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Glycohistochemical study of the toadfish Halobatrachus didactylus (Scheider, 1801) stomach
Desantis, S.; Acone, F.; Zizza, S.; Deflorio, M.; Palazón Fernández, J.L.; Sarasquete, C.; De Metrio, G. (2009). Glycohistochemical study of the toadfish Halobatrachus didactylus (Scheider, 1801) stomach. Sci. Mar. (Barc.) 73(3): 515-525
In: Scientia Marina (Barcelona). Consejo Superior de Investigaciones Científicas. Institut de Ciènces del Mar: Barcelona. ISSN 0214-8358, more
Peer reviewed article  

Available in Authors 

Keywords
    Histochemistry; Stomach; Marine

Authors  Top 
  • Desantis, S.
  • Acone, F.
  • Zizza, S.
  • Deflorio, M.
  • Palazón Fernández, J.L.
  • Sarasquete, C.
  • De Metrio, G.

Abstract
    Toadfish Halobatrachus didactylus gastric mucosa was studied using conventional and lectin histochemistry. Conventional histochemistry revealed neutral glycoconjugates predominating over acidic ones in the apical zone of both surface epithelial cells and pit cells. The neck cells contained a few neutral glycoconjugates, whereas gastric glands were negative to PAS and AB staining. Lectin histochemistry showed different oligosaccharide expression along the columnar cells. The sub-nuclear cytoplasm was stained with RCA120, SBA, HPA, GSA I-B4, GSA II, UEA I, LTA, Con A, KOH-sialidase-WGA. The Golgi zone reacted with RCA120, DBA, SBA, HPA, KOH-sialidase-WGA, GSA I-B4, GSA II, UEA I, LTA, MAL II, SNA, and showed an increase in DBA staining after KOH-sialidase treatment. The granules of the apical zone stained with PNA, UEA I, LTA and showed increased PNA reactivity after KOH-sialidase treatment. The luminal cell coat reacted with PNA, HPA, Con A, KOH-sialidase-WGA, UEA I, LTA, MAL II, SNA and KOH-sialidase-PNA. Pit cells showed a minor expression of lectin-binding sites with respect to columnar cells. Neck cells linked UEA I and LTA and gastric glands reacted with PNA, DBA, SBA, HPA, Con A, GSA I-B4, KOH-sialidase-WGA and KOH-sialidase-DBA. The results suggest that the stomach of the toadfish H. didactylus is characterised by a species-specific glycoconjugate pattern.

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