Cell and Tissue Distribution of Lysosomal Cysteine Proteinases, Cathepsins B, H, and L, and their Biological Roles.

Uchiyama, Yasuo; Waguri, Satoshi; Satô, Noboru; Watanabe, Tsuyoshi; Ishido, Kazumi; Kominami, Eiki

doi:10.1267/ahc.27.287

Cited by 41 publications

(27 citation statements)

References 104 publications

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“…Although the discrepancy between these two results has not been explained, Dittmer et al (1997) have suggested that other parameters, including the structure of the underlying oligosaccharides, the position of the phosphorylated mannose residues within the oligosaccharides, and the polypeptide backbone, would determine the affinity of the enzyme for the two MPRs. When we consider these notions, our present results could indicate that the difference in affinity of the two MPRs for each lysosomal enzyme contributes to the different distribution patterns of the MPRs, because lysosomal enzymes also show heterogeneous distribution patterns depending on enzymes, cells, and tissues (Uchiyama et al 1994). However, more information concerning differences in the oligosaccharide modification and the phosphorylation state of lysosomal enzymes for several types of cells and tissues will be needed.…”

Section: Discussionmentioning

confidence: 86%

Different Distribution Patterns of the Two Mannose 6-phosphate Receptors in Rat Liver

Waguri

Kohmura

Kanamori

et al. 2001

J Histochem Cytochem.

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Two mannose 6-phosphate receptors, cation-dependent and -independent receptors (CDMPR and CIMPR), play an important role in the intracellular transport of lysosomal enzymes. To investigate functional differences between the two in vivo, their distribution was examined in the rat liver using immunohistochemical techniques. Positive signals corresponding to CIMPR were detected intensely in hepatocytes and weakly in sinusoidal Kupffer cells and interstitial cells in Glisson's capsule. In the liver acinus, hepatocytes in the perivenous region showed a more intense immunoreactivity than those in the periportal region. On the other hand, positive staining of CDMPR was detected at a high level in Kupffer cells, epithelial cells of interlobular bile ducts, and fibroblast-like cells, but the corresponding signal was rather weak in hepatocytes. In situ hybridization analysis also revealed a high level of expression of CIMPR mRNAs in hepatocytes and of CDMPR mRNA in Kupffer cells. By double immunostaining, OX6-positive antigen-presenting cells in Glisson's capsule were co-labeled with the CDMPR signal but were only faintly stained with anti-CIMPR. These different distribution patterns of the two MPRs suggest distinct functional properties of each receptor in liver tissue.

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Section: Discussionmentioning

confidence: 86%

Different Distribution Patterns of the Two Mannose 6-phosphate Receptors in Rat Liver

Waguri

Kohmura

Kanamori

et al. 2001

J Histochem Cytochem.

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“…This report strongly indicates a different role of Cath H from those of Cath B and Cath L. In fact, contrary to Cath H, the overexpression of Cath B and Cath L has been reported in lung tumours as well as in several other studies of aetiologically different cancers (reviewed by Kos et al, 1998). Although Cath B, L and H are all lysosomal cysteine peptidases, large variations in expression of individual cathepsins in different tissues (Qian et al, 1991) and even in different types of cells within the same tissue (Uchiyama et al, 1994) have been reported. Selective expression of individual peptidases in different types of tumour suggest that they may participate in specialized cellular functions (San Segundo et al, 1986;Chapman et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

Cysteine proteinase cathepsin H in tumours and sera of lung cancer patients: relation to prognosis and cigarette smoking

et al. 2000

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Summary In order to evaluate the role of cysteine peptidase cathepsin H (Cath H) in human lung cancer its protein levels were determined in 148 pairs of lung tumour tissue and adjacent non-tumourous lung parenchyma using the enzyme-linked immunosorbent assay technique. Additionally, Cath H levels were determined in sera of 171 patients with malignant tumours, 34 patients with benign lung diseases and 47 healthy controls. The median level of Cath H in tumour tissue was 0.64 times that in the corresponding lung parenchyma. Relating tumour levels with histological type we found higher Cath H levels in small-cell and adenocarcinomas and lower levels in squamous cell carcinoma, large-cell carcinoma and secondary tumours. A significant difference in Cath H level between lung tumour tissue and non-tumourous lung parenchyma was associated with the group of cigarette smokers (156 vs 263 ng mg -1 protein, P < 0.001). For this group of patients Cath H tumour levels correlated with the survival rate, while for the entire patient population this was not the case. Smokers with high tumour levels of Cath H experienced poor survival. Cath H was significantly higher in sera of patients with malignant and benign lung diseases than in control sera (P < 0.001). The increase was significant for all histological types, being the highest in small-cell and squamous cell carcinomas. Our study reveals that in lung tumours there is different behaviour of Cath H compared with other cysteine peptidases, e.g. cathepsin B and cathepsin L. Variations between tissue and serum levels of Cath H indicate either reduced expression or enhanced secretion of this enzyme in lung tumours.

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“…Lysosomes, as an acidic compartment with limiting membranes, are ubiquitous in all animal cells and play an important role in the maintenance of the cellular metabolic turnover by degrading unneeded intra-and extracellular materials into biological monomers which are then reutilized by the cells (UCHIYAMA et al, 1994). Cathepsins B and D are representative cysteine and aspartic proteinases in lysosomes of mammalian cells.…”

Section: Discussionmentioning

confidence: 99%

An Ultrastructural and Immunohistochemical Study of PC12 Cells During Apoptosis Induced by Serum Deprivation with Special Reference to Autophagy and Lysosomal Cathepsins.

Ohsawa

Isahara

Kanamori

et al. 1998

Archives of Histology and Cytology

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Cell and Tissue Distribution of Lysosomal Cysteine Proteinases, Cathepsins B, H, and L, and their Biological Roles.

Cited by 41 publications

References 104 publications

Different Distribution Patterns of the Two Mannose 6-phosphate Receptors in Rat Liver

Different Distribution Patterns of the Two Mannose 6-phosphate Receptors in Rat Liver

Cysteine proteinase cathepsin H in tumours and sera of lung cancer patients: relation to prognosis and cigarette smoking

An Ultrastructural and Immunohistochemical Study of PC12 Cells During Apoptosis Induced by Serum Deprivation with Special Reference to Autophagy and Lysosomal Cathepsins.

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