scholarly journals Prime region subsite specificity characterization of human cathepsin D: The dominant role of position 128

1998 ◽  
Vol 7 (1) ◽  
pp. 88-95 ◽  
Author(s):  
Brian M. Beyer ◽  
Ben M. Dunn
Keyword(s):  
Cathepsin D ◽  
Dominant Role ◽  
Human Cathepsin

Alterations and Role of Human Cathepsin D in Cancer Metastasis

1996 ◽  
Vol 49 (1-3) ◽  
pp. 106-116 ◽  
Author(s):  
Henri Rochefort ◽  
Emmanuelle Liaudet ◽  
Marcel Garcia
Keyword(s):  
Cathepsin D ◽  
Cancer Metastasis ◽  
Human Cathepsin

scholarly journals Production, Characterization, and Epitope Mapping of a Monoclonal Antibody against Aspartic Proteinase ofCandida albicans

1999 ◽  
Vol 6 (3) ◽  
pp. 429-433 ◽  
Author(s):  
Byoung-Kuk Na ◽  
Gyung-Tae Chung ◽  
Chul-Yong Song
Keyword(s):  
Monoclonal Antibody ◽  
Candida Albicans ◽  
Candida Tropicalis ◽  
Cathepsin D ◽  
Epitope Mapping ◽  
Candida Parapsilosis ◽  
Aspartic Proteinase ◽  
Ofcandida Albicans ◽  
Human Cathepsin

ABSTRACT A monoclonal antibody (MAb; MAb CAP1) that was reactive with extracellular aspartic proteinase of Candida albicans (CAP) was produced. The MAb showed strong sensitivity and reactivity to CAP but not to the aspartic proteinases of Candida parapsilosis, Candida tropicalis, andAspergillus fumigatus or to human cathepsin D or porcine pepsin. The epitope of the CAP recognized by the MAb was the proteinaseous part of CAP and the putative epitope of the MAb was located in the Asp77 to Gly103 sequence. This antibody could be useful for the characterization of CAP and would be a valuable probe for the detection of CAP antigen in the sera of patients with invasive candidiasis.

scholarly journals Characterization of the proximal estrogen-responsive element of human cathepsin D gene.

1994 ◽  
Vol 8 (6) ◽  
pp. 693-703 ◽  
Author(s):  
P Augereau ◽  
F Miralles ◽  
V Cavaillès ◽  
C Gaudelet ◽  
M Parker ◽  
...  
Keyword(s):  
Cathepsin D ◽  
Estrogen Responsive Element ◽  
Human Cathepsin ◽  
Responsive Element

scholarly journals Structural Basis of Subtilase Cytotoxin SubAB Assembly

2013 ◽  
Vol 288 (38) ◽  
pp. 27505-27516 ◽  
Author(s):  
Jérôme Le Nours ◽  
Adrienne W. Paton ◽  
Emma Byres ◽  
Sally Troy ◽  
Brock P. Herdman ◽  
...  
Keyword(s):  
Dominant Role ◽  
Functional Characterization ◽  
Structural Basis ◽  
Sequence Comparisons ◽  
A Subunit ◽  
The Individual ◽  
A1 Domain ◽  
Cellular Dysfunction

Pathogenic strains of Escherichia coli produce a number of toxins that belong to the AB5 toxin family, which comprise a catalytic A-subunit that induces cellular dysfunction and a B-pentamer that recognizes host glycans. Although the molecular actions of many of the individual subunits of AB5 toxins are well understood, how they self-associate and the effect of this association on cytotoxicity are poorly understood. Here we have solved the structure of the holo-SubAB toxin that, in contrast to other AB5 toxins whose molecular targets are located in the cytosol, cleaves the endoplasmic reticulum chaperone BiP. SubA interacts with SubB in a similar manner to other AB5 toxins via the A2 helix and a conserved disulfide bond that joins the A1 domain with the A2 helix. The structure revealed that the active site of SubA is not occluded by the B-pentamer, and the B-pentamer does not enhance or inhibit the activity of SubA. Structure-based sequence comparisons with other AB5 toxin family members, combined with extensive mutagenesis studies on SubB, show how the hydrophobic patch on top of the B-pentamer plays a dominant role in binding the A-subunit. The structure of SubAB and the accompanying functional characterization of various mutants of SubAB provide a framework for understanding the important role of the B-pentamer in the assembly and the intracellular trafficking of this AB5 toxin.

