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Reactivity of mucin-specific lectin from Sambucus sieboldiana with simple sugars, normal mucins and tumor-associated mucins. Comparison with other lectins.
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Mucin-specific lectin from Sambucus sieboldiana (SSA-M) reacts in Western blotting and ELISA with mucins from porcine stomach, bovine and ovine submaxillary glands, the human milk fat globule membrane, in vitro human ovarian, breast and colonic tumor cell lines, and mucins produced in vivo in the
Altered sialyl- and fucosyl-linkage on mucins in cystic fibrosis patients promotes formation of the sialyl-Lewis X determinant on salivary MUC-5B and MUC-7.
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Destruction of the lungs as a consequence of recurrent infections with microorganisms such as Pseudomonas aeruginosa remains the underlying cause of most morbidity and mortality in cystic fibrosis (CF). We have hypothesized that changes in the glycosylation of key tracheal mucins such as MUC5B and
Monoclonal antibodies reacting with the mucin-specific lectin from Sambucus sieboldiana (SSA-M).
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Monoclonal antibodies (MAbs) were prepared against the mucin-specific lectin from Sambucus sieboldiana (SSA-M). The majority of MAbs reacted with both free SSA-M and SSA-M bound to porcine mucin. However, MAbs SS16, SS18, and SS19 did not react with mucin-bound lectin, suggesting that these MAbs may
Mucin-specific bark lectin from elderberry Sambucus sieboldiana and its applications to the affinity chromatography of mucin.
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Three bark lectins were isolated from elderberry Sambucus sieboldiana using fetuin-Sepharose 4B and mucin-Sepharose 4B, and were studied comparatively for their binding to glycoprotein and to clarify various physicochemical features. For each, a unique pattern on isoelectric focusing was noted and
Reaction of various lectins to mucin derived from the different layers of rat gastric mucosa: comparison of enzyme-linked lectin binding assay with lectin histochemistry.
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The purpose of this study was to demonstrate that the histochemical staining reactivities of lectins in rat stomach actually represent the gastric mucins, and to estimate the utility of the lectins for mucin histochemistry. In this paper, the lectin histochemistry was compared with an enzyme-linked
Effects of PGE2 and of different synthetic PGE derivatives on the glycosylation of pig gastric mucins.
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The glycosylation of pig gastric mucins, discharged in response to prostaglandin (PG) E2 and to three synthetic PGE-derivatives (misoprostol, nocloprost, rioprostil) was compared. After a 20 h culture period in the absence or presence of 1 micromol/l of one of the PGs, mucins were isolated by gel
POMGNT1 Is Glycosylated by Mucin-Type O-Glycans.
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Protein O-linked mannose β1,2-N-acetylglucosaminyltransferase 1 (POMGNT1) is a Golgi glycosyltransferase that catalyzes the formation of the N-acetylglucosamine (GlcNAc) β1→2Man linkage of O-mannosyl glycan. POMGNT1 is not modified by N-glycans because there are no potential N-glycosylation sites;
Mucin-type O-glycans in tears of normal subjects and patients with non-Sjögren's dry eye.
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OBJECTIVE
O-linked carbohydrates (O-glycans) contribute to the hydrophilic character of mucins in mucosal tissues. This study was conducted to identify the repertoire of O-glycans in the tear film and the glycosyltransferases associated with their biosynthesis, in normal subjects and patients with
Membrane-bound mucins and mucin terminal glycans expression in idiopathic or Helicobacter pylori, NSAID associated peptic ulcers.
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OBJECTIVE
To determine the expression of membrane-bound mucins and glycan side chain sialic acids in Helicobacter pylori (H. pylori)-associated, non-steroidal inflammatory drug (NSAID)-associated and idiopathic-gastric ulcers.
METHODS
We studied a cohort of randomly selected patients with H. pylori
Identification of 9-O-acetyl-N-acetylneuraminic acid in normal canine pre-ocular tear film secreted mucins and its depletion in Keratoconjunctivitis sicca.
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O-Acetylated sialic acids have been reported in many sialoglycoproteins where they mediate a variety of immune and other biological events. We have previously demonstrated that the protective mucus barrier on the surface of the canine eye contains sialoglycoproteins. We have also investigated the
Lectin histochemical examination of rabbit bladder glycoproteins and characterization of a mucin isolated from the bladder mucosa.
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The glycocalyx of the mucosal surface of urinary bladder acts as an effective barrier against invasion by pathogenic microorganisms and injury from toxic substances in the urine. Defects in these bladder mucosal components could thus be important factors in the development of diseases such as
Novel interactions of complex carbohydrates with peanut (PNA), Ricinus communis (RCA-I), Sambucus nigra (SNA-I) and wheat germ (WGA) agglutinins as revealed by the binding specificities of these lectins towards mucin core-2 O-linked and N-linked glycans and related structures.
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Plant lectins through their multivalent quaternary structures bind intrinsically flexible oligosaccharides. They recognize fine structural differences in carbohydrates and interact with different sequences in mucin core 2 or complex-type N-glycan chain and also in healthy and malignant tissues. They
The use of mucin-specific monoclonal antibodies and lectins in the detection of tumor-associated serum markers in gynecological cancer.
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The use of the mucin-specific lectin from Sambucus sieboldiana (SSAM) in the detection of tumor-associated serum antigens produced by patients with ovarian, cervical, and uterine cancer was investigated. Two-site assays were developed which used either SSAM or the MUC1 core protein-specific
Distribution of sialic acids on mucins and gels: a defense mechanism.
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Moist mucosal epithelial interfaces that are exposed to external environments are dominated by sugar epitopes, some of which (e.g., sialic acids) are involved in host defense. In this study, we determined the abundance and distribution of two sialic acids to assess differences in their availability
[Different receptor specificity of influence viruses from ducks and chickens and its reflection in the composition of sialosides on host cells and mucins].
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The ability of influenza viruses from different hosts to bind to the intestinal epithelium of various birds (Anseriformes (Anatidae), Galliformes, Charadriiformes (sandpipers and sea gulls), Ciconiiformes (storks), Podicipediformes (grebes), and Gruiformes was studied. The composition of
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