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PubMed1982

Structural studies of the carbohydrate moieties of lectins from potato (Solanum tuberosum) tubers and thorn-apple (Datura stramonium) seeds.

1. Methylation analysis of potato (Solanum tuberosum) lectin and thorn-apple (Datura stramonium) lectin confirmed previous conclusions that both glycoproteins contained high proportions of l-arabinofuranosides and lesser amounts of d-galactopyranosides. The arabinofuranosides are present in both lectins as short unbranched chains containing 1-->2- and 1-->3-linkages, which are known to be linked to hydroxyproline. Galactopyranosides are present as monosaccharides, which are known to be attached to serine, in potato lectin and as both the monosaccharide and the 1-->3-linked disaccharide in Datura lectin. 2. Alkaline digestion of potato lectin and subsequent separation of the components by gel filtration led to the isolation of four fractions corresponding to the mono-, di-, tri- and tetra-arabinosides of hydroxyproline. The latter two fractions accounted for over 70% of the total hydroxyproline. 3. Methylation analysis was used to show that the triarabinoside contained only 1-->2-linkages between sugars, but that the tetra-arabinoside contained both 1-->2- and 1-->3-linkages. Direct-insertion mass spectrometry of these compounds using electron impact and chemical ionization, in a comparison with other known structural patterns, was used to determine the sequences of the sugars, which were Araf1-->2Araf1-->2Araf1-->Hyp and Araf1-->3Araf1-->2Araf1-->2Araf 1-->Hyp. 4. On the basis of optical rotation it had previously been suggested [Allen, Desai, Neuberger & Creeth (1978) Biochem. J.171, 665-674] that all the arabinose of potato lectin was present as the beta-l-furanoside. However, measurement of the optical rotations of the hydroxyprolyl arabinosides showed that whereas the diarabinoside had a molar rotation ([m]) value close to that predicted, the triarabinoside was more dextrorotatory and the tetra-arabinoside was less dextrorotatory than expected. Possible explanations for these findings are that, although the di- and tri-arabinosides contain exclusively beta-arabinofuranosides, in the tri-arabinoside, interactions between pentose units lead to an enhanced positive rotation. The tetra-arabinoside, however, is proposed to contain a single alpha-arabinofuranoside residue, which is responsible for the lower than expected positive rotation. The observed rotation of the tetra-arabinoside was found to be close to the theoretical value predicted on that basis. Furthermore, the action of a specific alpha-arabinofuranosidase on the tetrasaccharide was to remove a single arabinose residue, presumably the terminal non-reducing sugar, and to produce a product that was indistinguishable on electrophoresis from the triarabinoside. Changes in rotation were compatible with this assumption. 5. It is concluded that the structures of the hydroxyprolyl tri- and tetra-arabinosides of potato lectin are: betaAraf1-->2betaAraf1-->2betaAraf1-->Hyp and alphaAraf1-->3betaAraf1-->2betaAraf 1-->2betaAraf1-->Hyp. These are identical with compounds that have been isolated from the insoluble hydroxyproline-rich glycoproteins of plant cell walls.

Amino Acids↗
PubMed1984

A comparison of tomato (Lycopersicon esculentum) lectin with its deglycosylated derivative.

A deglycosylated derivative of tomato (Lycopersicon esculentum) lectin was prepared with the use of trifluoromethanesulphonic acid. Its properties were generally similar to those of the native lectin, but differences were evident in terms of relative agglutinating activity towards sheep, (untreated) human and trypsin-treated human erythrocytes. The two forms of tomato lectin were used in conjunction with a battery of specific antisera to investigate structural relatedness among solanaceous lectins. Immunological cross-reactivity between tomato, potato and Datura lectins depends on the integrity of the glycosylated region of those lectins; that between Datura lectin and other seed lectins, however, has a separate structural basis.

Cross Reactions↗
PubMed1998

Affinity of four lectins for endocervical and endometrial non-neoplastic and neoplastic glandular epithelium.

