Structural studies of the asparagine-linked sugar chains of two immunoglobulin M's purified from a patient with Waldenström's macroglobulinemia

Ohbayashi, Hirokazu; Endo, Tamao; Mihaesco, Edith; Gonzales, Mercedes G.; Kochibe, Naohisa; Kobata, Akira

doi:10.1016/0003-9861(89)90130-6

Cited by 19 publications

(10 citation statements)

References 39 publications

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“…G2, G2F and GN2FB were obtained from lipocalin‐type prostaglandin D synthase purified from human urine by hydrazinolysis and derivatized by 2AB as described above [16]. G3 was obtained from fetuin [17], and M9 and M5 were obtained from human IgM [18], respectively. M3 and M3F were obtained by digestion of G2 and G2F with a mixture of diplococcal β‐galactosidase and β‐ N ‐acetylhexosaminidase, respectively.…”

Section: Methodsmentioning

confidence: 99%

Analysis of N‐glycans of pathological tau: possible occurrence of aberrant processing of tau in Alzheimer's disease

et al. 2001

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In a previous study Nat. Med. 2, 871^875], Wang et al. found (i) that abnormally hyperphosphorylated tau (AD P-tau) isolated from Alzheimer's disease (AD) brain as paired helical filaments (PHF)-tau and as cytosolic AD P-tau but not tau from normal brain were stained by lectins, and (ii) that on in vitro deglycosylation the PHF untwisted into sheets of thin straight filaments, suggesting that tau only in AD brains is glycosylated. To elucidate the primary structure of N-glycans, we comparatively analyzed the N-glycan structures obtained from PHF-tau and AD P-tau. More than half of N-glycans found in PHF-tau and AD P-tau were different. High mannose-type sugar chains and truncated Nglycans were found in both taus in addition to a small amount of sialylated bi-and triantennary sugar chains. More truncated glycans were richer in PHF-tau than AD P-tau. This enrichment of more truncated glycans in PHF might be involved in promoting the assembly and or stabilizing the pathological fibrils in AD. ß 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

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Section: Methodsmentioning

confidence: 99%

Analysis of N‐glycans of pathological tau: possible occurrence of aberrant processing of tau in Alzheimer's disease

et al. 2001

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“…IgAl and IgA2 myeloma proteins. Thoroughly dried IgAl myeloma protein (Car, 4.7 mg) and IgA2 myeloma protein (Fel, 3.5 mg) were suspended in 0.5 ml of anhydrous hydrazine and subjected to hydrazinolysis at 100°C for 9 h. Released oligosaccharides were N acetylated and purified as described previously (25,28). One portion of the oligosaccharide fractions was reduced with NaB3H4 (0.4 mCi; New England Nuclear Corp., Boston, Mass.)…”

Section: Structural Analysis Of Asparagine-linked Oligosaccharides Ofmentioning

confidence: 99%

“…The rest was reduced with NaBH4 (2 mg) for methylation analysis. All other experimental procedures were the same as described earlier (25,28).…”

Section: Structural Analysis Of Asparagine-linked Oligosaccharides Ofmentioning

confidence: 99%

Secretory immunoglobulin A carries oligosaccharide receptors for Escherichia coli type 1 fimbrial lectin

et al. 1990

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Type 1 fimbriae with mannose-specific lectins are widely distributed among members of the family Enterobacteriaceae and confer the ability to attach to a range of host cells, including colonic epithelial cells. The mucosal surfaces are protected by secretory immunoglobulin A (IgA), which agglutinates microorganisms and prevents their attachment to host epithelial cells. This action has been attributed to a specificity of the antigen-combining site of mucosal immunoglobulins for bacterial and viral surface components. Here, we report a novel mechanism for the antibacterial effect of secretory IgA. Secretory IgA and IgA myeloma proteins, especially those of the IgA2 subclass, were shown to possess carbohydrate receptors for the mannose-specific lectin of type 1-fimbriated Escherichia coli. The presence of the high-mannose oligosaccharide chain Manal-6(Manal-3)Manxl-6(Manal-3)Man,ll-4GlcNAcIl-4GlcNAc correlated with binding activity. The interaction between bacterial mannose-specific lectins and IgA receptor oligosaccharide resulted in agglutination of the bacteria and in inhibition of bacterial attachment to colonic epithelial cells. Thus, this interaction could form the basis for a broad antibacterial function of secretory IgA against enterobacteria regardless of the specificity of antibody molecules.

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“…IgMl and lgM2. Although other biclonal gammapalhies have been analysed [19] a detailed analysis involving a comparison of the IgMs at structural and functional level has nol been previously reported. IgMl is a cryoglobulin and lgM2 showed reactivity against intermediate lilamenl proteins.…”

Section: Discussionmentioning

confidence: 99%

“…In addition to gene rearrangement it has been indicaicd [23] that point mutations can occur within assembled immunoglobulin gcne.s, to further expand antibody diversity. Our results suggest that IgMl and IgM 2 may arise from two B clones, wilh a common precursor, after several mutations, since both contain the heavy chains of the same subgroup (subgroup HI) [24] and the same lambda liglit chains (subgroup II, variant BUR) [18,19]; bul they differ in several amino acids. !n this way it has been shown that the frequency of mutations that accumulate wilhin an expanding clone of B cell is much higher than that of other somatic mutations [24], This alteration of several amino acids may result in a change of antibody aetivity like that indicated in the present study.…”

Section: Ttic Wm Igmi Antibodies Reaet With Smooth Musclementioning

confidence: 99%

The structure of two IgMs showing different activity from a patient with Waldenstrom's macroglobulinaemia

Méndez¹,

Osuna

Sánchez

et al. 1992

Clinical and Experimental Immunology

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SUMMARYThe two monoclonal IgMs (IgM I and lgM2) were characterized from a patient with Waldenstrom's macroglobulinaemia that rcsullcd in a gamniapathy. Heavy and light chains were isolated from Ihe IgM. The complete primary structure ofthe two light chains and the NH;-tcrminal region of the iwo heavy chain molecules were determined. The sequence dala indicated that the heavy and light chains from bolh IgMs belong to the same (III and II) lambda subgroups. By testing their antibody activity it was found by imtiiunonuorescencc and immunoblotting that only IgM2 reacts with an intermediate filament protein.

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Structural studies of the asparagine-linked sugar chains of two immunoglobulin M's purified from a patient with Waldenström's macroglobulinemia

Cited by 19 publications

References 39 publications

Analysis of N‐glycans of pathological tau: possible occurrence of aberrant processing of tau in Alzheimer's disease

Analysis of N‐glycans of pathological tau: possible occurrence of aberrant processing of tau in Alzheimer's disease

Secretory immunoglobulin A carries oligosaccharide receptors for Escherichia coli type 1 fimbrial lectin

The structure of two IgMs showing different activity from a patient with Waldenstrom's macroglobulinaemia

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