Infection with Leishmania infantum Inhibits actinomycin D-induced apoptosis of human monocytic cell line U-937. 2005

Sabrina Lisi, and Margherita Sisto, and Angela Acquafredda, and Rosa Spinelli, and Mariaangela Schiavone, and Vincenzo Mitolo, and Olga Brandonisio, and Mariaantonietta Panaro
Department of Human Anatomy and Histology, University of Bari, I-70124 Bari, Italy. s.lisi@anatomia.unib.it

Modulation of host cell apoptosis has been observed in many bacterial, protozoal, and viral infections. The aim of this work was to investigate the effect of viscerotropic Leishmania (L.) infantum infection on actinomycin D-induced apoptosis of the human monocytic cell line U-937. Cells were infected with L. infantum promastigotes or treated with the surface molecule lipophosphoglycan (LPG) or with parasite-free supernatant of Leishmania culture medium and submitted to action of actinomycin D as the apoptosis-inducing agent. Actinomycin D-induced apoptosis in U-937 cells was inhibited in the presence of both viable L. infantum promastigotes and soluble factors contained in Leishmania culture medium or purified LPG. Leishmania infantum affected the survival of U-937 cells via a mechanism involving inhibition of caspase-3 activation. Furthermore, protein kinase C delta (PKC delta) cleavage was increased in actinomycin D-treated U-937 cells and was inhibited by the addition of LPG. Thus, inhibition of the PKC-mediated pathways by LPG can be implicated in the enhanced survival of the parasites. These results support the claim that promastigotes of L. infantum, as well as its surface molecule, LPG, which is in part released in the culture medium, inhibit macrophage apoptosis, thus allowing intracellular parasite survival and replication.

UI MeSH Term Description Entries
D009000 Monocytes Large, phagocytic mononuclear leukocytes produced in the vertebrate BONE MARROW and released into the BLOOD; contain a large, oval or somewhat indented nucleus surrounded by voluminous cytoplasm and numerous organelles. Monocyte
D010401 Penicillin G Benzathine Semisynthetic antibiotic prepared by combining the sodium salt of penicillin G with N,N'-dibenzylethylenediamine. Benzathine Penicillin,Bencelin,Benzathine Benzylpenicillin,Benzathine Benzylpénicilline Panpharma,Benzetacil,Bicillin,Bicillin L-A,Brevicilina,Cepacilina,Debecillin,Extencilline,Pendepon,Penduran,Pendysin,Penicillin G Benzathine Anhydrous,Penidural,Peniroger Retard,Permapen,Provipen Benzatina,Tardocillin,Benzathine, Penicillin G,Benzylpenicillin, Benzathine,Bicillin L A,Bicillin LA,Penicillin, Benzathine
D011493 Protein Kinase C An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters. Calcium Phospholipid-Dependent Protein Kinase,Calcium-Activated Phospholipid-Dependent Kinase,PKC Serine-Threonine Kinase,Phospholipid-Sensitive Calcium-Dependent Protein Kinase,Protein Kinase M,Calcium Activated Phospholipid Dependent Kinase,Calcium Phospholipid Dependent Protein Kinase,PKC Serine Threonine Kinase,Phospholipid Sensitive Calcium Dependent Protein Kinase,Phospholipid-Dependent Kinase, Calcium-Activated,Serine-Threonine Kinase, PKC
D003609 Dactinomycin A compound composed of a two CYCLIC PEPTIDES attached to a phenoxazine that is derived from STREPTOMYCES parvullus. It binds to DNA and inhibits RNA synthesis (transcription), with chain elongation more sensitive than initiation, termination, or release. As a result of impaired mRNA production, protein synthesis also declines after dactinomycin therapy. (From AMA Drug Evaluations Annual, 1993, p2015) Actinomycin,Actinomycin D,Meractinomycin,Cosmegen,Cosmegen Lyovac,Lyovac-Cosmegen,Lyovac Cosmegen,Lyovac, Cosmegen,LyovacCosmegen
D004791 Enzyme Inhibitors Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction. Enzyme Inhibitor,Inhibitor, Enzyme,Inhibitors, Enzyme
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D000953 Antigens, Protozoan Any part or derivative of any protozoan that elicits immunity; malaria (Plasmodium) and trypanosome antigens are presently the most frequently encountered. Protozoan Antigens
D017209 Apoptosis A regulated cell death mechanism characterized by distinctive morphologic changes in the nucleus and cytoplasm, including the endonucleolytic cleavage of genomic DNA, at regularly spaced, internucleosomal sites, i.e., DNA FRAGMENTATION. It is genetically programmed and serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth. Apoptosis, Extrinsic Pathway,Apoptosis, Intrinsic Pathway,Caspase-Dependent Apoptosis,Classic Apoptosis,Classical Apoptosis,Programmed Cell Death,Programmed Cell Death, Type I,Apoptoses, Extrinsic Pathway,Apoptoses, Intrinsic Pathway,Apoptosis, Caspase-Dependent,Apoptosis, Classic,Apoptosis, Classical,Caspase Dependent Apoptosis,Cell Death, Programmed,Classic Apoptoses,Extrinsic Pathway Apoptoses,Extrinsic Pathway Apoptosis,Intrinsic Pathway Apoptoses,Intrinsic Pathway Apoptosis
D053148 Caspase 3 A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 9. Isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA. CASP3,Apopain,Caspase-3,Pro-Caspase-3,Procaspase-3,Pro Caspase 3,Procaspase 3

