Heat shock protein synthesis over time in infective Trichinella spiralis larvae raised in suboptimal culture conditions.
Changes in the viability, infectivity and heat shock protein (Hsp) levels are reported in Trichinella spiralis first stage larvae (L1) stored in 199 medium for up to seven days at 37 degrees C. These conditions induce stress that the larvae, eventually, cannot overcome. After three days of storage, the infectivity and viability were unchanged, although higher Hsp70 levels were observed. After this time, larvae gradually lost viability and infectivity, coinciding with a decrease in Hsp70 and Hsp90 and an increase in actin (a housekeeping protein). In addition, a possibly inducible heat shock protein, Hsp90i, appeared as constitutive Hsp90 disappeared. No significant changes in Hsp60 levels were detected at any time. These results suggest that heat shock proteins initially try to maintain homeostasis, but on failing, may be involved in cell death.
Martinez
J
J
Facultad de Farmacia, Departmento de Microbiologia y Parasitologia, Universidad de Alcalá de Henares, Madrid, Spain. francisco.martinez@uah.es
Perez-Serrano
J
J
Bernadina
W E
WE
Rincon
I
I
Rodriguez-Caabeiro
F
F
D000818:Animals; D015415:Biomarkers / Q000032:analysis; D016923:Cell Death; D018840:HSP70 Heat-Shock Proteins / Q000032:analysis / Q000096:biosynthesis; D018841:HSP90 Heat-Shock Proteins / Q000032:analysis / Q000096:biosynthesis; D006360:Heat-Shock Proteins / Q000032:analysis / Q000096:biosynthesis*; D006358:Hot Temperature; D010274:Parasitology / Q000379:methods; D013997:Time Factors; D017160:Trichinella spiralis / Q000737:chemistry / Q000378:metabolism*
D015415:Biomarkers; D018840:HSP70 Heat-Shock Proteins; D018841:HSP90 Heat-Shock Proteins; D006360:Heat-Shock Proteins