Molecular cloning, expression and functional analysis of TNF13b (BAFF) in Japanese sea perch, Lateolabrax japonicus

B Cell-Activating Factor Regulates Different Aspects of B Cell Functionality and Is Produced by a Subset of Splenic B Cells in Teleost Fish

“…A few studies in fish have concluded a capacity of BAFF to induce proliferation of total leukocyte populations using methodological approaches that do not make a distinction between proliferation and survival (22, 23, 27, 29). Thus, in this study, we wanted to clearly address this issue and clarify whether fish BAFF has proliferative effects or, as in mammals, it is exclusively a survival factor.…”

“…In addition, BAFF sequences have been reported in different teleost fish species including zebrafish ( Danio rerio ) (21), mefugu ( Takifugu obscurus ) (22), Japanese sea perch ( Lateolabrax japonicus ) (23), grass carp ( Ctenopharyngodon idella ) (24), yellow grouper ( Epinephelus awoara ) (25), miiuy croaker ( Miichthys miiuy ) (26), tongue sole ( Cynoglossus semilaevis ) (27), Nile tilapia ( Oreochromis niloticus ) (28), rock bream ( Oplegnathus fasciatus ) (29), and cartilaginous fish such as white-spotted catshark ( Chiloscyllium plagiosum ) (30), spiny dogfish ( Squalus acanthias ) (31), and small-spotted catshark ( Scyliorhinus canicula ) (32). Although recombinant BAFF proteins have been produced for some of these species (21–23, 25, 27–30), many of these studies have exclusively tested the effect of recombinant fish BAFF on B cell survival using mammalian B cells (21, 22, 25, 28, 30). Furthermore, those studies, which have concluded a capacity of BAFF to induce proliferation using teleost leukocytes, have not made a distinction between proliferation and survival as they have only determined increased numbers of leukocytes after BAFF treatment and have not clearly established that the cells showing increased survival or proliferating were in fact B cells (21–23, 27, 29).…”

“…Although recombinant BAFF proteins have been produced for some of these species (21–23, 25, 27–30), many of these studies have exclusively tested the effect of recombinant fish BAFF on B cell survival using mammalian B cells (21, 22, 25, 28, 30). Furthermore, those studies, which have concluded a capacity of BAFF to induce proliferation using teleost leukocytes, have not made a distinction between proliferation and survival as they have only determined increased numbers of leukocytes after BAFF treatment and have not clearly established that the cells showing increased survival or proliferating were in fact B cells (21–23, 27, 29). Consequently, the role that BAFF plays on B cell function in teleost remains largely unknown.…”

Characterization of BAFF and APRIL subfamily receptors in rainbow trout (Oncorhynchus mykiss). Potential role of the BAFF / APRIL axis in the pathogenesis of proliferative kidney disease

“…Regarding the BAFF and APRIL subfamily of ligands and receptors, BAFF sequences have been reported recently in different teleosts including zebrafish ( Danio rerio ) [9], mefugu ( Takifugu obscurus ) [10], Japanese sea perch ( Lateolabrax japonicus ) [11], grass carp ( Ctenopharyngodon idella ) [12], yellow grouper ( Epinephelus awoara ) [13], miiuy croaker ( Miichthys miiuy ) [14], tongue sole ( Cynoglossus semilaevis ) [15], Nile tilapia ( Oreochromis niloticus ) [16], rock bream ( Oplegnathus fasciatus ) [17], rainbow trout ( Oncorhynchus mykiss ) [18], rohu ( Labeo rohita ) [19] and cartilaginous fish such as white-spotted catshark ( Chiloscyllium plagiosum ) [20], spiny dogfish ( Squalus acanthias ) [21] and small-spotted catshark ( Scyliorhinus canicula ) [22]. APRIL sequences, on the other hand, have only been identified in channel catfish ( Ictalurus punctatus ), Atlantic salmon ( Salmo salar ) and rainbow trout [18, 22].…”

Molecular cloning, expression and bioactivity of B cell activating factor (BAFF) in African ostrich

“…The sequence alignment showed high similarity of OsBAFF with other birds' BAFFs. Mammalian BAFF is processed by a furin-like protease after a characteristic sequence motif which results in the release of biologically active soluble protein [37]. A putative furin cleavage site (R-X-R-R) (X = any amino acid) is located near the amino terminus of the OsBAFF protein ( Fig.…”