Isolation and Characterization of a Novel Inducible Mammalian Galectin

Dunphy, Jillian L.; Balic, Adam; Barcham, Garry; Horváth, Anita; Nash, Andrew D.; Meeusen, Elza Nicole Theresia

doi:10.1074/jbc.m003739200

Cited by 92 publications

(95 citation statements)

References 40 publications

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“…Galectin 14 in particular, is expressed by eosinophils which characteristically accumulate at the site of infection [18]. Similarly, galectin 15 (OVGAL11) expression was shown to be greatly upregulated in helminth larval infected gastrointestinal tissue subject to inflammation and eosinophil infiltration [3]. Immunohistological analysis has showed that the protein is localized in the cytoplasm and nucleus of upper epithelial cells of the gastrointestinal tract and it has also been detected in mucus samples collected from infected abomasum but not from uninfected tissue [3].…”

Section: Discussionmentioning

confidence: 99%

“…Similarly, galectin 15 (OVGAL11) expression was shown to be greatly upregulated in helminth larval infected gastrointestinal tissue subject to inflammation and eosinophil infiltration [3]. Immunohistological analysis has showed that the protein is localized in the cytoplasm and nucleus of upper epithelial cells of the gastrointestinal tract and it has also been detected in mucus samples collected from infected abomasum but not from uninfected tissue [3]. Gastrointestinal infection is characterised by the presence of increased numbers of mucosal mast cells, and these are pivotal in the immediate hypersensitivity reaction associated with immune rejection of nematode parasites in rodents [12,21].…”

Section: Discussionmentioning

confidence: 99%

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Proteomic approach to identify candidate effector molecules during the in vitro immune exclusion of infectiveTeladorsagia circumcinctain the abomasum of sheep

Athanasiadou

Pemberton²,

Jackson³

et al. 2008

Vet. Res.

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-In the present study we have employed an in vitro organ challenge model to study the post-challenge responses in parasite naïve and immune gastric tissue of sheep, in an attempt to identify the host derived factors involved in immune exclusion of Teladorsagia circumcincta larvae. Proteins present in the epithelial cells and mucus from ovine abomasa following parasite challenge in previously naïve and immune animals were analysed through Matrix Assisted Laser Desorption/Ionization-Time of Flight (MALDI-Tof)-MS and shotgun proteomics. MALDI-ToF analysis of epithelial cell lysates revealed that a number of proteins identified were differentially expressed in naïve and immune cells. These included intelectin and lysozymes, which were present at higher levels in epithelial cell lysates derived from immune samples. A large number of proteins were identified in the mucosal wash from immune tissue which were not present in the mucosal wash of the naïve tissue. Some of these proteins were present in washes of immune tissue prior to the parasite challenge including immunoglobulin A, galectin 14 and 15 and sheep mast cell protease 1. However, other proteins, such as calcium activated chloride channel and intelectin were only detected in the washings from the challenged tissue. The latter may be related to an enhanced mucus release, which may result in entrapment of infective larvae and thus reduced establishment in tissue that has been previously challenged with the parasite. In conclusion, several proteins have been identified which may be involved, either directly or indirectly, in the exclusion and immune elimination of incoming infective larvae. In the present study, the usefulness of the in vitro model has been confirmed, and the global proteomic approach has identified proteins that had not previously been associated with parasite exclusion from abomasal mucosa, such as the calcium activated chloride channel.immunity / mucus / proteomics / sheep / Teladorsagia circumcincta

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Proteomic approach to identify candidate effector molecules during the in vitro immune exclusion of infectiveTeladorsagia circumcinctain the abomasum of sheep

Athanasiadou

Pemberton²,

Jackson³

et al. 2008

Vet. Res.

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“…The nuclear staining was variable and may depend on the nature of the stimuli or different stages of the cell cycle. Galectins 1, 3, 10, and 11 are all known to localize simultaneously to the nucleus and cytoplasm under various conditions (11). The role galectins 10 and 11 play in the nucleus remains unknown, but it has been postulated that galectins 1 and 3 regulate pre-mRNA splicing (11).…”

Section: Expression Of Galectin-14 In Lung Tissue and Its Release Intmentioning

confidence: 99%

Isolation and Characterization of a Novel Eosinophil-specific Galectin Released into the Lungs in Response to Allergen Challenge

