Binding profiles and cytokine-inducing effects of fish rhamnose-binding lectins on Burkitt's lymphoma Raji cells

Masahiro Hosono, Shigeki Sugawara, Atsushi Matsuda, Takeo Tatsuta, Yasuhiro Koide, Imtiaji Hasan, Yasuhiro Ozeki, Kazuo Nitta

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Rhamnose-binding lectin (RBL) is one of the animal lectin categories which take part in the innate immune responses of fish. Osmerus lanceolatus lectin (OLL) from shishamo smelt eggs is an RBL composed of two tandem-repeated domains, both of which are considered to be a carbohydrate-recognition domain. SAL, catfish (Silurus asotus) egg RBL composed of three domains, binds to Burkitt's lymphoma Raji cells through globotriaosylceramide (Gb3) carbohydrate chain and to reduce cell size and growth by altering membrane composition without causing cell death. In this experiment, we tried to compare the binding effects of these two RBLs on Raji cells. Flow cytometric and fluorescence microscopic analyses revealed that OLL also directly bound to and shrunk Raji cells with ten times less reactivity than SAL but reduced cell growth with decreasing cell viability. Anti-Gb3 antibody completely blocked the binding of SAL to Raji cells but not that of OLL. In addition, the direct bindings of OLL and SAL to Raji cells were comparably inhibited by melibiose, but lactose was more effective inhibitor for the binding of OLL than that of SAL. These results suggest that OLL has slightly different cell-binding property compared with SAL and binds not only to Gb3 but also to the other carbohydrate receptor-bearing β-galactoside chains. The quantitative RT-PCR analysis revealed that SAL induced the expression of TNF-α but not of IFN-γ, IL-1β, and IL-10. Thus, SAL-induced cytostatic effect on Raji cells might be partially caused by TNF-α-mediated signaling pathway.

Original languageEnglish
Pages (from-to)1559-1572
Number of pages14
JournalFish Physiology and Biochemistry
Volume40
Issue number5
DOIs
Publication statusPublished - 2014
Externally publishedYes

Fingerprint

Rhamnose
Burkitt Lymphoma
rhamnose
Osmerus
lymphoma
Lectins
lectins
Fish
carbohydrate
Fishes
cytokines
Cytokines
fish
egg
cells
immune response
antibody
inhibitor
fish roe
viability

Keywords

  • Burkitt's lymphoma
  • Domain structure
  • Fish eggs
  • Gb3
  • Lectin
  • TNF-α

ASJC Scopus subject areas

  • Aquatic Science
  • Biochemistry
  • Physiology
  • Medicine(all)

Cite this

Binding profiles and cytokine-inducing effects of fish rhamnose-binding lectins on Burkitt's lymphoma Raji cells. / Hosono, Masahiro; Sugawara, Shigeki; Matsuda, Atsushi; Tatsuta, Takeo; Koide, Yasuhiro; Hasan, Imtiaji; Ozeki, Yasuhiro; Nitta, Kazuo.

In: Fish Physiology and Biochemistry, Vol. 40, No. 5, 2014, p. 1559-1572.

Research output: Contribution to journalArticle

Hosono, Masahiro ; Sugawara, Shigeki ; Matsuda, Atsushi ; Tatsuta, Takeo ; Koide, Yasuhiro ; Hasan, Imtiaji ; Ozeki, Yasuhiro ; Nitta, Kazuo. / Binding profiles and cytokine-inducing effects of fish rhamnose-binding lectins on Burkitt's lymphoma Raji cells. In: Fish Physiology and Biochemistry. 2014 ; Vol. 40, No. 5. pp. 1559-1572.
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AU - Hosono, Masahiro

AU - Sugawara, Shigeki

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AU - Tatsuta, Takeo

AU - Koide, Yasuhiro

AU - Hasan, Imtiaji

AU - Ozeki, Yasuhiro

AU - Nitta, Kazuo

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AB - Rhamnose-binding lectin (RBL) is one of the animal lectin categories which take part in the innate immune responses of fish. Osmerus lanceolatus lectin (OLL) from shishamo smelt eggs is an RBL composed of two tandem-repeated domains, both of which are considered to be a carbohydrate-recognition domain. SAL, catfish (Silurus asotus) egg RBL composed of three domains, binds to Burkitt's lymphoma Raji cells through globotriaosylceramide (Gb3) carbohydrate chain and to reduce cell size and growth by altering membrane composition without causing cell death. In this experiment, we tried to compare the binding effects of these two RBLs on Raji cells. Flow cytometric and fluorescence microscopic analyses revealed that OLL also directly bound to and shrunk Raji cells with ten times less reactivity than SAL but reduced cell growth with decreasing cell viability. Anti-Gb3 antibody completely blocked the binding of SAL to Raji cells but not that of OLL. In addition, the direct bindings of OLL and SAL to Raji cells were comparably inhibited by melibiose, but lactose was more effective inhibitor for the binding of OLL than that of SAL. These results suggest that OLL has slightly different cell-binding property compared with SAL and binds not only to Gb3 but also to the other carbohydrate receptor-bearing β-galactoside chains. The quantitative RT-PCR analysis revealed that SAL induced the expression of TNF-α but not of IFN-γ, IL-1β, and IL-10. Thus, SAL-induced cytostatic effect on Raji cells might be partially caused by TNF-α-mediated signaling pathway.

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