Growth hormone as an in vitro phagocyte-activating factor in the gilthead sea bream ( Sparus aurata )

1997 ◽  
Vol 287 (3) ◽  
pp. 535-540 ◽  
Author(s):  
Josep Alvar Calduch-Giner ◽  
Ariadna Sitjà-Bobadilla ◽  
Pilar Alvarez-Pellitero ◽  
Jaume Pérez-Sánchez
1994 ◽  
Vol 95 (3) ◽  
pp. 321-329 ◽  
Author(s):  
B. Cavari ◽  
P.-Y. Le Bail ◽  
B. Levavi-Sivan ◽  
P. Melamed ◽  
H. Kawauchi ◽  
...  

1995 ◽  
Vol 46 (3) ◽  
pp. 494-500 ◽  
Author(s):  
J. M. Mancera ◽  
P. Fernandez-Llebrez ◽  
J. M. Perez-Figares

Aquaculture ◽  
2015 ◽  
Vol 442 ◽  
pp. 138
Author(s):  
George Rigos ◽  
Evdokia Karagouni ◽  
Ioannis Kyriazis ◽  
Evita Athanasiou ◽  
Kriton Grigorakis ◽  
...  

1995 ◽  
Vol 146 (3) ◽  
pp. 459-467 ◽  
Author(s):  
J A Calduch-Giner ◽  
A Sitjà-Bobadilla ◽  
P Álvarez-Pellitero ◽  
J Pérez-Sánchez

Abstract Receptors for GH were characterized in the head kidney of gilthead sea bream (Sparus aurata), using radioiodinated and biotinylated ligands. The specific binding of radiolabelled recombinant gilthead sea bream GH (rsbGH) to head kidney membrane preparations was dependent on membrane concentration. Salmon prolactin, salmon gonadotrophin and carp gonadotrophin did not compete for 125I-labelled rsbGH-binding sites. Unlabelled rsbGH competitively displaced 125I-labelled rsbGH bound to head kidney membranes. Scatchard plots were always linear, denoting the presence of a single class of binding sites. The binding affinity (Ka=2·7 × 109 m−1) was equivalent to that found in liver membrane preparations, but the binding capacity (2·5 ±0·30 fmol/mg protein) was 50- to 75-fold lower. To identify the cells which express the GH receptor, head kidney smears were incubated with biotinylated rsbGH, followed by incubation with an avidin–biotin complex conjugated to alkaline phosphatase. The reaction with the new-fuchsin substrate gave a red precipitate, showing a specific and intense labelling in erythroblasts, polychromatophilic erythroblasts and myeloblasts. Noticeable binding was observed in myelocytes and immature granulocytes, tending to disappear at the latter stages of granulocyte maturation. Light but appreciable binding was also observed in monocytes, lymphocytes and acidophilic erythroblasts, whereas it was completely absent in proerythrocytes and erythrocytes. The proliferative action of rsbGH and recombinant human IGF-I on in vitro cultures of head kidney cells was demonstrated by a 5-bromo-2′-deoxy-uridine immunoassay. To our knowledge, this is the first report that provides suitable evidence for a role of GH as a haemopoietic growth and differentiation factor in lower vertebrate species. Journal of Endocrinology (1995) 146, 459–467


1993 ◽  
Vol 71 (8) ◽  
pp. 1500-1505 ◽  
Author(s):  
P.-Y. Le Bail ◽  
B. Mourot ◽  
Y. Zohar ◽  
J. Pérez-Sánchez

The development of a homologous radioimmunoassay (RIA) for gilthead sea bream growth hormone (sbGH) is described. RIA sensitivity was 0.4 ng/mL, and ED50 was 1.74 ± 0.05 ng/mL. Intra- and inter-assay coefficients of variation were 3.4 and 8.8%, respectively, at ED50 levels. Mammalian growth hormones (GH), carp gonadotropin, chinook salmon gonadotropin, ovine porlactin, and recombinant tilapia prolactin did not show cross-reactivity. Serial dilutions of recombinant trout GH indicated a low but significant cross-reactivity. The displacement curves for plasma and pituitary homogenates from sparid fish (gilthead sea bream, blacktail, white sea bream, Couch's sea bream, and marmor-brassen) were parallel to that of the sbGH standard. Pituitary homogenates from other perciform fish tested (gaper, grey mullet, red mullet, and sea pike) also showed parallel slopes of inhibition. Pituitary homogenates from common sole, sea scorpion, forked hake, goldfish, rainbow trout, and European eel showed low or negligible cross-reactivity. These results suggest that the GHs of perciform fish have a number of similarities in structure. RIA of sea bream GH can be used to quantify the GH of sparid fish and perciform fish, provided a validation has been carried out.


1995 ◽  
Vol 110 (4) ◽  
pp. 335-340 ◽  
Author(s):  
Juan Pedro Martínez-Barberá ◽  
Carlos Pendón ◽  
Hilario Martí-Palanca ◽  
Josep A. Calduch-Giner ◽  
Ramón B. Rodríguez ◽  
...  

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