Dipeptidyl-aminopeptidases and aminopeptidases in Dictyostelium discoideum

Chan, Samuel A.T.; Toursarkissian, Karim; Sweeney, John P.; Jones, Theodore H.D.

doi:10.1016/s0006-291x(85)80038-3

Cited by 20 publications

(11 citation statements)

References 8 publications

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“…For the CatC substrate, no non-specific conversion was observed. This result follows data by [51], who have shown that cathepsin C substrate is very specifically converted by dipeptidylaminopeptidase I (CatC).…”

Section: Resultssupporting

confidence: 91%

Effects of Five Substances with Different Modes of Action on Cathepsin H, C and L Activities in Zebrafish Embryos

Küster

Kalkhof

Aulhorn

et al. 2019

IJERPH

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Cathepsins have been proposed as biomarkers of chemical exposure in the zebrafish embryo model but it is unclear whether they can also be used to detect sublethal stress. The present study evaluates three cathepsin types as candidate biomarkers in zebrafish embryos. In addition to other functions, cathepsins are also involved in yolk lysosomal processes for the internal nutrition of embryos of oviparous animals until external feeding starts. The baseline enzyme activity of cathepsin types H, C and L during the embryonic development of zebrafish in the first 96 h post fertilisation was studied. Secondly, the effect of leupeptin, a known cathepsin inhibitor, and four embryotoxic xenobiotic compounds with different modes of action (phenanthrene—baseline toxicity; rotenone—an inhibitor of electron transport chain in mitochondria; DNOC (Dinitro-ortho-cresol)—an inhibitor of ATP synthesis; and tebuconazole—a sterol biosynthesis inhibitor) on in vivo cathepsin H, C and L total activities have been tested. The positive control leupeptin showed effects on cathepsin L at a 20-fold lower concentration compared to the respective LC50 (0.4 mM) of the zebrafish embryo assay (FET). The observed effects on the enzyme activity of the four other xenobiotics were not or just slightly more sensitive (factor of 1.5 to 3), but the differences did not reach statistical significance. Results of this study indicate that the analysed cathepsins are not susceptible to toxins other than the known peptide-like inhibitors. However, specific cathepsin inhibitors might be identified using the zebrafish embryo.

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Section: Resultssupporting

confidence: 91%

Effects of Five Substances with Different Modes of Action on Cathepsin H, C and L Activities in Zebrafish Embryos

Küster

Kalkhof

Aulhorn

et al. 2019

IJERPH

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“…The PsaA RNA and protein expression profiles are in agreement with a role for PsaA in growing cells and during late development, when spore cells are undergoing terminal differentiation, as the levels of PsaA are the highest at those points. Several developmentally regulated aminopeptidases have been shown to exist in D. discoideum (8,13,36). However, PsaA is the first whose function has been characterized to any extent (7).…”

Section: Discussionmentioning

confidence: 99%

Bestatin Inhibits Cell Growth, Cell Division, and Spore Cell Differentiation in Dictyostelium discoideum

2012

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ABSTRACTBestatin methyl ester (BME) is an inhibitor of Zn2+-binding aminopeptidases that inhibits cell proliferation and induces apoptosis in normal and cancer cells. We have usedDictyosteliumas a model organism to study the effects of BME. Only two Zn2+-binding aminopeptidases have been identified inDictyosteliumto date, puromycin-sensitive aminopeptidase A and B (PsaA and PsaB). PSA from other organisms is known to regulate cell division and differentiation. Here we show that PsaA is differentially expressed throughout growth and development ofDictyostelium, and its expression is regulated by developmental morphogens. We present evidence that BME specifically interacts with PsaA and inhibits its aminopeptidase activity. Treatment of cells with BME inhibited the rate of cell growth and the frequency of cell division in growing cells and inhibited spore cell differentiation during late development. Overexpression of PsaA-GFP (where GFP is green fluorescent protein) also inhibited spore cell differentiation but did not affect growth. Using chimeras, we have identified that nuclear versus cytoplasmic localization of PsaA affects the choice between stalk or spore cell differentiation pathway. Cells that overexpressed PsaA-GFP (primarily nuclear) differentiated into stalk cells, while cells that overexpressed PsaAΔNLS2-GFP (cytoplasmic) differentiated into spores. In conclusion, we have identified that BME inhibits cell growth, division, and differentiation inDictyosteliumlikely through inhibition of PsaA.

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“…Subsequently, its homologues were identified from a variety of prokaryotic and eukaryotic species. It has been described in human erythrocytes [19,40], neutrophils [23], monocytes and lymphocytes [41], placenta [42,43] and retroplacental serum [42], seminal plasma [44], muscle [45], skin [46], cerebrospinal fluid [24], eye lens extracts [47,48], neuroblastoma cells (IMR 32 cells) [16]; rat liver [49], skin [46], brain [18,50], erythrocytes [51], cataractous lens [22], spinal cord dorsal horn [27]; mouse cataract [52], rabbit erythrocytes [53], brain of monkey, guinea pig and goat [20,38,54]; porcine skeletal muscle and spleen [39,55], bovine epididymis and eye lens extracts [48,56], mouse ES cells [57], golden‐mantled ground squirrel [58], Echis coloratus venom [59], Drosophila melanogaster [60], Blaberus craniifer [61], Dictyostelium discoideum [62], S. cerevisiae [63], extracts of adult Schistosomes [64], Leishmania major [60] and Entamoeba histolytica [65].…”

Section: Dpp III a Ubiquitous Peptidasementioning

confidence: 99%

Dipeptidyl peptidase III: a multifaceted oligopeptide N‐end cutter

2011

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Dipeptidyl peptidase III (DPP III), the sole member and representative of the M49 family of metallopeptidases, is a zinc-dependent aminopeptidase. It sequentially hydrolyses dipeptides from the N-terminal of oligopeptides ranging from three to 10 amino acid residues. Although implicated in an array of pathophysiological phenomena, the precise function of this peptidase is still unclear. However, a number of studies advocate its contribution in terminal stages of protein turnover. Altered expression of DPP III which suggests its involvement in primary ovarian carcinoma, oxidative stress (Nrf2 nuclear localization), pain, inflammation and cataractogenesis has recently led to resurgence of interest in delineating the role of the peptidase in these pathophysiological processes. This review article intends to bring forth the latest updates in this arena which may serve as a base for future studies on the peptidase.

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Dipeptidyl-aminopeptidases and aminopeptidases in Dictyostelium discoideum

Cited by 20 publications

References 8 publications

Effects of Five Substances with Different Modes of Action on Cathepsin H, C and L Activities in Zebrafish Embryos

Effects of Five Substances with Different Modes of Action on Cathepsin H, C and L Activities in Zebrafish Embryos

Bestatin Inhibits Cell Growth, Cell Division, and Spore Cell Differentiation in Dictyostelium discoideum

Dipeptidyl peptidase III: a multifaceted oligopeptide N‐end cutter

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