AIMS: Endocervical and endometrial tissues were stained with four lectins to determine the difference in staining pattern between non-neoplastic and neoplastic conditions of these tissues. METHODS AND RESULTS: The lectins used were Ulex europaeus agglutinin (UEA), Dolicho biflorus agglutinin (DBA). Concanavalin A (Con A), and Phaseolus vulgaris agglutinin (PHA). Endocervical tissues included normal endocervical glands, microglandular hyperplasia, minimal deviation adenocarcinoma and endocervical adenocarcinoma, well to poorly differentiated types. Endometrial tissues were collected from normal endometrium, simple glandular hyperplasia, complex hyperplasia, atypical hyperplasia and adenocarcinoma grades 1-3. Non-neoplastic and neoplastic endocervical and endometrial glandular epithelium showed positive reaction for UEA, Con A and PHA. Non-neoplastic glands showed mild to moderate intensity and apical and/polar type of staining pattern for all lectins. Endocervical adenocarcinoma including minimal deviation adenocarcinoma (MDC) and adenocarcinoma well to moderately differentiated type showed diffuse cytoplasmic type of staining pattern for all lectins, but poorly differentiated adenocarcinoma of endocervix showed only a stromal pattern for all lectins. Endometrial hyperplasia and adenocarcinoma grades 1-3 showed positive reaction for all lectins except for DBA. The staining pattern of endometrial hyperplasia was variable, but adenocarcinoma grades 1-3 showed diffuse type. CONCLUSION: Intensity and staining patterns of lectins are helpful in distinguishing between endocervical and endometrial non-neoplastic and neoplastic lesions. Intense positive reaction of MDC, especially for Con A and PHA, can differentiate this lesion from normal endocervical glands. The stromal type of staining pattern of poorly differentiated endocervical adenocarcinoma can also have diagnostic significance. Negative reactions of DBA lectin for endometrial adenocarcinoma can be used for differentiating it from endocervical adenocarcinoma.

Adenocarcinoma↗
PubMed1974

Lectin binding and perturbation of the outer surface of the cell membrane induces a transmembrane organizational alteration at the inner surface.

Binding of Ricinus communis I agglutinin to the outer surface of resealed human erythrocyte ghosts results in an organizational perturbation that is translated to the inner membrane surface. The organizational change was detected by an enhancement in the chemical cross-linking of several erythrocyte membrane components by the bifunctional reagent, dimethyl malonimidate, resulting in their loss or reduction after sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the solubilized erythrocyte components. Of the components that failed to appear, or are reduced in amount, on the gels (protein bands Ia, Ib, IVa, and VII), two are known to be the subunits of spectrin (bands Ia and Ib), an inner-surface peripheral protein. A new band, which was identified as R. communis lectin, appeared on the polyacrylamide gels of lectin-treated ghosts with or without crosslinking. The loss of spectrin and other bands after lectin treatment and chemical crosslinking was due to a specific transmembrane event because: (a) beta-lactose, an inhibitor of R. communis agglutinin, prevented labeling of ghosts by the lectin and loss of spectrin and other erythrocyte components on gels after crosslinking; (b) use of inactive bifunctional or active monofunctional crosslinking reagents did not result in loss of spectrin or other components from lectin-treated ghosts; (c) the loss of spectrin and other components after lectin treatment and crosslinking was sensitive to temperature and lectin concentration; (d) no new bands appeared on the gels except for the band identified as R. communis agglutinin; (e) R. communis agglutinin does not interact with purified spectrin; and (f) previously published data indicate the R. communis lectin binds exclusively to the outer membrane surface while spectrin is located on the inner membrane surface. Perturbation of components of the outer membrane surface that can be translated to the cell interior by transmembrane linkages may provide a structural means of membrane communication that could be important in a variety of cellular control processes.

Binding Sites, Antibody↗
PubMed1995

C-terminal post-translational proteolysis of plant lectins and their recombinant forms expressed in Escherichia coli. Characterization of "ragged ends" by mass spectrometry.

