TY - JOUR
T1 - An acidic sphingomyelinase Type C activity from Mycobacterium Tuberculosis
AU - Castro-Garza, Jorge
AU - González-Salazar, Francisco
AU - Quinn, Frederick D.
AU - Karls, Russell K.
AU - De La Garza-Salinas, Laura Hermila
AU - Guzmán-De La Garza, Francisco J.
AU - Vargas-Villarreal, Javier
N1 - Publisher Copyright:
© 2016 Asociación Argentina de Microbiología.
PY - 2016/1/1
Y1 - 2016/1/1
N2 - Sphingomyelinases (SMases) catalyze the hydrolysis of sphingomyelin to ceramide and phosphorylcholine. Sphingolipids are recognized as diverse and dynamic regulators of a multitude of cellular processes mediating cell cycle control, differentiation, stress response, cell migration, adhesion, and apoptosis. Bacterial SMases are virulence factors for several species of pathogens. Whole cell extracts of Mycobacterium tuberculosis strains H37Rv and CDC1551 were assayed using [N-methyl-
14C]-sphingomyelin as substrate. Acidic Zn
2+-dependent SMase activity was identified in both strains. Peak SMase activity was observed at pH 5.5. Interestingly, overall SMase activity levels from CDC1551 extracts are approximately 1/3 of those of H37Rv. The presence of exogenous SMase produced by M. tuberculosis during infection may interfere with the normal host inflammatory response thus allowing the establishment of infection and disease development. This Type C activity is different from previously identified M. tuberculosis SMases. Defining the biochemical characteristics of M. tuberculosis SMases helps to elucidate the roles that these enzymes play during infection and disease.
AB - Sphingomyelinases (SMases) catalyze the hydrolysis of sphingomyelin to ceramide and phosphorylcholine. Sphingolipids are recognized as diverse and dynamic regulators of a multitude of cellular processes mediating cell cycle control, differentiation, stress response, cell migration, adhesion, and apoptosis. Bacterial SMases are virulence factors for several species of pathogens. Whole cell extracts of Mycobacterium tuberculosis strains H37Rv and CDC1551 were assayed using [N-methyl-
14C]-sphingomyelin as substrate. Acidic Zn
2+-dependent SMase activity was identified in both strains. Peak SMase activity was observed at pH 5.5. Interestingly, overall SMase activity levels from CDC1551 extracts are approximately 1/3 of those of H37Rv. The presence of exogenous SMase produced by M. tuberculosis during infection may interfere with the normal host inflammatory response thus allowing the establishment of infection and disease development. This Type C activity is different from previously identified M. tuberculosis SMases. Defining the biochemical characteristics of M. tuberculosis SMases helps to elucidate the roles that these enzymes play during infection and disease.
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UR - http://www.mendeley.com/catalogue/actividad-una-esfingomielinasa-%C3%A1cida-tipo-c-producida-por-mycobacteriumtuberculosis
U2 - 10.1016/j.ram.2016.01.001
DO - 10.1016/j.ram.2016.01.001
M3 - Article
SN - 0325-7541
VL - 48
SP - 21
EP - 26
JO - Revista Argentina de Microbiologia
JF - Revista Argentina de Microbiologia
IS - 1
ER -
