Disease relevance of BSM

• The data also indicate that haemagglutination-inhibition (HI) by RMG and BSM and most likely virus attachment to cell surfaces involves binding of influenza C virus to Neu5,9Ac2 [1].
• Using a solid-phase binding assay, we further demonstrated that the ability of reovirus type 3 or reassortant 1HA3 and the inability of reovirus type 1 or reassortant 3HA1 to bind avidly to BSM was a property of the viral S1 genome segment and required the presence of sialic acid residues on BSM oligosaccharides [2].
• Bovine salivary mucin (BSM) inhibits rotavirus replication in vitro and in vivo [3].
• The inhibitory effect of BSM in vitro is abolished by Arthrobacter ureafaciens neuraminidase but not by Clostridia perfringens neuraminidase; it is abolished by mild base deacetylation but not by influenza C acetylesterase [3].
• One IgM(K) monoclonal antibody derived from peripheral blood lymphocytes of a patient with a lung adenocarcinoma was generated with binding reactivity for bovine submaxillary mucin (BSM) [4].

High impact information on BSM

• Two of the MAbs, designated Mu-2 and Mu-4, recognized a CSAp determinant containing sialic acid, and this epitope was also expressed on bovine submaxillary mucin (BSM) [5].
• After inactivation, RMG and BSM were found to contain reduced amounts of N-acetyl-9-O-acetylneuraminic acid (Neu5,9Ac2) and increased amounts of N-acetylneuraminic acid (Neu5Ac) [1].
• Monosaccharides present on human glycophorin A, neuraminyl lactoses, bovine and porcine submaxillary mucins (BSM and PSM), and hyaluronic acid as well as proteoglycan N-linked glycosidase F(PNGaseF)- and sialidase A-treated human erythrocyte glycoproteins (hEGP) and human erythrocytes were all tested for inhibitory potential in the rosetting assay [6].
• However, Iso relaxations in porcine/bovine BSM were significantly suppressed by inhibitors of the internal Ca(2+) pump (cyclopiazonic acid; 10(-5) M) or of myosin light chain phosphatase (calyculin; 10(-6) M) [7].
• Northern analysis of submaxillary gland RNA with the BSM421 probe detected multiple messages of BSM with sizes from 1.1 to over 10 kb [8].

Chemical compound and disease context of BSM

• The data suggest that SA11 rotavirus binds to a specific sialic acid structure on BSM different from the sialic acids recognized by other viruses [3].

Biological context of BSM

• A number of cDNA fragments coding for bovine submaxillary mucin (BSM) were cloned, and the nucleotide sequence of the largest clone, BSM421, was determined [8].
• When we treated bovine submaxillary mucin (BSM) with influenza C virus, we observed a dramatic increase in its potency as an inhibitor of RV3 hemagglutination [9].
• The substrate specificity was examined using the natural substrate bovine submaxillary mucin (BSM) and/or synthetic substrates p-nitrophenylacetate (p-NiA) and alpha-naphthylacetate (alpha-NA) and compared with several strains of MHV and influenza viruses [10].
• Unusually marked mitotic reaction, unaffected by parasite age and origin, was recorded in the B-cell line, BSM, also without commensurate count increase, indicating that induced mitosis resulted in cell loss [11].
• At the low ionic strength < or = 0.2 mol x L(-1) and pH 7.0, the BSM-R8 interaction was exceedingly complex, hydrogen bonds, hydrophobic interaction and electrostatic forces were involved in the interaction between R8 and BSM, the binding sites of BSM bound R8 were markedly increased [12].

Anatomical context of BSM

• The development of cultured rabbit preimplantation embryos grown in standard media (Ham's F-10 or BSM II supplemented with bovine serum albumin (BSA) or homologous serum) or in Ham's medium supplemented with uterine flushings was compared [13].
• BSM inhibits the adhesion of lymphocytes when coimmobilized with intercellular adhesion molecule-1 (ICAM-1) and blocks the activation of T lymphocytes when coimmobilized with anti-CD3 [14].
• 3. Although produced from a fusion that used splenocytes from donor mice immune to bovine salivary mucin (BSM), EG2.3 bound selectively to a number of human tumor cell lines including colon adenocarcinoma LS174T [15].
• AIM: To determine the thermodynamics of binding reaction of arginine oligomer (R8) to bovine submaxillary mucin (BSM) in order to provide the foundation for understanding the influence of mucin on transport of macromolecules through mucosa mediated by arginine oligomer [12].

Associations of BSM with chemical compounds

• We examined the mechanisms underlying relaxations evoked by isoproterenol (Iso) in isolated porcine, bovine, or human tracheal and bronchial tissues (TSM and BSM, respectively) [7].
• Exoglycosidase digestion of BSM showed that 6G9 recognized Sia as a nonreducing monosaccharide but neither Gal nor GlcNAc [16].
• On the other hand, desialization of BSM and OSM largely abolished their aggregating capability towards S. rattus BHT [17].
• Multicellular capsules formed around Sepharose conjugated to galactose-rich molecules such as PSM, asialo-PSM, asialo-fetuin or asialo-BSM were highly significantly thicker than those formed around control untreated beads, whereas capsules around BSA, fetuin or BSM conjugates were significantly thinner [18].
• One assay used p-nitrophenyl acetate (PNPA) as substrate and detected serine-esterase activity; the second assay monitored AE function with bovine submaxillary mucin (BSM) as substrate [19].

Other interactions of BSM

• The antibody bound to ovine and bovine submaxillary mucins (OSM and BSM) [20].
• However, pure PRP-1 adsorbed in similar amounts to both hydrophilic and hydrophobic surfaces in the concentration range investigated and BSM adsorbed in larger amounts at high concentrations on hydrophilic surfaces [21].
• The film VCD results on AGP and BSM suggested that the secondary structures of polypeptide fold in the film state are similar to those in the solution [22].
• For comparable concentrations, PRP-1 was found to have a more pronounced lubricating effect than BSM, which in turn showed a higher lubricity than statherin [23].
• The hemagglutination activities of the lectins were effectively inhibited by bovine and porcine submaxillary mucins (BSM and PSM), and NH2-terminal glyco-octapeptides obtained by cyanogen bromide cleavage of human erythrocyte glycophorin A [24].

Analytical, diagnostic and therapeutic context of BSM

• Western blots performed with anti-TML monoclonal antibodies revealed bands identical with those in the silver-stained gels, suggesting homogeneity of the BSM -Sepharose-purified lectin [25].
• The BSM-based ELISA holds great promise as a serodiagnostic and prognostic assay for VL [26].
• Hemagglutination (lectin) activity was partially purified from sporozoite lysates by affinity chromatography with BSM coupled to Sepharose-4B [27].
• Oligosaccharide-alditols released from BSM by alkaline borohydride treatment were separated into three acidic (A-1-A-3) and five neutral (N-1-N-5) oligosaccharide-alditol fractions by liquid chromatography on columns of an ion-exchange resin and Bio-Gel P-4 [28].
• Vibrational circular dichroism (VCD) spectra for the glycoproteins alpha1-acid glycoprotein (AGP) and bovine submaxillary mucin (BSM), have been measured in D2O solutions and for the films prepared from aqueous (H2O) buffer solutions in the 1800 to 900 cm(-1) region [22].

References