Electrospray mass spectrometry was used to accurately measure the molecular masses of single chain lectins from legume seeds and also of three recombinant lectins, expressed in Escherichia coli. The five single chain lectins, Erythrina corallodendron lectin, soybean and peanut agglutinins, Dolichos biflorus lectin, and Phaseolus vulgaris hemagglutinin E, all showed evidence of C-terminal proteolytic processing, in some cases to "ragged" ends, when their masses were compared to those expected from their cDNA sequences and their known carbohydrate chains. Recombinant forms of the lectins from E. corallodendron, soybean, and peanut also showed C-terminal trimming, but not to the same points as the natural forms. Discrepancies between the protein and cDNA sequences of the E. corallodendron lectin were resolved by combined liquid chromatography-mass spectrometry peptide mapping and protein sequencing experiments, and the presence of a second glycosylation site was demonstrated. Our data show that all of these lectins undergo C-terminal proteolytic processing of a readily attacked peptide segment. This trimming is frequently imprecise, and the resulting heterogeneity may be a major contributor to the appearance of isolectin forms of these proteins.

Amino Acid Sequence↗
PubMed1999

A comparative study on the purification of the Amaranthus leucocarpus syn. hypocondriacus lectin.

Amaranthus leucocarpus lectin is a homodimeric glycoprotein of 35 kDa per sub-unit, which interacts specifically with N-acetyl-galactosamine. In this work, we compared different glycoproteins that contain Galbeta1-3 GalNAcalpha1-3 Ser/Thr or GalNAcalpha1-3 Ser/Thr in their structure as ligands to purify the A. leucocarpus lectin. From the glycoproteins tested, fetuin was the most potent inhibitor of the hemagglutinating activity and the better ligand for lectin purification; however, the use of desialylated stroma from erythrocytes represented the cheapest method to purify this lectin. O-linked glycans released from the glycoproteins used as affinity matrix and those from different erythrocytes were less inhibitory than parental glycoproteins. The NH2-terminal of the lectin is blocked; moreover, this is the only example of a lectin isolated from this genus to be a glycoprotein. Analysis of the glycoprotein sequences with inhibitory activity for the lectin, showed a different pattern in the O-glycosylation, which confirms that A. leucocarpus lectin recognizes conformation and, probably, distances among O-linked glycans moieties.

Amino Acid Sequence↗
PubMed1990

The Mel 14 antibody binds to the lectin domain of the murine peripheral lymph node homing receptor.

Murine and human leukocytes express surface glycoproteins, termed homing receptors (HRs), containing lectin-like, EGF-like (egf), and complement binding-like domains, that apparently endow these cells with the ability to home to peripheral lymph nodes (pln's) by virtue of an adhesive interaction with the pln postcapillary venule endothelium. The murine pln HR was initially characterized with a rat monoclonal antibody, Mel 14, that was specific for the murine form of the receptor. This work demonstrated that Mel 14 blocked the binding of murine lymphocytes to pln endothelium both in vitro and in vivo, a result consistent with the possibility that this monoclonal antibody recognizes a region of the HR that is involved with endothelium recognition and adhesion. In addition, this antibody also blocked the binding to the HR of PPME, a polyphosphomannan carbohydrate known to inhibit lymphocyte-pln endothelium interactions, suggesting that Mel 14 may recognize the lectin domain of the pln HR. Here we show that, while Mel 14 recognized truncated HR containing both the lectin and egf domains, antibody recognition was lost when the lectin domain alone was expressed. Chimeric molecules, in which regions of the lectin domain of the non-Mel 14-reactive human pln HR were replaced with homologous regions of the murine pln HR, demonstrated that the Mel 14 recognition site is within the NH2-terminal 53 amino acids of the lectin domain. These results suggest that the Mel 14 monoclonal antibody recognizes a determinant within the lectin domain of the pln HR whose conformation may be dependent upon the presence of the egf domain. Since Mel 14 efficiently blocks lymphocyte-endothelial interactions, these results support the hypothesis that the pln HR lectin domain may be directly involved with binding of lymphocytes to a carbohydrate ligand on the pln postcapillary venule endothelium.

Animals↗
PubMed1981

Lectin labeling of sprouting neurons. II. Relative movement and appearance of glycoconjugates during plasmalemmal expansion.

