Synthesis and intracellular distribution of cathepsins E and D in differentiating murine friend erythroleukemia cells
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Cited by (15)
Cathepsin E: An Aspartic Protease with Diverse Functions and Biomedical Implications
2016, Encyclopedia of Cell BiologyCathepsin E is critical for proper trafficking of cell surface proteins
2012, Journal of Oral BiosciencesCitation Excerpt :In other cell types, including erythrocytes, renal proximal tubule cells and osteoclasts, this protein is exclusively confined to the plasma membrane mainly as a proenzyme having complex-type oligosaccharides [5,6]. In a variety of other cells, cathepsin E is also detected in the endoplasmic reticulum and Golgi complex [4,5,7]. Although cathepsin E has been implicated in various physiological and pathological processes [1,8,9], the precise role of this protein remains speculative, because physiological substrates have not yet been identified.
Emerging roles of cathepsin e in host defense mechanisms
2012, Biochimica et Biophysica Acta - Proteins and ProteomicsCitation Excerpt :The association of cathepsin E with plasma membrane is observed in erythrocytes [18,19], intracellular canaliculi of gastric parietal cells [14], renal proximal tubule cells [14], bile canaliculi of hepatic cells [14], intestinal and tracheobronchial epithelial cells [15,20] and osteoclasts [21]. Cathepsin E is also found in the endoplasmic reticulum and Golgi complex [3,14] and the cytosol [14,22] of various cell types. Besides its intracellular localization, cathepsin E is highly secreted as the catalytically active enzyme by activated phagocytes [3,23].
Gene expression profiling of mammary glands of cathepsin E-deficient mice compared with wild-type littermates
2008, BiochimieCitation Excerpt :In some types of cells, including erythrocytes, renal proximal tubule cells, and osteoclasts, cathepsin E is exclusively confined to the plasma membrane [23,24] mainly as a proenzyme having complex-type oligosaccharides. In a variety of other cell types, cathepsin E is also detected in the endoplasmic reticulumn and Golgi complex [10,23,25]. Cathepsin E has been implicated in various physiological and pathological processes (see for review refs. [26,27]), the precise role of this protein remains largely unknown, because the physiological substrates of this protein have not yet been identified.
Intracellular trafficking and degradation of unassociated proα2 chains of collagen type I
2004, Experimental Cell ResearchExpression and localization of ferritin mRNA in ameloblasts of rat incisor
1998, Archives of Oral Biology