Neutrophil migration induced in vivo and in vitro by marine algal lectins

Neves, S. A.; Dias‐Baruffi, Marcelo; Freitas, Ana Lúcia Ponte; Roque‐Barreira, Maria Cristina

doi:10.1007/pl00000222

Cited by 24 publications

(14 citation statements)

References 6 publications

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“…In general, they have no affinity for simple sugars but are more specific for complex oligosaccharides, often glycoproteins, especially those found in animals (Hori et al 1990;Rogers and Hori 1993). Although physiological function(s) of lectins in algae is presently unknown, recent studies show that macroalgal lectins also possess in vitro or in vivo immunomodulatory, anti-tumor and anti-cancer activities (Kawakubo et al 1997;Sugahara et al 2001;Neves et al 2001;Pinto et al 2009). Specially, a lectin GRFT from the red alga Griffithsia sp.…”

Section: Introductionmentioning

confidence: 94%

A new screening for hemagglutinins from Vietnamese marine macroalgae

Hung¹,

Lý²,

Trang³

et al. 2011

J Appl Phycol

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Aqueous extracts from 42 species of Vietnamese marine macroalgae, including 17 Chlorophyta, 22 Rhodophyta, and three Phaeophyta species, were examined for hemagglutination activity using native and enzyme-treated different animal and human erythrocytes. All extracts agglutinated at least one type of erythrocytes tested. Strong activity was detected in extracts from four Chlorophyta (Caulerpa serulata var. boryana, Caulerpa sertularioides f. longipes, Halimeda velasquezii, and Halimeda discoidea) and two Rhodophyta species (Gelidiella acerosa and Titanophora pulchra) with enzyme-treated rabbit and horse erythrocytes. The hemagglutinins of some active species were examined for sugar-binding specificity, pH, temperature stability, and divalent cation independency using ammonium sulfate precipitates prepared from their extracts. In a hemagglutination-inhibition test with various monosaccharides and glycoproteins, none of the hemagglutinins had affinity for monosaccharides. The activity of the hemagglutinins was inhibited by some glycoproteins tested. The inhibition profiles with glycoproteins were different depending on hemagglutinin species, suggesting the presence of lectins specific for complex N-glycans, high mannose N-glycans or O-glycans. On the other hand, the activities of almost all algal hemagglutinins were stable over a wide range of pH and temperature, and independent of the presence of divalent cations, except Gelidiopsis scoparia hemagglutinin, its activity was dependent on the presence of divalent cations. These results suggest that Vietnamese marine macroalgae may be good sources of useful lectins for many biological applications.

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Section: Introductionmentioning

confidence: 94%

A new screening for hemagglutinins from Vietnamese marine macroalgae

Hung¹,

Lý²,

Trang³

et al. 2011

J Appl Phycol

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“…Although the physiological function of agglutinins in algae is not clear, biochemical studies indicate that algal haemagglutinins have potentially useful applications in biochemical, drug, and clinical studies. For example, several studies have reported that algal haemagglutinins exhibit immunomodulatory and antitumour activities in vitro and in vivo [16,19,22].…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of a novel haemagglutinin from Chlorella pyrenoidosa

Chu

Huang

Ling

2006

J Ind Microbiol Biotechnol

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We previously identified a strong haemagglutination activity in the freshwater unicellular green alga, Chlorella pyrenoidosa. Here, we sought to purify and characterize the haemagglutinin associated with this activity. Ammonium sulfate precipitation, gel filtration on sephacryl S-200 and DEAE-Sepharose ion-exchange chromatography were used to purify the haemagglutinin, which was designated CPH (Chlorella pyrenoidosa haemagglutinin). The molecular weight of CPH was estimated as 58 kDa by SDS-PAGE and 60 kDa by gel filtration of the native protein, indicating that this haemagglutinin exists as a monomer. The haemagglutinin activity of CPH was inhibited by glycoproteins, especially yeast mannan, but not by monosaccharides or disaccharides, indicating that CPH is carbohydrate-specific. In addition to the composition of CPH shown to be rich in glycine and acidic amino acids, heamagglutinating activity of CPH was insensitive to variations in pH or the presence of divalent cations, and atomic force microscopy revealed that the protein is rod-shaped. These results indicate that the characteristics of CPH are consistent with its identification as a haemagglutinin, and suggest that CPH may be a viable candidate for applications in a variety of biomedical fields.

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“…The pro-inflammatory effect of lectins from marine red algae (Amansia multifida, Bryothamnion seaforthii, Bryothamnion triquetrum and Gracilaria caudata) has been previously reported by inducing chemotaxis of human neutrophils in vitro and neutrophil migration into the peritoneal cavity of rats or mice and the dorsal air pouch of rats [12]. Depending on the administration route used, lectins can exert pro-or anti-inflammatory actions, activating or inhibiting neutrophil migration via interactions between the lectin domain of exogenous lectins with carbohydrate residues present in the inflammatory cell membranes (e.g., lectins isolated from leguminous seeds of Araucaria angustifolia and Dioclea violacea) [24,25].…”

Section: Discussionmentioning

confidence: 99%

“…Regarding the inflammatory process, most lectins have shown anti-inflammatory activities [9][10][11], but some have presented pro-inflammatory activity [12]. Moreover, immunomodulatory properties have also been described [13].…”

Section: Introductionmentioning

confidence: 99%