To study the dynamics of membrane components during neuritic growth, we carried out a series of pulse-chase experiments with ferritin-conjugated and unconjugated lectins on sympathetic neurons sprouting in vitro. Labeling of aldehyde-prefixed cultures with wheat-germ agglutinin or with the galactose-specific lectin of Ricinus communis is consistently dense near the distal end of the neurites. By contrast, if live cultures are labeled with these lectins and chased for 3-20 min, label-free plasmalemmal areas appear in the most peripheral regions of the growth cone, on filopodia and, furthermore, over vesicle clusters (SPVs). These marker-free areas, however, contain lectin receptors, as can be shown by relabeling the chased cultures with the same lectins after the aldehyde fixation. In a further set of experiments, cultures are labeled with a saturating concentration of native lectin, chased, aldehyde-fixed, and then relabeled with the ferritin conjugate of the same lectin. In this case, the surfaces of filopodia and of SPV clusters are selectively labeled with the ferritin conjugate, indicating the insertion of new lectin receptors into the plasma membrane in the growth cone periphery. These results indicate that plasmalemmal expansion in the neuron occurs by a mechanism of polarized growth, possibly involving SPVs as plasmalemmal precursor vesicles.

Animals↗
PubMed1995

Lectins inhibit the Aujeszky's disease virus-induced interferon-alpha production of porcine peripheral blood mononuclear cells.

The interaction between virus and peripheral blood mononuclear cells (PBMC) required to elicit the production of interferon-alpha (IFN-alpha) by the so-called natural interferon-producing cell is unknown. However, results from inhibition experiments suggest that viral glycoproteins are essential in this IFN induction process. We demonstrate here that cellular glycoproteins also appear to be involved in the initiation of IFN-alpha production. Lectins, that is, sugar binding glycoproteins, inhibited the Aujeszky's disease virus-induced IFN-alpha production of porcine PBMC by up to 99%. The level of inhibition varied with lectin used (concanavalin A, Galanthus nivalis lectin, Helix pomatia lectin, and lentil lectin). Preincubation experiments with porcine cells and concanavalin A (ConA) revealed that the lectin exerted its major effect directly on the PBMC. Although the IFN-alpha production in some cases was reduced by more than 90%, the PBMC were still able to proliferate in response to mitogenic lectins. The ConA-mediated inhibition of the IFN-alpha production was reduced if the lectin was added later than 6-8 h after the start of induction and was not mediated by soluble factors. Both orthovanadate and staurosporine inhibited the IFN-alpha production and did not relieve the ConA-mediated inhibition. Thus, ConA seems to interfere with the early events during IFN-alpha induction, but the mechanisms behind this interference could not be clarified.

Alkaloids↗
PubMed1996

ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins.

Based on sequence homologies with leguminous lectins, the intermediate compartment marker ERGIC-53 was proposed to be a member of a putative new class of animal lectins associated with the secretory pathway. Independent, a promyelocytic protein, MR60, was purified by mannose-column chromatography, and a cDNA was isolated that matched MR60 peptide sequences. This cDNA was identical to that of ERGIC-53 and homologies with the animal lectin family of the galectins were noticed. Not all peptide sequences of MR60, however, were found in ERGIC-53, raising the possibility that another protein associated with ERGIC-53 may possess the lectin activity. Here, we provide the first direct evidence for a lectin function of ERGIC-53. Overexpressed ERGIC-53 binds to a mannose column in a calcium-dependent manner and also co-stains with mannosylated neoglycoprotein in a morphological binding assay. By using a sequential elution protocol we show that ERGIC-53 has selectivity for mannose and low affinity for glucose and GlcNAc, but no affinity for galactose. To experimentally address the putative homology of ERGIC-53 to leguminous lectins, a highly conserved protein family with an invariant asparagine essential for carbohydrate binding, we substituted the corresponding asparagine in ERGIC-53. This mutation, as well as a mutation affecting a second site in the putative carbohydrate recognition domain, abolished mannose-column binding and co-staining with mannosylated neoglycoprotein. These findings establish ERGIC-53 as a lectin and provide functional evidence for its relationship to leguminous lectins. Based on its monosaccharide specificity, domain organization, and recycling properties, we propose ERGIC-53 to function as a sorting receptor for glyco-proteins in the early secretory pathway.

