Regionally specific distribution of the binding of anti-glutamine synthetase and anti-S100 antibodies and of Datura stramonium lectin in glial domains of the optic lobe of the giant prawn.
We previously characterized some crustacean glial cells by markers such as 2',3'-cyclic nucleotide 3'-phosphodiesterase and glial fibrillary acidic protein. Here we use antibodies against glutamine synthetase full-length molecule (anti-GS/FL), a GS C-terminal peptide (anti-GS/20aa-C), and brain S100 (anti-S100), as well as the binding of the insect glia and rat astrocytic marker Datura stramonium lectin (DSL), in the optic lobe of the prawn Macrobrachium rosenbergii. All markers label the lamina ganglionaris cartridge region (lighter: anti-GS/FL; heavier: DSL). In addition, anti-GS/FL labels superficial somata of external and internal medullas and internal chiasm cells. Both anti-GS/20aa-C and anti-S100 label heavily the glial sheaths of the lamina ganglionaris. In addition, anti-S100 binds to the perineurial glia of medullary parenchymal vessels. Western blot analyses show that both anti-GS/FL and anti-GS/20aa-C bind mostly to a band of 50-55 kDa, compatible with a long isoform of vertebrate GS, and accessorily to a possible dimer and, in the case of anti-GS/20aa-C, to an ill-defined band of intermediate mass. Binding of anti-S100 is selective for a single band of about 68 kDa but shows no protein in the weight range of the canonical S100 protein superfamily. DSL reveals two bands of about 75 and about 120 kDa, thus within the range of maximal recognition for rat astrocytes. Our results suggest that phenotype protein markers of the optic lobe glia share antigenic determinants with S100 and (a long form of) GS and that, similarly to vertebrate and insect glia, crustacean glia protein and N-glycan residue markers display regional heterogeneity.
Allodi
Silvana
S
Departamento de Histologia e Embriologia, Instituto de Ciências Biomédicas, ICB, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil.
Bressan
Cristine M
CM
Carvalho
Sergio L
SL
Cavalcante
Leny A
LA
D000818:Animals; D000906:Antibodies / Q000378:metabolism; D000941:Antigens / Q000276:immunology; D015415:Biomarkers / Q000378:metabolism; D002462:Cell Membrane / Q000276:immunology / Q000378:metabolism; D019143:Evolution, Molecular; D005974:Glutamate-Ammonia Ligase / Q000096:biosynthesis / Q000276:immunology*; D018698:Glutamic Acid / Q000378:metabolism; D007150:Immunohistochemistry / Q000379:methods; D008970:Molecular Weight; D009457:Neuroglia / Q000166:cytology / Q000201:enzymology*; D019581:Neuropil / Q000276:immunology / Q000378:metabolism; D009899:Optic Lobe, Nonmammalian / Q000166:cytology / Q000201:enzymology*; D033541:Palaemonidae / Q000166:cytology / Q000201:enzymology*; D037121:Plant Lectins / Q000378:metabolism* / Q000493:pharmacokinetics; D011134:Polysaccharides / Q000276:immunology; D011485:Protein Binding / Q000276:immunology; D009418:S100 Proteins / Q000096:biosynthesis / Q000276:immunology*; D013045:Species Specificity
D000906:Antibodies; D000941:Antigens; D015415:Biomarkers; C041384:Datura stramonium lectin; D037121:Plant Lectins; D011134:Polysaccharides; D009418:S100 Proteins; D018698:Glutamic Acid; D005974:Glutamate-Ammonia Ligase