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The primary structure and tissue distribution of cathepsin C.
TLDR
A cDNA for rat cathepsin C (dipeptidylaminopeptidase I) was isolated and belongs to papain family, although its propeptide region is much longer than those of other cysteine proteinases and show no significant sequence similarity to any other cySteine proteinase. Expand
Specific storage of subunit c of mitochondrial ATP synthase in lysosomes of neuronal ceroid lipofuscinosis (Batten's disease).
TLDR
Results indicate a specific accumulation of sub unit c in lysosomes, and suggest that the two forms of Batten's disease are caused by a specific failure in the degradation of subunit c. Expand
Membrane markers of endoplasmic reticulum preserved in autophagic vacuolar membranes isolated from leupeptin-administered rat liver.
TLDR
The prominent markers of endoplasmic reticulum from which autophagosomes originate are well preserved in autophagic vacuole membranes, and retention of these markers is highly dependent on the formation and subsequent maturation process of autophotic vacuoles. Expand
Cathepsin L activity is increased in alveolar macrophages and bronchoalveolar lavage fluid of smokers.
TLDR
The data suggest that cigarette smoking induces mRNA expression and the synthesis of cathepsin L in AM and the release of procat hepsin from AM into extracellular milieu, which may contribute to the proteolysis of elastin in the process of lung destruction associated with cigarette smoking. Expand
The selective role of cathepsins B and D in the lysosomal degradation of endogenous and exogenous proteins
TLDR
A small contribution of cathepsins B and D to the initiation of lysosomal proteolysis is suggested, as well as the inhibition of endocytosed FITC‐labeled asialofetuin. Expand
Molecular cloning of cDNA for rat cathepsin C. Cathepsin C, a cysteine proteinase with an extremely long propeptide.
TLDR
A cDNA for rat cathepsin C (dipeptidylaminopeptidase I) was isolated and four potential glycosylation sites were found, three located in the propeptide region, and one in the mature enzyme region, making it a member of the papain family. Expand
Both cathepsin B and cathepsin D are necessary for processing of ovalbumin as well as for degradation of class II MHC invariant chain.
TLDR
Two main conclusions are drawn, not only aspartyl protease, such as cathepsin D, but also thiol protease is involved in antigen processing by APC and both cat hepsin B and cathePSin D are necessary for degradation of the invariant chain from the MHC class II alpha beta heterodimer in endosomes in order to express functional MHCclass II molecules for binding antigenic peptides. Expand
Processing and transport of the precursor of cathepsin C during its transfer into lysosomes.
TLDR
The biosynthesis and processing of a lysosomal cysteine proteinase, cathepsin C (dipeptidylaminopeptidase I), was investigated by pulse-chase experiments in cultured rat macrophages and revealed that the precursor product exists as an oligomeric form. Expand
Effect of metabolic alterations on the density and the contents of cathepsins B, H and L of lysosomes in rat macrophages.
TLDR
The level of pyruvate kinase, an autophagic sequestration marker in heavy autolysosomes from E-64-d-treated cells, was much higher in serum-deprived cells, indicating that the contribution of heterophotic sequestration towards an increase in the density of lysosomes is much greater than that of autophagy. Expand
Amino acid sequence of iron‐superoxide dismutase from Pseudomonas ovalis
The amino acid sequence of iron‐superoxide dismutase from Pseudomonas ovalis was deduced by the analyses of peptides derived from limited hydrolysis of the aminoethylated or pyridylethylatedExpand
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