Amino Acid Sequence↗
PubMed1992

Peanut lectin: a mitogen for normal human colonic epithelium and human HT29 colorectal cancer cells.

BACKGROUND: The protein peanut agglutinin (PNA) is a galactose-binding lectin whose receptor, the Thomsen-Friedenreich (TF) blood-group antigen, shows increased expression in hyperplastic and neoplastic colonic epithelium. PURPOSE: Our hypothesis was that, under these conditions, increased lectin receptors could interact with dietary lectins, which would act as tumor promoters by stimulating cell proliferation. This study was designed to confirm whether active PNA is recoverable from feces after ingestion of peanuts and to assess the mitogenic effect of PNA on proliferation of epithelial cells in the colon. METHODS: Peanut lectin was extracted from feces by lactose-agarose affinity chromatography and was assayed for hemagglutinating activity. Cultured explants of histologically normal biopsy specimens of colonic mucosa from 31 patients were examined. Crypt cell production rate and incorporation of [3H]N-acetylglucosamine into mucin were assessed as indicators of proliferative and metabolic responses to PNA. In addition, we evaluated the separate and combined effects of PNA and epidermal growth factor (EGF) on cell proliferation in human HT29 colorectal cancer cells, by using tritiated thymidine incorporation and cell counts. RESULTS: Peanut lectin extracted from feces showed hemagglutinating activity toward desialylated red blood cells similar to that of a lectin preparation extracted from raw peanuts. Evaluation of biopsy specimens of normal colonic mucosa demonstrated that PNA at a concentration of 25 micrograms/mL caused statistically significant increases in crypt cell production (31% [mean] +/- 5% [SD]; P = .00005) and mucus synthesis (77% +/- 12%; P less than .000001). At 7.5-100 micrograms/mL, PNA was mitogenic for the HT29 colorectal cancer cell line. At 25 micrograms/mL, PNA alone produced a statistically significant increase in thymidine incorporation (44% [mean] +/- 3.7% [SD]; P = .002). For PNA in combination with EGF at 100 pg/mL, the increase was significantly greater (222% +/- 11.2%) than that for EGF alone (57% +/- 5%; P = .003). CONCLUSIONS: These results suggest that expression of the PNA receptor, TF antigen, by hyperplastic or neoplastic colonic epithelium may affect cell proliferation. IMPLICATIONS: It is possible that dietary lectins such as PNA, which bind to the TF antigen, promote cell proliferation and thus cancerous growth, while galactose-containing vegetable fiber would inhibit this effect by competing for binding by these lectins.

Arachis↗
PubMed1992

Carbohydrate-binding peptides from several anti-H(O) lectins.

Peptide fragments have been obtained from L-fucose-binding anti-H(O) lectins [Lotus tetragonolobus lectin (LTA) and Ulex europeus lectin I (UEA-I)] and di-N-acetylchitobiose-binding anti-H(O) lectins [Ulex europeus lectin II (UEA-II) and Laburnum alpinum lectin I (LAA-I)] by treatment with endoproteinase Asp-N or Lys-C. The peptide fragments were fractionated by affinity chromatography on a column of Fuc-Gel for LTA and UEA-I, and on a column of N-acetyl-D-glucosamine oligomer-Sepharose for UEA-II and LAA-I. The peptides with affinity for these columns were identified by peptide sequencing. All of these retarded peptides were found to be parts of the metal-binding regions of these lectins. It is strongly suggested that these peptides represent the carbohydrate-binding and metal ion-binding sites of legume lectins, respectively.

Amino Acid Sequence↗
PubMed1979

Purification and characterization of a lectin from rice bran.