Related Publications

Sabrina Lisi, and Margherita Sisto, and Angela Acquafredda, and Rosa Spinelli, and Mariaangela Schiavone, and Vincenzo Mitolo, and Olga Brandonisio, and Mariaantonietta Panaro
March 1987, Japanese journal of cancer research : Gann,
Sabrina Lisi, and Margherita Sisto, and Angela Acquafredda, and Rosa Spinelli, and Mariaangela Schiavone, and Vincenzo Mitolo, and Olga Brandonisio, and Mariaantonietta Panaro
April 1985, Cellular immunology,
Sabrina Lisi, and Margherita Sisto, and Angela Acquafredda, and Rosa Spinelli, and Mariaangela Schiavone, and Vincenzo Mitolo, and Olga Brandonisio, and Mariaantonietta Panaro
March 1995, Journal of medical microbiology,
Sabrina Lisi, and Margherita Sisto, and Angela Acquafredda, and Rosa Spinelli, and Mariaangela Schiavone, and Vincenzo Mitolo, and Olga Brandonisio, and Mariaantonietta Panaro
December 2000, Biochemical pharmacology,
Sabrina Lisi, and Margherita Sisto, and Angela Acquafredda, and Rosa Spinelli, and Mariaangela Schiavone, and Vincenzo Mitolo, and Olga Brandonisio, and Mariaantonietta Panaro
July 1990, The American journal of physiology,
Sabrina Lisi, and Margherita Sisto, and Angela Acquafredda, and Rosa Spinelli, and Mariaangela Schiavone, and Vincenzo Mitolo, and Olga Brandonisio, and Mariaantonietta Panaro
January 1990, Journal of immunology (Baltimore, Md. : 1950),
Sabrina Lisi, and Margherita Sisto, and Angela Acquafredda, and Rosa Spinelli, and Mariaangela Schiavone, and Vincenzo Mitolo, and Olga Brandonisio, and Mariaantonietta Panaro
August 2001, Infection and immunity,
Sabrina Lisi, and Margherita Sisto, and Angela Acquafredda, and Rosa Spinelli, and Mariaangela Schiavone, and Vincenzo Mitolo, and Olga Brandonisio, and Mariaantonietta Panaro
July 1996, International journal of cancer,
Sabrina Lisi, and Margherita Sisto, and Angela Acquafredda, and Rosa Spinelli, and Mariaangela Schiavone, and Vincenzo Mitolo, and Olga Brandonisio, and Mariaantonietta Panaro
August 1998, The American journal of tropical medicine and hygiene,
Sabrina Lisi, and Margherita Sisto, and Angela Acquafredda, and Rosa Spinelli, and Mariaangela Schiavone, and Vincenzo Mitolo, and Olga Brandonisio, and Mariaantonietta Panaro
September 2001, Anti-cancer drugs,
Copied contents to your clipboard!