sarcoma/protease

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Molecular mechanics calculations on Rous sarcoma virus protease with peptide substrates.

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Molecular models of Rous sarcoma virus (RSV) protease and 20 peptide substrates with single amino acid substitutions at positions from P4 to P3', where the scissile bond is between P1 and P1'. were built and compared with kinetic measurements. The unsubstituted peptide substrate.

Morphological transformation of cells induced by Kirsten sarcoma virus transforming factor is independent of serine proteases.

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Reports from several laboratories have suggested that the virus transformed state may be maintained either by ectopically produced growth factors or alternatively by ectopically produced serine proteases including plasminogen activator. Here we show that the maintenance of transformation induced by

Structure of the aspartic protease from Rous sarcoma retrovirus refined at 2-A resolution.

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The structure of Rous sarcoma virus protease has been solved by multiple isomorphous replacement in the crystal form belonging to space group P3(1)21, with unit-cell parameters a = 88.95 A and c = 78.90 A. The enzyme belongs to the family of aspartic proteases with two identical subunits composing

HHV8 and Kaposi's sarcoma: should we really give up protease inhibitors in all HIV-infected patients?

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: We describe the first case of a patient presenting Kaposi's sarcoma with human herpes virus 8 (HHV8) viremia after switching from a protease inhibitor to an integrase inhibitor-based combination antiretroviral therapy, followed by a rapid remission when resuming protease inhibitor. We suggest that

Functional consequences of the Kaposi's sarcoma-associated herpesvirus protease structure: regulation of activity and dimerization by conserved structural elements.

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The structure of Kaposi's sarcoma-associated herpesvirus protease (KSHV Pr), at 2.2 A resolution, reveals the active-site geometry and defines multiple possible target sites for drug design against a human cancer-producing virus. The catalytic triad of KSHV Pr, (Ser114, His46, and His157) and

Proteolytic activities of mouse sarcoma 180 cells that are inhibited by Bowman-Birk and Kunitz protease inhibitors.

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In this study, using zymogram analysis two proteolytic activities were identified in the mouse sarcoma 180 (S-180) cells that were activated by trypsin treatment and inhibited by both BBI and ACTI. These enzymes, with molecular weights of 46 kDa (dominant band) and 62 kDa (minor band), were mainly

Auto-inactivation by cleavage within the dimer interface of Kaposi's sarcoma-associated herpesvirus protease.

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An autolysis site of functional and structural significance has been mapped within the dimer interface of Kaposi's sarcoma-associated herpesvirus protease. Cleavage 27 residues from the C terminus of the 230 amino acid residue, 25 kDa protein was observed to cause a loss of dimerization and

HIV protease inhibitors as new treatment options for Kaposi's sarcoma.

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A reduced incidence and regression of Kaposi's sarcoma (KS) and other tumours has been reported in Acquired Immune Deficiency Syndrome (AIDS) patients treated with antiretroviral combination therapies containing Human Immunodeficiency Virus (HIV) protease inhibitors (PIs) such as indinavir or

Effect of protease inhibitors on focus formation by murine sarcoma virus.

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The effect of six protease inhibitors, isolated from various species of actinomycetes, on focus formation by murine sarcoma virus was examined. Pepstatin was the only inhibitor. The treatment of cells with pepstatin at various times possibly retards the early stage of infection with murine sarcoma

Clinical and biological impact of antiretroviral therapy with protease inhibitors on HIV-related Kaposi's sarcoma.

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OBJECTIVE To evaluate the clinical and biological impact of protease inhibitors on HIV-associated Kaposi's sarcoma. METHODS A cohort of 10 patients included prospectively from April 1996 to June 1997 were studied in one institutional centre after initiation of protease inhibitors. METHODS All

Amino acids encoded downstream of gag are not required by Rous sarcoma virus protease during gag-mediated assembly.

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Rous sarcoma virus (RSV) and its relatives are unique in that they appear to encode their viral protease in the gag reading frame. As a result, this 124-amino-acid sequence is found at the carboxy terminus of each Gag precursor molecule and, upon ribosome frameshifting, embedded within each Gag-Pol

Characterization of the protease of a fish retrovirus, walleye dermal sarcoma virus.

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Three fish retroviruses infecting walleyes constitute the recently recognized genus called epsilonretrovirus. The founding member of this group, walleye dermal sarcoma virus (WDSV), induces benign skin tumors in the infected fish and replicates near 4 degrees C. While the viral genomic sequence is

Mechanism of inhibition of the retroviral protease by a Rous sarcoma virus peptide substrate representing the cleavage site between the gag p2 and p10 proteins.

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The activity of the avian myeloblastosis virus (AMV) or the human immunodeficiency virus type 1 (HIV-1) protease on peptide substrates which represent cleavage sites found in the gag and gag-pol polyproteins of Rous sarcoma virus (RSV) and HIV-1 has been analyzed. Each protease efficiently processed

The protease and the assembly protein of Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8).

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A genomic clone encoding the protease (Pr) and the assembly protein (AP) of Kaposi's sarcoma-associated herpesvirus (KSHV) (also called human herpesvirus 8) has been isolated and sequenced. As with other herpesviruses, the Pr and AP coding regions are present within a single long open reading frame.

Inhibition of protease activity in cultures of rous sarcoma virus-transformed cells: effect on the transformed phenotype.

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We have examined the role of proteolytic activity in the genesis and maintenance of the transformed phenotype by growing cultures of chick embryo fibroblasts transfromed by Rous sarcoma virus either in medium containing plasminogen-free serum or in medium to which protease inhibitors were added.

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