Dunphy¹,

Barcham²,

Bischof³

et al. 2002

Journal of Biological Chemistry

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A novel galectin cDNA (galectin-14) was cloned from ovine eosinophil-rich leukocytes by low stringency reverse transcriptase-PCR and cDNA library screening. Data base searches indicate that this gene encodes a novel prototype galectin that contains one putative carbohydrate recognition domain and exhibits most identity to galectin-9/ecalectin, a potent eosinophil chemoattractant. The sugar binding properties of the recombinant molecule were confirmed by a hemagglutination assay and lactose inhibition. The mRNA and protein of galectin-14 are expressed at high levels in eosinophilrich cell populations. Flow cytometry and cytospot staining demonstrate that the protein localizes to the cytoplasmic, but not the granular, compartment of eosinophils. In contrast, galectin-14 mRNA and protein were not detected in neutrophils, macrophages, or lymphocytes. Western blot analysis of bronchoalveolar lavage fluid indicates that galectin-14 is released from eosinophils into the lumen of the lungs after challenge with house dust mite allergen. The restricted expression of this novel galectin to eosinophils and its release into the lumen of the lung in a sheep asthma model indicates that it may play an important role in eosinophil function and allergic inflammation.The immune response of mammals to multicellular parasite infections and allergens is characterized by the recruitment of eosinophils (1, 2). The role eosinophils play in both parasite infections and allergic reactions remains controversial, and little is known of the specific function of eosinophil constituents in combating multicellular parasites or exacerbating allergic responses. The presence of eosinophils and eosinophil-derived products in the respiratory tract does, however, correlate with the pathological manifestations of allergic asthma (2-4).One of the limitations in the study of eosinophils is the scarcity of this cell population in normal individuals and the difficulty in obtaining sufficient numbers of unmanipulated cells from allergic tissues. Sheep offer a unique experimental system in which large numbers of eosinophils can be obtained using the relatively non-invasive procedure of mammary infusion of allergens followed by "milking" of the mammary gland to obtain the inflammatory cells recruited into the lumen (5, 6). Using this experimental system, the present study describes the identification of a novel galectin (galectin-14) specifically expressed by eosinophils. The expression of galectin-14 was up-regulated in the lung tissue of sensitized sheep challenged with house dust mite extract (HDM), 1 and the protein was released into the bronchoalveolar lavage (BAL) fluid.Galectins are carbohydrate binding proteins that have been increasingly implicated in both adaptive and innate immune responses. The eosinophil-specific expression of galectin-14 and its secretion into the lumen of the lung in a sheep asthma model indicates that it may play an important role in regulating the activity of eosinophils during allergic responses and further highlights the i...

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“…Western-blot analyses of separated protein was conducted as described previously (Spencer et al 1999a) using enhanced chemiluminescence detection. Immunoreactive galectin-15 was detected using primary rabbit anti-ovine galectin-15 serum (provided kindly by Dr Els N T Meeusen, Monash University, Melbourne, Australia; Dunphy et al 2000) at a 1:2500 dilution. Negative control blots were performed in which primary antibody was replaced by rabbit serum at the same concentration.…”

Section: Western-blot Analysesmentioning

confidence: 99%

“…Galectin-15 was originally identified in ovine intestinal epithelium as being induced in response to infection by Haemonchus contortus, a nematode parasite (Dunphy et al 2000). Expression of the galectin-15 gene was detected only after day 10 of pregnancy in the endometrial LE and superficial ductal GE (sGE) and was induced by progesterone and further stimulated by interferon t, the pregnancy-recognition signal produced by the conceptus.…”

Section: Introductionmentioning

confidence: 99%

Galectin-15 in ovine uteroplacental tissues

Gray

Dunlap²,

Burghardt³

et al. 2005

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Galectin-15 is the newest member of a secreted b-galactoside-binding lectin family. The galectin-15 gene is expressed specifically by the endometrial luminal epithelium (LE) and superficial ductal glandular epithelium (sGE) of the ovine uterus. The proposed extracellular role of secreted galec7tin-15 is to regulate implantation and placentation by functioning as a heterophilic cell adhesion molecule between the conceptus trophectoderm and endometrial LE, while that of intracellular galectin-15 is to regulate cell survival, differentiation and function. The present study determined galectin-15 expression in uteroplacental tissues during gestation and in the postpartum uterus. In the uterine lumen, secreted galectin-15 was found as multimers, particularly on days 14 and 16 of pregnancy. In the endometrial epithelium and conceptus trophectoderm, intracellular galectin-15 protein was found associated with crystalline structures. Between days 20 and 120 of pregnancy, galectin-15 mRNA was expressed specifically by the LE and sGE of the intercaruncular endometrium of ewes. Immunoreactive galectin-15 protein was most abundant in the trophectoderm with lower levels in the endometrial LE and sGE. Galectin-15 protein was detected in allantoic fluid, but not in amniotic fluid. After parturition, galectin-15 mRNA declined in the endometrium from postpartum day (PPD) 1 to 28 and exhibited a variegated expression pattern in the LE and sGE. These results indicate that galectin-15 is synthesized and secreted throughout gestation by the endometrial LE/sGE and is absorbed by the placenta and forms crystals within the trophectoderm, whereas the remainder is cleared into the allantois after being transported into the fetal circulation via the placental areolae. Based on the biological properties of other galectin family members, galectin-15 is hypothesized to have biological roles in conceptus -endometrial interactions, uterine immune and inflammatory responses, and placental morphogenesis and function.

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Isolation and Characterization of a Novel Inducible Mammalian Galectin

Cited by 92 publications

References 40 publications

Proteomic approach to identify candidate effector molecules during the in vitro immune exclusion of infectiveTeladorsagia circumcinctain the abomasum of sheep

Proteomic approach to identify candidate effector molecules during the in vitro immune exclusion of infectiveTeladorsagia circumcinctain the abomasum of sheep

Isolation and Characterization of a Novel Eosinophil-specific Galectin Released into the Lungs in Response to Allergen Challenge

Galectin-15 in ovine uteroplacental tissues

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