Browsing by Subject "cathepsin"

Now showing items 1-9 of 9

    • Bauhinia Kunitz-type proteinase inhibitors: structural characteristics and biological properties 

      Oliva, Maria Luiza Vilela [UNIFESP]; Sampaio, Misako Uemura [UNIFESP] (Walter de Gruyter & Co, 2008-08-01)
      Plant proteinase inhibitors are involved in the regulation of the activity of many proteinases and, in consequence, in biological processes driven by proteolysis. in this review, we summarize recent results on the activity ...

    • Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase 

      Klemencic, I; Carmona, Adriana Karaoglanovic [UNIFESP]; Cezari, Maria Helena Sedenho [UNIFESP]; Juliano, Maria Aparecida [UNIFESP]; Juliano, Luiz [UNIFESP]; Guncar, G.; Turk, D.; Krizaj, I; Turk, V; Turk, B. (Wiley-Blackwell, 2000-09-01)
      Cathepsin X, purified to homogeneity from human liver, is a single chain glycoprotein with a molecular mass of approximate to 33 kDa and pI 5.1-5.3. Cathepsin X was inhibited by stefin A, cystatin C and chicken cystatin ...

    • Chemoenzymatic synthesis of organoselenium(IV) compounds and their evaluation as cysteine protease inhibitors 

      Piovan, Leandro; Alves, Marcio Fernando [UNIFESP]; Juliano, Luiz [UNIFESP]; Brömme, Dieter; Cunha, Rodrigo Luiz Oliveira Rodrigues [UNIFESP]; Andrade, Leandro H (Sociedade Brasileira de Química, 2010-01-01)
      A series of organoselenium dihalides (organoselenanes) was synthesized from organoselenides using a chemoenzymatic approach. The organoselenanes have variations in their stereochemistry and in the halogen atom bonded to ...

    • Crystal structure of a novel cysteinless plant Kunitz-type protease inhibitor 

      Hansen, Daiane; Macedo-Ribeiro, Sandra; Verissimo, Paula; Im, Sonia Yoo; Sampaio, Misako Uemura; Oliva, Maria Luiza Vilela (Elsevier B.V., 2007-09-07)
      Bauhinia bauhinioides Cruzipain Inhibitor (BbCI) is a cysteine protease inhibitor highly homologous to plant Kunitz-type inhibitors. However, in contrast to classical Kunitz family inhibitors it lacks cysteine residues and ...

    • Cysteine Cathepsins in Human Carious Dentin 

      Nascimento, F. D.; Minciotti, C. L.; Geraldeli, S.; Carrilho, M. R.; Pashley, D. H.; Tay, F. R.; Nader, H. B. [UNIFESP]; Salo, T.; Tjaderhane, L.; Tersariol, I. L. S. [UNIFESP] (Sage Publications Inc, 2011-04-01)
      Matrix metalloproteinases (MMPs) are important in dentinal caries, and analysis of recent data demonstrates the presence of other collagen-degrading enzymes, cysteine cathepsins, in human dentin. This study aimed to examine ...

    • Enzimas lisossomais em células renais em cultura submetidas a condições que mimetizam o estado diabético 

      Peres, Giovani Bravin [UNIFESP] (Universidade Federal de São Paulo (UNIFESP), 2016-08-31)
      Diabetic nephropathy affects about one third of ali diabetic patients, and is the most common cause of end-stage renal disease. By the use of intravital microscopy and fluorescent albumin, it has been shown that the renal ...

    • Inhibitory effect of the sugarcane cystatin CaneCPI-4 on cathepsins B and L and human breast cancer cell invasion 

      Gianotti, Andreia; Sommer, Csar A.; Carmona, Adriana K. [UNIFESP]; Henrique-Silva, Flavio (Walter de Gruyter & Co, 2008-04-01)
      The lysosomal cysteine proteases cathepsin B and L play important roles in tumor cell invasion. An imbalance between these cathepsins and their endogenous inhibitors, the cystatins, has been associated with development of ...

    • Probing cathepsin K activity with a selective substrate spanning its active site 

      Lecaille, Fabien; Weidauer, Enrico; Juliano, Maria Aparecida [UNIFESP]; Bromme, Dieter; Lalmanach, Gilles (Portland Press, 2003-10-15)
      The limited availability of highly selective cathepsin substrates seriously impairs studies designed to monitor individual cathepsin activities in biological samples. Among mammalian cysteine proteases, cathepsin K has a ...

    • Structure of cruzipain/cruzain inhibitors isolated from Bauhinia bauhinioides seeds 

      Oliveira, Cleide de [UNIFESP]; Santana, Lucimeire Aparecida de [UNIFESP]; Carmona, Adriana Karaoglanovic [UNIFESP]; Cezari, Maria Helena Sedenho [UNIFESP]; Sampaio, Misako Uemura [UNIFESP]; Sampaio, Claudio Augusto Machado [UNIFESP]; Oliva, Maria Luiza Vilela [UNIFESP] (Walter De Gruyter & Co, 2001-05-01)
      The saline extract of Bauhinia bauhinioides dry seeds was shown to inhibit cruzipain, a cysteine proteinase from Trypanosoma cruzi. The inhibitory activity was assigned to a protein with 164 amino acid residues and molecular ...