Potassium Transport in the Mammalian Collecting Duct

2001 ◽  
Vol 81 (1) ◽  
pp. 85-116 ◽  
Author(s):  
Shigeaki Muto
Keyword(s):  
Driving Forces ◽  
Collecting Duct ◽  
Dominant Role ◽  
Duct Cell ◽  
Cell Types ◽  
Cortical Collecting Duct ◽  
Membrane Conductances ◽  
Collecting Duct Cells

The mammalian collecting duct plays a dominant role in regulating K+ excretion by the nephron. The collecting duct exhibits axial and intrasegmental cell heterogeneity and is composed of at least two cell types: collecting duct cells (principal cells) and intercalated cells. Under normal circumstances, the collecting duct cell in the cortical collecting duct secretes K+, whereas under K+ depletion, the intercalated cell reabsorbs K+. Assessment of the electrochemical driving forces and of membrane conductances for transcellular and paracellular electrolyte movement, the characterization of several ATPases, patch-clamp investigation, and cloning of the K+ channel have provided important insights into the role of pumps and channels in those tubule cells that regulate K+ secretion and reabsorption. This review summarizes K+ transport properties in the mammalian collecting duct. Special emphasis is given to the mechanisms of how K+ transport is regulated in the collecting duct.

scholarly journals Interaction of human cathepsin D with the inhibitor pepstatin

1976 ◽  
Vol 155 (1) ◽  
pp. 117-125 ◽  
Author(s):  
C G Knight ◽  
A J Barrett
Keyword(s):  
Cathepsin D ◽  
Specific Activity ◽  
Dissociation Constants ◽  
Equilibrium Dialysis ◽  
Tight Binding ◽  
Extinction Coefficients ◽  
Titration Curves ◽  
Human Cathepsin

1. Because of the proposed role of cathepsin D in a variety of biological and pathological processes, the characteristics of inhibition by the potentially useful agent, pepstatin, were determined. 2. The β and γ forms of human cathepsin D, separated by isoelectric focusing, have identical specific extinction coefficients and specific activity in the degradation of haemoglobin. 3. Cathepsin D showed tight binding of 1 mol of pepstatin per 43000 g of protein, indicating that titration with the inhibitor represents a useful method for determination of absolute concentrations of the enzyme. 4. The titration curves were used to determine apparent dissociation constants (KD) for the binding of pepstatin and pepstatin methyl ester at pH3.5; values of approx. 5 } 10(-10)M were obtained. 5. Pepstatinyl-[3H]glycine was synthesized and shown to have a KD similar to that of pepstatin. Gel-chromatographic experiments showed that the binding of pepstatin and its derivatives is strongly pH-dependent. 6. The effect of pH on the KD for pepstatinyl-glycine was determined by equilibrium dialysis. As the pH was raised from 5.0 to 6.4, KD rose from 5 } 10(-10)M to 2 } 10(-6)M. 7. The catalytic activity of cathepsin D declines essentially to zero on going from pH5.0 to pH7.0, and we suggest that the binding site for substrate and pepstatin is abolished by a conformational change in the enzyme molecule. 8. The data indicate that, in biological experiments near neutral pH, large molar excesses of pepstatin over cathepsin D will be required for efficient inhibition.

Characterization of Dictyostelium discoideum cathepsin D

1999 ◽  
Vol 112 (21) ◽  
pp. 3833-3843 ◽  
Author(s):  
A. Journet ◽  
A. Chapel ◽  
S. Jehan ◽  
C. Adessi ◽  
H. Freeze ◽  
...  
Keyword(s):  
Dictyostelium Discoideum ◽  
Cathepsin D ◽  
Developmental Regulation ◽  
Endocytic Pathway ◽  
Common Antigen ◽  
Sds Page ◽  
Differentiation Stage ◽  
Endocytic Vesicles

Previous studies using magnetic purification of Dictyostelium discoideum endocytic vesicles led us to the identification of some major vesicle proteins. Using the same purification procedure, we have now focused our interest on a 44 kDa soluble vesicle protein. Microsequencing of internal peptides and subsequent cloning of the corresponding cDNA identified this protein as the Dictyostelium homolog of mammalian cathepsins D. The only glycosylation detected on Dictyostelium cathepsin D (CatD) is common antigen 1, a cluster of mannose 6-sulfate residues on N-linked oligosaccharide chains. CatD intracellular trafficking has been studied, showing the presence of the protein throughout the entire endocytic pathway. During the differentiation process, the catD gene presents a developmental regulation, which is also observed at the protein level. catD gene disruption does not alter significantly the cell behaviour, either in the vegetative form or the differentiation stage. However, modifications in the SDS-PAGE profiles of proteins bearing common antigen 1 were detected, when comparing parental and catD(-) cells. These modifications point to a possible role of CatD in the maturation of a few Dictyostelium lysosomal proteins.

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