Xenopus laevis lectin is localized at several sites in Xenopus oocytes, eggs, and embryos.

Roberson, Marie; Barondes, Samuel H.

doi:10.1083/jcb.97.6.1875

Cited by 46 publications

(27 citation statements)

References 15 publications

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“…However, hIntL was also expressed on various tissues other than oocytes, and it has been reported that the other homologues are also present in various tissues (26,28,40). Thus, hIntL and its homologues may not only participate in formation of the fertilization envelope but also have other physiological functions.…”

Section: Discussionmentioning

confidence: 99%

Human Intelectin Is a Novel Soluble Lectin That Recognizes Galactofuranose in Carbohydrate Chains of Bacterial Cell Wall

Tsuji

Uehori

Matsumoto

et al. 2001

Journal of Biological Chemistry

333

312

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Galactofuranosyl residues are present in various microorganisms but not in mammals. In this study, we identified a human lectin binding to galactofuranosyl residues and named this protein human intelectin (hIntL). The mature hIntL was a secretory glycoprotein consisting of 295 amino acids and N-linked oligosaccharides, and its basic structural unit was a 120-kDa homotrimer in which 40-kDa polypeptides were bridged by disulfide bonds. The hIntL gene was split into 8 exons on chromosome 1q21.3, and hIntL mRNA was expressed in the heart, small intestine, colon, and thymus. hIntL showed high levels of homology with mouse intelectin, Xenopus laevis cortical granule lectin/oocyte lectin, lamprey serum lectin, and ascidian galactose-specific lectin. These homologues commonly contained no carbohydrate recognition domain, which is a characteristic of C-type lectins, although some of them have been reported as Ca 2؉ -dependent lectins. Recombinant hIntL revealed affinities to D-pentoses and a D-galactofuranosyl residue in the presence of Ca 2؉ , and recognized the bacterial arabinogalactan of Nocardia containing D-galactofuranosyl residues. These results suggested that hIntL is a new type lectin recognizing galactofuranose, and that hIntL plays a role in the recognition of bacteria-specific components in the host.In host defense, the recognition of bacterial components is important for induction of immune responses. The cell wall components of pathogens have various biological activities and contain the bacteria-specific carbohydrate chains that do not exist in mammals. The recognition of these carbohydrate chains is useful to induce the cellular responses and fluidphase immune reactions for elimination of pathogens.In the innate immune response, the bacterial carbohydrate chains are recognized by the animal lectins that are present on cells as phagocytosis receptors or in plasma as opsonins or agglutinins. As a phagocytosis receptor, the mannose receptor binds materials containing terminal mannosyl residues such as zymosan and enhances their clearance by phagocytes (1, 2).The collectins and the ficolins are soluble lectins, and these lectins function as opsonins or agglutinins for bacteria (3)(4)(5)(6). In addition, the mannose-binding lectin (MBL), 1 a typical collectin, and ficolin/P32 form complexes with MBL-associated serine proteases in plasma. Binding of these complexes to targets activates the complement system, and complement activation induces opsonization of the targets by phagocytes and the target killing by formation of the membrane attack complex (7-9). This lectin-dependent complement activation pathway is named the lectin pathway and plays important roles in innate immunity (10, 11). These biological defense lectins commonly have affinity to mannose or N-acetylglucosamine, and binding is sustained by Ca 2ϩ (1-6), although the opposite results have been reported with regard to the Ca 2ϩ dependence of ficolins (5, 6, 12). On the other hand, animal lectins also include a group of lectins that have affinity to...

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Section: Discussionmentioning

confidence: 99%

Human Intelectin Is a Novel Soluble Lectin That Recognizes Galactofuranose in Carbohydrate Chains of Bacterial Cell Wall

Tsuji

Uehori

Matsumoto

et al. 2001

Journal of Biological Chemistry

333

312

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“…The rat lectin showed one major protein band with M, -14 .500 when examined by PAGE (Fig. 2), but there was also a clear minor band with M, 29,000 and a small amount of protein trailing behind the major band. On the basis of microdensitometry (Fig.…”

Section: Lectin Purificationmentioning

confidence: 99%

Endogenous mammalian lectin localized extracellularly in lung elastic fibers

Cerra¹

1984

The Journal of Cell Biology

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An affinity-purified antibody preparation raised against a beta- galactoside-binding lectin from bovine lung was used to localize a similar lectin in rat lung by immunofluorescence and by electron microscopy after on-grid staining visualized with colloidal gold conjugated second antibody. The endogenous mammalian lectin was found in smooth muscle cells and squamous alveolar epithelial (type I) cells and was concentrated extracellularly in elastic fibers of pulmonary parenchyma and blood vessels. The extracellular localization of this lectin suggests that it, like others, functions by interaction with extracellular glycoconjugates.

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“…On the contrary, Roberson and Barondes (15) did not detect the lectin in VC of either unfertilized or fertilized eggs. The possibility that they used an antiserum other than that used by Greve and Hedrick (6) or in the present work must be excluded by comparison of the biochemical natures of the antigens (12,14,23,24).…”

Section: Discussionmentioning

confidence: 98%

“…From immunocytochemical observations on specimens embedded in a plastic resin, Greve and Hedrick (6) concluded that CGLs were present in the F layer and the perivitelline space, but not in the VC. However, Roberson and Barondes (15) could not confirm the presence of lectin in the fertilization coat (which probably consists of the VC plus the F layer), but they detected lectin in the cortical granules in sections embedded in plastic. These discrepant results were probably due to differences in immunohistochemical techniques and/or limited resolution by light microscopy.…”

Section: Introductionmentioning

confidence: 99%

Immunoelectron Microscopic Demonstration of Cortical Granule Lectins in Coelomic, Unfertilized and Fertilized Eggs of Xenopus laevis

Yoshizaki

1989

Dev Growth Differ

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lmmunoelectron microscopic studies demonstrated cortical granule lectins (CGLs) in coelomic, unfertilized and fertilized eggs of Xenopus laevis. An antiserum raised against purified cortical granule lectin 1 specifically reacted with the CGLs in irnmunoblotting and agar diffusion tests. When ultrathin sections were treated with the antiserum and protein A-gold solution, gold particles, indicating antigenic sites, were seen over cortical granules of coelomic and unfertilized eggs, and over the perivitelline space, the vitelline coat and the condensed region of the fertilization layer of fertilized eggs. The pre-fertilization layer immediately adjacent to the outer margin of the vitelline coat in unfertilized eggs was free from gold particles. These observations suggest that released CGLs permeate through the vitelline coat of fertilized eggs and interact with the pre-fertilization layer mainly at the outer margin of the vitelline coat, resulting in formation of the fertilization layer which acts as a block to polyspermy.

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Xenopus laevis lectin is localized at several sites in Xenopus oocytes, eggs, and embryos.

Cited by 46 publications

References 15 publications

Human Intelectin Is a Novel Soluble Lectin That Recognizes Galactofuranose in Carbohydrate Chains of Bacterial Cell Wall

Human Intelectin Is a Novel Soluble Lectin That Recognizes Galactofuranose in Carbohydrate Chains of Bacterial Cell Wall

Endogenous mammalian lectin localized extracellularly in lung elastic fibers

Immunoelectron Microscopic Demonstration of Cortical Granule Lectins in Coelomic, Unfertilized and Fertilized Eggs of Xenopus laevis

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