of proteinases in B16 cell invasion in vitro using synthetic, classspecific proteinase inhibitors and (2) to assess the inhibitory effect of some naturally occurring cysteine proteinase inhibitors. Serine proteinase inhibitor reduced invasiveness by up to 24%, whereas inhibition of aspartic proteinases reduced invasion by 11%. Synthetic inhibitors of cysteine proteinases markedly impaired invasion: cathepsin B inhibitors, particularly Ca 074Me, inhibited invasion from 20 40%, whereas cathepsin L inhibitor Clik 148 reduced invasion by 11%. The potato cysteine proteinase inhibitor PCPI 8.7 inhibited invasion by 21%, whereas another potato inhibitor, PCPI 6.6, and the mushroom cysteine proteinase inhibitor clitocypin had no effects. As the inhibitors that inhibited cathepsin B were in general more efficient at impairing the invasiveness, we conclude that of the two cysteine proteinases, cathepsin B plays a more important role than cathepsin L in murine melanoma cell invasion.

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