Galectins. Structure and function of a large family of animal lectins.

Barondes, Samuel H.; Cooper, Douglas N.W.; Gitt, Michael A.; Leffler, Hakon

doi:10.1016/s0021-9258(17)31891-4

Cited by 1,313 publications

(206 citation statements)

References 78 publications

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“…4 Importantly, galectin-3, as a regulator in acute and chronic inflammation, is found not only in the myocardium but also in numerous cells and tissues, with its effects on intra-and extracellular cell signalling of macrophages and neutrophils. [4][5][6] In rat models of heart failure, expression of galectin-3 increases more than 5-fold in the myocardium. 3 Furthermore, when galectin-3 is actively infused into the rat pericardium, the animals develop collagen deposition and systolic dysfunction.…”

Section: Introductionmentioning

confidence: 99%

Galectin-3 increase in endurance athletes

Hättasch

Spethmann

Boer

et al. 2013

Eur J Prev Cardiolog

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Section: Introductionmentioning

confidence: 99%

Galectin-3 increase in endurance athletes

Hättasch

Spethmann

Boer

et al. 2013

Eur J Prev Cardiolog

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“…A number of soluble galactoside binding lectins have been isolated from various mammalian tissues. All these proteins show well-conserved amino acid sequence in their carbohydrate binding domains (CBDs) and therefore are believed to constitute a distinct protein family recently designated galectins (Barondes et al 1994; Kasai and Hirabayashi 1996). To date, 10 different types of galectins have been cloned and characterized.…”

mentioning

confidence: 99%

“…They include galectin-1 (Clerch et al 1988), −2 (Gitt et al 1992), −3 (Cherayil et al 1989), −4 (Oda et al 1993), −5 (Gitt et al 1995), −6 (Gitt et al 1998), −7 (Madsen et al 1995), −8 (Hadari et al 1995), −9 (Wada and Kanwar 1997), and −10 (Leonidas et al 1995). These are expressed as 14−36−kD cytosolic proteins without a secretion signal peptide (Barondes et al 1994), which have one (galectin−1, −2, −3, −5, −7, and −10) or two (galectin−4, −6, −8, and −9) CBDs within a single molecule. Of galectin−4, −6 and a splicing isoform of galectin−9, which are exclusively localized in gastrointestinal (GI) tract epithelia, the most well-studied is galectin-4 (G-4).…”

mentioning

confidence: 99%

Two Domains of Rat Galectin-4 Bind to Distinct Structures of the Intercellular Borders of Colorectal Epithelia

Wasano

Hirakawa

1999

J Histochem Cytochem.

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Galectin-4 (G4) is a member of a family of soluble galactoside-binding lectins found in various mammalian tissues. To determine the function of this protein in colorectal tissue, we separately produced the N- and C-terminal carbohydrate binding domains (CBD) of rat G4 as a recombinant glutathione S-transferase (GST) fusion protein (G4-N and G4-C) and examined the tissue binding site(s) of each CBD by light and electron microscopy (LM and EM). At the LM level, both fusion proteins stained the intercellular borders of the surface-lining epithelial cells of colorectal mucosa. At the EM level, two proteins recognized spatially close but distinct subcellular structures. G4-N stained electron-lucent flocculent substances freely located in the intercellular spaces, whereas G4-C bound to the lateral cell membranes demarcating the intercellular spaces. These findings suggest that colorectal G4 may be involved in crosslinking the lateral cell membranes of the surface-lining epithelial cells, thereby reinforcing epithelial integrity against mechanical stress exerted by the bowel lumen. (J Histochem Cytochem 47:75-82, 1999)

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“…Another protein of potential interest is beta-galactoside-binding lectin, belonging to galectins [78]. Galectins are involved as modulators in metabolic and inflammatory processes [79].…”

Section: Discussionmentioning

confidence: 99%

Immunoproteomic Analysis of Dirofilaria repens Microfilariae and Adult Parasite Stages

et al. 2021

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Dirofilariarepens is a parasitic nematode causing a vector-borne zoonotic infection (dirofilariosis), considered an emerging problem in human and veterinary medicine. Currently, diagnosis is based on the detection of the adult parasite and microfilariae in the host tissues. However, the efficacy of tests relying on microfilariae detection is limited by microfilariae periodic occurrence. Therefore, a new reliable and affordable serological diagnostic method is needed. Better characteristic of the parasite biology and its interaction with host immune system should help to achieve this goal. This study analyzes adult and microfilariae proteomes, and the use of one-dimensional electrophoresis (1-DE) and two-dimensional electrophoresis (2-DE) proteomics, immunoproteomics, and LC-MS/MS mass spectrometry allowed us to identify 316 potentially immunogenic proteins (75 belong to adult stage, 183 to microfilariae, and 58 are common for both). Classified by their ontology, the proteins showed important similarities and differences between both parasite stages. The most frequently identified proteins are structural, metabolic, and heat shock proteins. Additionally, real-time PCR analysis of some immunogenic targets revealed significant differences between microfilariae and adult life stages. We indicated molecules involved in parasite-host interactions and discussed their importance in parasite biology, which may help to reveal potential diagnostic antigens or select drug and vaccine targets.

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Galectins. Structure and function of a large family of animal lectins.

Cited by 1,313 publications

References 78 publications

Galectin-3 increase in endurance athletes

Galectin-3 increase in endurance athletes

Two Domains of Rat Galectin-4 Bind to Distinct Structures of the Intercellular Borders of Colorectal Epithelia

Immunoproteomic Analysis of Dirofilaria repens Microfilariae and Adult Parasite Stages

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