Down-regulation of proteolytic complexes following EBV activation in BL cells

Matusali, Giulia; Leo, Alessandra De; Gavioli, Riccardo; Bertelli, Laura; Renzo, Livia Di; Mattia, Elena Di

doi:10.1016/j.bbrc.2006.11.127

Cited by 3 publications

(3 citation statements)

References 28 publications

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“…As a first evaluation of the efficacy of the synthesized peptides as fluorogenic proteasome substrates we treated Raji lysate (representing human B cell lymphoma) with these following the literature protocol (described in the Supporting Information) [17] . Raji lysate contain iCP and cCP, as well as other proteases [27] . Measurement over time of the fluorescent signal that is the result of the released ACC/AMC group indicates proteasome activity (Figure 1A and Figure S1 in the Supporting Information).…”

Section: Resultsmentioning

confidence: 99%

“…[17] Raji lysate contain iCP and cCP, as well as other proteases. [27] Measurement over time of the fluorescent signal that is the result of the released ACC/AMC group indicates proteasome activity ( Figure 1A and Figure S1 in the Supporting Information). The resulting signals might, however, stem from proteasomemediated processing but also from other proteases able to process the fluorogenic substrates.…”

Section: Substrate Hydrolysis In Cell Extractsmentioning

confidence: 99%

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Structure‐Based Design of Fluorogenic Substrates Selective for Human Proteasome Subunits

et al. 2020

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Proteasomes are established therapeutic targets for hematological cancers and promising targets for autoimmune diseases. In the past, we have designed and synthesized mechanism-based proteasome inhibitors that are selective for the individual catalytic activities of human constitutive proteasomes and immunoproteasomes: β1c, β1i, β2c, β2i, β5c and β5i. We show here that by taking the oligopeptide recognition element and substituting the electrophile for a fluorogenic leaving group, fluorogenic substrates are obtained that report on the proteasome catalytic activity also targeted by the parent inhibitor. Though not generally applicable (β5c and β2i substrates showing low activity), effective fluorogenic substrates reporting on the individual activity of β1c, β1i, β2c and β5i subunits in Raji (human B cell) lysates and purified 20S proteasome were identified in this manner. Our work thus adds to the expanding proteasome research toolbox through the identification of new and/or more effective subunit-selective fluorogenic substrates.

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Section: Resultsmentioning

confidence: 99%

Section: Substrate Hydrolysis In Cell Extractsmentioning

confidence: 99%

Structure‐Based Design of Fluorogenic Substrates Selective for Human Proteasome Subunits

et al. 2020

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“…At the indicated times, samples (about 10 6 cells) were collected, washed and lysed as described [ 38 ]. 30 μg of proteins, as determined by a modified Lowry assay (RC DC protein assay, BioRad), were resolved by SDS-PAGE on a 10% gel and transferred onto nitrocellulose membrane.…”

Section: Methodsmentioning

confidence: 99%

Inhibition of Poly(ADP-ribose)polymerase impairs Epstein Barr Virus lytic cycle progression

Mattiussi

Tempera

Matusali

et al. 2007

Infect Agents Cancer

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Epstein-Barr virus lytic cycle activation alters proteasome subunit expression in Burkitt's lymphoma cells

Leo

Matusali

Arena

et al. 2010

Biological Chemistry

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We have shown that Epstein-Barr virus (EBV) lytic cycle activation in Burkitt's lymphoma (BL) cells down-regulates chymotrypsin- and caspase-like activities of the proteasome. The aim of the present study was to evaluate whether EBV activation might also affect proteasome subunit composition. Our results indicate that, independently of the latency program established in the host cells, induction of the EBV lytic cycle reduces the expression of the proteasomal components β5, β1 and β2i, whereas it increases that of β2, β1i, PA28α and PA28β. The modulation of the composition and enzymatic activities of the proteolytic complex are indicative of a less efficient generation of viral immunoepitopes.

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Down-regulation of proteolytic complexes following EBV activation in BL cells

Cited by 3 publications

References 28 publications

Structure‐Based Design of Fluorogenic Substrates Selective for Human Proteasome Subunits

Structure‐Based Design of Fluorogenic Substrates Selective for Human Proteasome Subunits

Inhibition of Poly(ADP-ribose)polymerase impairs Epstein Barr Virus lytic cycle progression

Epstein-Barr virus lytic cycle activation alters proteasome subunit expression in Burkitt's lymphoma cells

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