FEBS Open Bio, 2021 Disruption of the mannose 6‐phosphate (M‐6‐P) pathway in HeLa cells by inactivation of the GNPTAB gene, which encodes the α/β subunits of GlcNAc‐1‐phosphotransferase, results in missorting of newly synthesized lysosomal acid hydrolases to the cell ...
Lin Liu, Balraj Doray
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Cathepsin D expression levels in nongynecological solid tumors: Clinical and therapeutic implications [PDF]
, 2004 Cathepsin D is a lysosomal acid proteinase which is involved in the malignant progression of breast cancer and other gynecological tumors. Clinical investigations have shown that in breast cancer patients cathepsin D overexpression was significantly ...
Crescimanno, M. +4 more
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Status and future directions of anti-metastatic cancer nanomedicines for the inhibition of cathepsin L [PDF]
, 2020 Angiogenesis, tissue invasion and metastasis in the tumour microenvironment are all critical hallmarks of cancer. Upregulation of cathepsin L plays an important role in angiogenesis and metastasis through its ability to degrade the extracellular matrix ...
Pranjol, Md Zahidul I +3 more
core +2 more sources
A cardinal role for cathepsin d in co-ordinating the host-mediated apoptosis of macrophages and killing of pneumococci. [PDF]
PLoS Pathogens, 2011 The bactericidal function of macrophages against pneumococci is enhanced by their apoptotic demise, which is controlled by the anti-apoptotic protein Mcl-1.
Martin A Bewley +9 more
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Epoxysuccinyl peptide-derived cathepsin B inhibitors: Modulating membrane permeability by conjugation with the C-terminal heptapeptide segment of penetratin [PDF]
, 2002 Besides its physiological role in lysosomal protein breakdown, extralysosomal cathepsin B has recently been implicated in apoptotic cell death. Highly specific irreversible cathepsin B inhibitors that are readily cellpermeant should be useful tools to ...
Assfalg-Machleidt, Irmgard +5 more
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Family C1 cysteine proteases: Biological diversity or redundancy? [PDF]
, 2003 Recent progress in the identification and partial characterization of novel genes encoding cysteine proteases of the papain family has considerably increased our knowledge of this family of enzymes.
Brömme D. +4 more
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Fluorogenic Substrates for Cathepsin D [PDF]
Bioscience, Biotechnology, and Biochemistry, 1999 Fluorogenic substrates for cathepsin D; A-Tyr-Phe(NO2)-Leu-Leu (A; Ala-Arg-Pro-Lys-Pro-Leu-Leu-, Arg-Pro-Lys-Pro-Leu-Leu-, Pro-Lys-Pro-Leu-Leu-, Lys-Pro-Leu-Leu-, Pro-Leu-Leu-) and B-Phe(NO2)-Tyr-Leu-Leu (B; Arg-Pro-Lys-Pro-Leu-Leu-, Pro-Lys-Pro-Leu-Leu-, Lys-Pro-Leu-Leu-, Pro-Leu-Leu-) (Phe(NO2), p-nitrophenylalanine) were synthesized and digested by ...
H, Yonezawa +3 more
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Peptide synthesis by recombinant Fasciola hepatica cathepsin L1 [PDF]
, 2006 Synthesis of the tripeptide Z-Phe-Arg-SerNH2 has been accomplished by a recombinant cysteine protease, cathepsin L1 from liver fluke (Fasciola hepatica), using Z-Phe-Arg-OMe as acyl acceptor and SerNH2 as nucleophile in 0.1 M ammonium acetate pH 9.0–12.5%
Ciarán Ó'Fágáin +16 more
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Cathepsin D Expression in Colorectal Adenocarcinomas and Adenomas
The International Journal of Biological Markers, 2002 The aim of this study was to investigate the role of cathepsin D in colorectal cancer. For this purpose cathepsin D expression was evaluated by means of immunohistochemistry in stromal and tumor cells of 31 colorectal carcinomas and 29 adenomas ...
Y. Kanber +3 more
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DmCatD, a cathepsin D-like peptidase of the hematophagous insect Dipetalogaster maxima (Hemiptera: Reduviidae): Purification, bioinformatic analyses and the significance of its interaction with lipophorin in the internalization by developing oocytes [PDF]
, 2018 DmCatD, a cathepsin D-like peptidase of the hematophagous insect Dipetalogaster maxima, is synthesized by the fat body and the ovary and functions as yolk protein precursor. Functionally, DmCatD is involved in vitellin proteolysis.
Arrese, Estela L. +8 more
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