Adaptation of the black tiger shrimp, Penaeus monodon, to different salinities through an excretory function of the antennal gland.
Black tiger shrimps (Penaeus monodon) are able to survive and can be reared under various salinities, possibly by the cellular adaptation of their excretory system, particularly the antennal gland, which is known to regulate body fluid in crustaceans. We have investigated the morphological and biochemical alterations of the antennal glands in shrimp reared in 7, 15, or 30 ppt seawater. Drastic changes occur in animals reared under 7 ppt conditions. Ultrastructural studies of the antennal gland in shrimps reared in 7 ppt seawater have revealed that podocytic cells in the coelomosacs ramify with more cytoplasmic processes forming the filtration slits, and that the tubular labyrinth cells possess more mitochondria in their basal striation and a wider tubular lumen than those found in the other groups. Many apical cytoplasmic blebs from labyrinth cells have also been seen in the lumen of the labyrinths under 7 ppt conditions, a feature that is not as prominent under the other conditions. The expression and activity of the Na(+)/K(+)-ATPase in the antennal gland are also correlated with the surrounding environment: the lower the salinity, the higher the expression and activity of the enzyme. Immunohistochemistry results have demonstrated the highest staining intensity in the labyrinth cells of shrimps reared under 7 ppt conditions. Our findings thus suggest that one of the adaptation mechanisms of this shrimp to the surrounding salinity is the regulation of Na(+)/K(+)-ATPase expression in the antennal gland, in conjunction with subcellular changes in its excretory cells.
Buranajitpirom
Decha
D
Department of Anatomy, Faculty of Science, Mahidol University, Bangkok, Thailand.
Asuvapongpatana
Somluk
S
Weerachatyanukul
Wattana
W
Wongprasert
Kanokpan
K
Namwong
Wisa
W
Poltana
Pisit
P
Withyachumnarnkul
Boonsirm
B
D000222:Adaptation, Physiological; D000825:Animal Structures / Q000166:cytology / Q000201:enzymology / Q000502:physiology* / Q000648:ultrastructure; D000818:Animals; D033561:Penaeidae / Q000502:physiology*; D021122:Protein Subunits / Q000378:metabolism; D054712:Salinity; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism
D021122:Protein Subunits; D000254:Sodium-Potassium-Exchanging ATPase