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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Low salinity-induced alterations in epithelial ultrastructure, Na+/K+-ATPase immunolocalization and enzyme kinetic characteristics in the gills of the thinstripe hermit crab, Clibanarius vittatus (Anomura, Diogenidae)

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Antunes, Claudia Doi [1, 2] ; Lucena, Malson Neilson [3] ; Garcon, Daniela Pereira [4] ; Leone, Francisco Assis [3] ; McNamara, John Campbell [1, 2]
Total Authors: 5
[1] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Biol, BR-14040901 Ribeirao Preto, SP - Brazil
[2] Univ Sao Paulo, Ctr Biol Marinha, Sao Sebastiao, SP - Brazil
[3] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Quim, Ribeirao Preto, SP - Brazil
[4] Univ Fed Triangulo Mineiro, Campus Univ Iturama, Iturama, MG - Brazil
Total Affiliations: 4
Document type: Journal article
Web of Science Citations: 2

Fresh caught Clibanarius vittatus {[}SW, 31 parts per thousand salinity (S)] were acclimated to a dilute medium (15 parts per thousand S) for 10 days, employing silver staining to locate gill ion transporting tissue, immunofluorescence to localize the Na+/K+-ATPase alpha-subunit in the lamellae, and electron microscopy to portray ultrastructural changes in the gill epithelia. Na+/K+-ATPase activity was characterized kinetically in a gill microsomal fraction, including synergistic stimulation by NH4+ plus K+. Silver staining revealed that all 26 phyllobranchiate arthro-and pleurobranchiae participate in ion transport. Na+/K+-ATPase alpha-subunit staining was weak in SW crabs and distributed exclusively and irregularly within the intralamellar septal cells, particularly at the septal-pillar cell body junctions, and septal cell cytoplasm facing the hemolymph space. In 15 parts per thousand S crabs, alpha-subunit localization was intense, occupying the entire thickened septum. Pillar cells and flanges did not stain. Mitochondria and membrane foldings increased in the pillar cell flanges and intralamellar septal cells, greatly amplifying surface area. Only a single ATP binding site (V-M = 130.8 +/- 10.5 nmol min(-1) mg protein(-1); K-0.5 = 55.3 +/- 1.7 mu mol l(-1)) obeying Michaelis-Menten kinetics was disclosed. Na+/K+-ATPase activity was modulated by Mg2+, Na+, and NH4+, exhibiting site-site interactions; K+ modulation showed Michaelis-Menten kinetics. K+ plus NH4+ synergistically stimulated activity approximate to 1.7-fold. Ouabain inhibited total ATPase activity by approximate to 70% (K-I = 220-300 mu mol l(-1)), revealing phosphohydrolytic activities other than the Na+/K+-ATPase. Despite ample phylogenetic separation, the phyllobranchiate lamellae of the Anomura and Caridea share many ultrastructural features, that is, an intralamellar septum and opposed abutting pillar cells, similar Na+/K+-ATPase distribution, and comparable kinetic characteristics. These findings suggest either convergent evolution at the structural and biochemical levels, or preservation of traits present in a remote common ancestor. (AU)

FAPESP's process: 10/17534-0 - Role of (Na,K)-ATPase in osmoregulation and excretion of ammonium ions in euryhaline crustaceans: identification and influence of FXYD2 on the regulation of gill (Na,K)-ATPase of the crab Callinectes danae
Grantee:Francisco de Assis Leone
Support type: Regular Research Grants
FAPESP's process: 13/24252-9 - The (Na+,K+)-ATPase in osmoregulatory capacity in crab Ucides cordatus: biochemical and molecular view
Grantee:Malson Neilson de Lucena
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 13/22605-1 - Kinetic and molecular characterization of gill tissue (Na+,K+)-ATPase from Cardisoma guanhumi (Latreille)crab
Grantee:Francisco de Assis Leone
Support type: Regular Research Grants
FAPESP's process: 10/50188-8 - Decapod crustaceans: multi-disciplinary characterization of the sea biodiversity of the State of São Paulo (taxonomy, spermiotaxonomy, molecular biology and population dynamics)
Grantee:Fernando Luis Medina Mantelatto
Support type: BIOTA-FAPESP Program - Thematic Grants