A rice bran lectin was purified to homogeneity by precipitation with ammonium sulfate and chromatography on ovomucoid-Sepharose and CM-cellulose. The molecular weight of the dimer lectin was estimated to be around 37,000 by ultracentrifugation studies. The sedimentation coefficient was 3.8S. On Sepharose 6B gel filtration in the presence of 6 M guanidine-HCl, the lectin showed a molecular weight of 19,000. On reduction and carboxymethylation, the lectin further dissociated into two nonidentical subunits, with molecular weights of about 11,000 and 8,000. These subunits did not show hemagglutinating activity. Equilibrium dialysis experiments using N-acetyl-[1-14C]glucosamine indicated that about 1.8 mol of the sugar was bound to 19,000 g of the lectin. The lectin was mitogenic against mouse splenic lymphocytes and human peripheral lymphocytes. The lectin enhanced the rate of glucose oxidation and inhibited epinephrine-stimulated lipolysis in mouse adipocytes. Some characteristics of the lectin are compared with those of wheat germ agglutinin.

Acetylglucosamine↗
PubMed1984

Binding and cytotoxicity of Ricinus communis lectins to HeLa cells, Sarcoma 180 ascites tumor cells and erythrocytes.

The binding of Ricinus communis lectins to HeLa cells, Sarcoma 180 ascites tumor cells and human erythrocytes was studied in detail. Scatchard plots of binding of 125I-lectins to these cells gave biphasic lines except for HeLa cells at 0 degree C. The association constants of lectins for the three cell types at 37 degrees C were lower than those at 0 degree C. The numbers of total binding sites were estimated to be 7 to 16 X 10(7) per HeLa cell, 3 to 4 X 10(7) per Sarcoma 180 ascites tumor cell and 0.4 to 1 X 10(6) per erythrocyte. A fraction, 16 to 27% of the total amount of cell-bound lectin at 37 degrees C, appeared to be bound irreversibly as judged by non-removal on washing with 0.1 M lactose, whereas no lectin was irreversibly bound at 0 degree C. In the case of erythrocytes, no lectin became irreversibly bound even at 37 degrees C. The toxicity of lectins on HeLa cells and Sarcoma 180 ascites tumor cells was investigated. The toxicity of ricin D was 50 times for Sarcoma 180 ascites tumor cells and 140 times for HeLa cells as much as that for castor bean hemagglutinin. As to the sensitivities of both cell types to these lectins, it became apparent that Sarcoma 180 ascites tumor cells were more susceptible than HeLa cells.

Animals↗
PubMed1998

Lectins in the vulva. II. Vulvar intraepithelial neoplasia and squamous cell carcinoma.

This study used lectins as histologic probes to determine the cell surface oligosaccharide expression in different grades and types of vulvar intraepithelial neoplasia (VIN). Lectin binding patterns in metastasizing and non-metastasizing squamous cell carcinomas (SCCs) of the vulva were also compared to correlate lectin binding patterns with metastatic potential and other clinical/tumor characteristics. Twenty cases each of VIN epithelium, metastasizing SCC, and non-metastasizing vulvar carcinoma were randomly chosen from the pathology archives. Sixteen lectins were used to probe individual terminal oligosaccharide residues in formalin-fixed, paraffin-embedded tissue specimens from these cases through an indirect immunohistochemical technique. There were no differences in lectin binding patterns between the different histologic subtypes of VIN. In addition, there were no consistent differences between metastasizing and non-metastasizing primary tumors and no major differences in staining patterns between nodal metastases and the corresponding primary tumors. Furthermore, there was no identifiable correlation between lectin binding patterns and subsequent survival or local or regional recurrence; however, lectin staining of invasive tumor cells did appear to be related to local invasiveness. In addition, positive PNA binding was found to be a constant finding in each of the VIN and invasive SCC cases, confirming that the T-antigen becomes unmasked during the process of vulvar carcinogenesis. However, poorly-differentiated areas consistently showed absent lectin binding, suggesting loss of specific glycosyl transferase activities. In addition, the blood group "A" antigen appears to be lost during the process of tumorgenesis, although the blood group "O" antigen appears to be preserved.

Carcinoma in Situ↗
PubMed1995

The bark of Robinia pseudoacacia contains a complex mixture of lectins. Characterization of the proteins and the cDNA clones.

