cathepsin-g has been researched along with pepstatin* in 2 studies
2 other study(ies) available for cathepsin-g and pepstatin
Article | Year |
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Regulation of cathepsin G reduces the activation of proinsulin-reactive T cells from type 1 diabetes patients.
Autoantigenic peptides resulting from self-proteins such as proinsulin are important players in the development of type 1 diabetes mellitus (T1D). Self-proteins can be processed by cathepsins (Cats) within endocytic compartments and loaded to major histocompatibility complex (MHC) class II molecules for CD4(+) T cell inspection. However, the processing and presentation of proinsulin by antigen-presenting cells (APC) in humans is only partially understood. Here we demonstrate that the processing of proinsulin by B cell or myeloid dendritic cell (mDC1)-derived lysosomal cathepsins resulted in several proinsulin-derived intermediates. These intermediates were similar to those obtained using purified CatG and, to a lesser extent, CatD, S, and V in vitro. Some of these intermediates polarized T cell activation in peripheral blood mononuclear cells (PBMC) from T1D patients indicative for naturally processed T cell epitopes. Furthermore, CatG activity was found to be elevated in PBMC from T1D patients and abrogation of CatG activity resulted in functional inhibition of proinsulin-reactive T cells. Our data suggested the notion that CatG plays a critical role in proinsulin processing and is important in the activation process of diabetogenic T cells. Topics: Blotting, Western; Carrier Proteins; Cathepsin G; Cell-Penetrating Peptides; Cells, Cultured; Diabetes Mellitus, Type 1; Enzyme-Linked Immunosorbent Assay; Humans; Leucine; Pepstatins; Polymerase Chain Reaction; Proinsulin; T-Lymphocytes | 2011 |
Angiotensin-producing enzyme I of serum: formation by immunization with renin.
Immunization with renin from the kidneys of hog, beef, dog, rabbit and man induced the formation of a highly active enzyme (enzyme I) in the serum of dogs, guinea pigs, rabbits and rats. Enzyme I produces angiotensin I maximally at pH 4.7, up to 2900 ng/ml serum/h, i.e. at a rate 2500 times higher than the endogenous renin of normal serum. At pH 7.2 the angiotensin I production by enzyme I is about 16 to 28 times higher than that of plasma renin. Enzyme I is produced by immunization with renin and not by other kidney proteins. Enzymatically-active renin is required and separate mechanisms are involved in the formation of enzyme I and antirenin. Enzyme I is not identical to renin, pepsin, cathepsin D, plasmin, tonin or cathepsin G and it is inhibited by pepstatin, but not by diisopropyl fluorophosphate. Topics: Animals; Antibodies; Carboxypeptidases; Cathepsin D; Cathepsin G; Cathepsins; Cattle; Dogs; Fibrinolysin; Guinea Pigs; Humans; Hydrogen-Ion Concentration; Immunization; Lysine Carboxypeptidase; Pepsin A; Pepstatins; Peptidyl-Dipeptidase A; Rabbits; Rats; Renin; Serine Endopeptidases; Substrate Specificity; Swine | 1984 |