TY - JOUR
T1 - Expression and activity of glycogen synthase kinase during vitellogenesis and embryogenesis of Rhipicephalus (Boophilus) microplus
AU - Logullo, Carlos
AU - Witola, William H.
AU - Andrade, Caroline
AU - Abreu, Leonardo
AU - Gomes, Josiana
AU - da Silva Vaz, Itabajara
AU - Imamura, Saiki
AU - Konnai, Satoru
AU - Ohashi, Kazuhiko
AU - Onuma, Misao
PY - 2009/5/12
Y1 - 2009/5/12
N2 - Glycogen synthase kinase 3 (GSK-3) is classically described as a key enzyme involved in glycogen metabolism in mammals. GSK-3 belongs to a highly conserved family of serine/threonine protein kinases, whose members are involved in hormonal regulation, nuclear signaling, and cell fate determination in higher eukaryotes. We have cloned and characterized the RmGSK-3 gene from Rhipicephalus (Boophilus) microplus tick embryos. DNA and protein sequence analysis depicted high similarity to the corresponding enzyme, from both vertebrate and invertebrate animals. In addition, the mRNA transcription profile identified during embryogenesis was analyzed. We observed that the RmGSK-3 mRNA rapidly decreases from the 1st to 3rd day of development, and increases from the 3rd to 15th day. After the 15th day of development, we observed a near 50% reduction in RmGSK-3 mRNA transcription in comparison to the 1st day. We detected the GSK-3β isoform in egg homogenates throughout embryogenesis using Western blot analysis. RmGSK-3 mRNA was present in fat body, midgut and ovary from partially and fully engorged adult female ticks. The highest mRNA level was observed in ovaries from both developmental stages and in first-day eggs. Furthermore, RmGSK-3 activity correlated with glycogen content variation. Finally, kinase activity in egg homogenates was inhibited by the specific inhibitor, SB-216763. These data suggest that RmGSK-3β may be involved in glycogen metabolism regulation during R. microplus embryogenesis.
AB - Glycogen synthase kinase 3 (GSK-3) is classically described as a key enzyme involved in glycogen metabolism in mammals. GSK-3 belongs to a highly conserved family of serine/threonine protein kinases, whose members are involved in hormonal regulation, nuclear signaling, and cell fate determination in higher eukaryotes. We have cloned and characterized the RmGSK-3 gene from Rhipicephalus (Boophilus) microplus tick embryos. DNA and protein sequence analysis depicted high similarity to the corresponding enzyme, from both vertebrate and invertebrate animals. In addition, the mRNA transcription profile identified during embryogenesis was analyzed. We observed that the RmGSK-3 mRNA rapidly decreases from the 1st to 3rd day of development, and increases from the 3rd to 15th day. After the 15th day of development, we observed a near 50% reduction in RmGSK-3 mRNA transcription in comparison to the 1st day. We detected the GSK-3β isoform in egg homogenates throughout embryogenesis using Western blot analysis. RmGSK-3 mRNA was present in fat body, midgut and ovary from partially and fully engorged adult female ticks. The highest mRNA level was observed in ovaries from both developmental stages and in first-day eggs. Furthermore, RmGSK-3 activity correlated with glycogen content variation. Finally, kinase activity in egg homogenates was inhibited by the specific inhibitor, SB-216763. These data suggest that RmGSK-3β may be involved in glycogen metabolism regulation during R. microplus embryogenesis.
KW - Embryogenesis
KW - Glycogen synthase kinase
KW - Metabolism
KW - Rhipicephalus (Boophilus) microplus
KW - Tick egg
UR - http://www.scopus.com/inward/record.url?scp=64749103817&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=64749103817&partnerID=8YFLogxK
U2 - 10.1016/j.vetpar.2009.01.029
DO - 10.1016/j.vetpar.2009.01.029
M3 - Article
C2 - 19285806
AN - SCOPUS:64749103817
SN - 0304-4017
VL - 161
SP - 261
EP - 269
JO - Veterinary parasitology.
JF - Veterinary parasitology.
IS - 3-4
ER -