Two lectins were isolated from the inner bark of Robinia pseudoacacia (black locust). The first (and major) lectin (called RPbAI) is composed of five isolectins that originate from the association of 31.5- and 29-kD polypeptides into tetramers. In contrast, the second (minor) lectin (called RPbAII) is a hometetramer composed of 26-kD subunits. The cDNA clones encoding the polypeptides of RPbAI and RPbAII were isolated and their sequences determined. Apparently all three polypeptides are translated from mRNAs of approximately 1.2 kb. Alignment of the deduced amino acid sequences of the different clones indicates that the 31.5- and 29-kD RPbAI polypeptides show approximately 80% sequence identity and are homologous to the previously reported legume seed lectins, whereas the 26-kD RPbAII polypeptide shows only 33% sequence identity to the previously described legume lectins. Modeling the 31.5-kD subunit of RPbAI predicts that its three-dimensional structure is strongly related to the three-dimensional models that have been determined thus far for a few legume lectins. Southern blot analysis of genomic DNA isolated from Robinia has revealed that the Robinia bark lectins are the result of the expression of a small family of lectin genes.

Amino Acid Sequence↗
PubMed1989

Expression of rice lectin is governed by two temporally and spatially regulated mRNAs in developing embryos.

Two cDNA clones encoding rice lectin have been isolated and characterized to investigate the expression of rice lectin at the molecular and cellular levels. The two cDNA clones code for an identical 23-kilodalton protein which is processed to the mature polypeptide of 18 kilodaltons by co-translational cleavage of a 2.6-kilodalton signal sequence and selective removal of a 2.7-kilodalton COOH-terminal peptide which contains a potential N-linked glycosylation site. In addition, the mature 18-kilodalton lectin is post-translationally cleaved between residues 94 and 95 to yield polypeptides of 10 kilodaltons and 8 kilodaltons, corresponding to the NH2- and COOH-terminal portions of the mature subunit, respectively. RNA gel blot analysis established that rice lectin is encoded by two mRNA transcripts (0.9 kilobase and 1.1 kilobase). On DNA gel blots, the rice lectin cDNAs hybridize specifically to a single restriction fragment. In situ hybridization showed localization of the 1.1-kilobase rice lectin mRNA in root caps and specific cell layers of the radicle, coleorhiza, scutellum, and coleoptile. RNA gel blot analysis demonstrated that both the 0.9-kilobase and 1.1-kilobase mRNAs are present in developing rice embryos. The two lectin mRNAs are differentially expressed temporally such that the 1.1-kilobase lectin mRNA accumulates to levels twofold higher than the 0.9-kilobase mRNA.

Amino Acid Sequence↗
PubMed1988

A survey of lectin binding in Paramecium.

To better understand the general distribution of glycoproteins and the distribution of specific glycoprotein-bound sugar residues in Paramecium, a survey of the binding pattern of selected lectins was carried out in P. tetraurelia, P. caudatum, and P. multimicronucleatum. Lectins studied were concanavalin A (Con A), Griffonia simplicifolia agglutinins I and II (GS I and GS II), wheat germ agglutinin (WGA), Ulex europaeus (UEA I), peanut agglutinin (PNA), Ricinis communis toxin (RCA60) and agglutinin (RCA120), soybean agglutinin (SBA), Bauhinia purpurea agglutinin (BPA), Dolichos biflorus agglutinin (DBA), and Maclura pomifera agglutinin (MPA). Those giving the most distinctive patterns were Con A, GS II, WGA, UEA I, and PNA. No significant differences were found between the three species. Concanavalin A, a mannose/glucose-binding lectin, diffusely labeled the cell surface and cytoplasm and, unexpectedly, the nuclear envelopes. Events of nuclear division, and nuclear size and number were thus revealed. Both WGA and GS II, which are N-acetylglucosamine-binding lectins, labeled trichocyst tips, the cell surface, and the oral region, revealing stages of stomatogenesis. The lectin WGA, in addition, labeled the compartments of the phagosome-lysosome system. The lectin PNA, an N-acetyl galactosamine/galactose-binding protein, was very specific for digestive vacuoles. Finally, UEA I, a fucose-binding lectin, brightly labeled trichocysts, both their tips and body outlines. We conclude that a judicious choice of lectins can be used to localize glycoproteins and specific sugar residues as well as to study certain events of nuclear division, cellular morphogenesis, trichocyst discharge, and events in the digestive cycle of Paramecium.

Animals↗