Immunochemical and biochemical study of a human Fcμ fragment (μ‐chain disease)

Lebreton, Jean‐Pierre; Ropartz, C; Rousseaux, J.; Roussel, Philippe; Dautrevaux, M; Biserte, G

doi:10.1002/eji.1830050306

Cited by 18 publications

(6 citation statements)

References 34 publications

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“…He died 3 1/2 months after the diagnosis was made. The p-heavy chain fragments from five patients (cases 1, 7, 8, 11, and 26) have been subjected to detailed chemical analysis by Franklin et al [30], Bakhshi et al [24], Barnikol-Watanabe et al [31], Mihaesco et al [32], Mihaesco et al [33], Lebreton et al [34,35], and Roussel et al [36]. Figure 1 depicts the structure of these five p H C D proteins compared with the normal p-heavy chain.…”

Section: Discussionmentioning

confidence: 99%

μ‐heavy chain disease: Presentation as a benign monoclonal gammopathy

Wahner‐Roedler

Kyle

1992

American J Hematol

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mu-Heavy chain disease (HCD) is a rare monoclonal lymphoid disorder characterized by the failure to assemble a complete IgM immunoglobulin. The mu-heavy chains analyzed to date revealed absence of the variable region and a shortened constant domain. We report the first case of mu-HCD presenting as a benign monoclonal gammopathy. The literature on the 27 reported mu-HCD cases is reviewed, and important clinical and laboratory findings are discussed. The ages of the patients ranged from 15 to 80 years (median, 57.5 years). Twenty-two of 27 patients had an associated lymphoplasma cell proliferative disorder. A monoclonal spike on routine serum protein electrophoresis was found in only 8 of 19 patients. Fourteen of 22 patients had Bence Jones proteinuria, but mu-HCD protein was reported in the urine of only two patients. The survival ranged from less than 1 month to 11 years (median, 24 months).

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Section: Discussionmentioning

confidence: 99%

μ‐heavy chain disease: Presentation as a benign monoclonal gammopathy

Wahner‐Roedler

Kyle

1992

American J Hematol

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“…The tryptic peptides t-1 to t-5 are all overlapped by the chymotryptic peptide ch-2; t-5 and t-6 are (1) 0.67 (1) 1.98 (2) 3.27 (3) 0.87 (1) 2.31 (2) 0.68 (1) 0.99 (1) 2.00 (2) 14 0.023 Asp n.d. ch-2 1.91 (2) 2.06 (2) 1.31 (1) 1.04 (1) 6.37 (6) 2.02 (2) 1.56 (2) (1) 0.76 (1) 0.63 (1) 0.96 ( overlapped by ch-3, partially also by peptides t-1 + 2 and t-3 + 4. Therefore, the order of the tryptic peptides in fragment F4 could be established unequivocally (Fig.…”

Section: Amino-acid Sequence Determination Of the Cyanogen-bromide Frmentioning

confidence: 93%

“…V8-3 appeared to consist of T20 and the last 4 C-terminal residues of Τ19, corresponding to Pos. 227 to 238 of μ-chain + 20 0.80 (1) 1.06 (1) 1.09 (1) 1.98 (2) 3.32 (3) 4.61 (5) 1.13 (1) 4.73 (5) 0.92 (I) 1.12 (1) 1.02 (1) 22 78.02 blocked T20 1.02 (1) 0.91 (1) 2.14 (2) 2.85 (3) 0.99 ( 1.58 (2) 1.02 (1) 0.58 (1) 0.98 (1) 1.76 (2) 1.27 (1) 1.45 (1) 1.07 (1) 1.04 (1) 0.83 (1) 0.94 (1) 1.02 (1) 14 13.53 Lys T24 1.08 (1) 0.72 (1) 0.79 (1) 0.74 (I) 0.90 (1) 0.84 (1) 1.06 (1) 1.03 (1) 0.96 (1) 1.25 (1) 1.63 (2) 1.11 (1) 2.38 (2) 1.00 (1) 4.67 (5) 3.43 ( (1) 1.65 (2) 0.84 (1) 0.98 (1) 1.06 (1) 6 7.914 Lys T29 0.94 …”

Section: Tryptic Peptides From Cyanogen-bromide Fragment F3-1mentioning

confidence: 96%

“…21 and 35 had been determined by analysis of their DABTH-amino-acid derivatives in the microEdman degradation procedure. (1) 0.91 (1) 1.28 (1) 2.00 (2) 3.09 (3) 0.99 (1) 2.01 (2) 0.98 (1) 0.88 (1) 1.00 (1) 0.83 (1) 0.95 (1) 1.82 (2) 0.75 (1) 2.25 (2) 5.28 (6) 1.02 (1) 2.36 (2) 1.07 (1) 1.09 (1) 1.12 (1) 1.88 ( …”

Section: Tryptic Pep Tides From Cyanogen-bromide Fragment F4mentioning

confidence: 96%

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The Primary Structure of μ-Chain-Disease Protein BOT. Peculiar Amino-Acid Sequence of the N-Terminal 42 Positions

Barnikol-Watanabe¹,

Mihaesco²,

Mihaesco³

et al. 1984

Hoppe-Seyler´s Zeitschrift für physiologische Chemie

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The complete primary structure of the mu heavy-chain disease (mu-HCD) protein BOT has been determined. The monomeric HCD-mu-chain consists of 391 amino-acid residues, lacking the VH and mu CH1 domains but including the entire CH2, CH3 and CH4 domains (349 residues). The sequence of the preceding 42 N-terminal residues which we designate as the "pre-C-part" presents no homology to any known variable or constant immunoglobulin sequence, but contains an internal homology of positions 10-19 to positions 20-29. The origin of the "pre-C-part" structure and the deletion of the mu CH1 domain of protein BOT are discussed.

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“…6) normal sequence resumes at the very beginning of the CH2 domain. It should be stressed that in the two other p-chain-disease proteins with available structural data, the resumption of normal sequence occurs at the beginning of CH1 for protein GLI [8] and CH3 for protein BUR [9]. (b) There are no peptides found in protein BOT implicated in insertions in the constant part or extending beyond the carboxy-terminal sequence of the p-chain GAL.…”

Section: 1mentioning

confidence: 99%

The Primary Structure of the Constant Part of μ‐Chain‐Disease Protein BOT

Mihaesco

Barnikol-Watanabe

Barnikol

et al. 1980

European Journal of Biochemistry

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The complete primary structure of the constant part of the p-chain-disease protein, BOT, was established. It includes the whole CH2, CH3 and CH4 domains. Two amino acid changes were found, at positions 309 (Ser -+ Gly) and 333 (Val ---f Gly) (GAL numbering). In two additional monoclonal p chains (SCO and CO), the same positions showed an amino acid variability. From these data it may be concluded that four types of p chains exist in the human: (1) GAL type with Ser-309 and Val-333; (2) OU type with Gly-309 and Val-333; (3) SCO type with Ser-309 and Gly-333; (4) BOTjCO type with Gly-309 and Gly-333. The meaning of this molecular polymorphism is discussed.The complete primary structure of the human IgM molecules is now established for two monoclonal proteins GAL and OU [l, 21. The amino acid sequence of their constant parts are essentially the same. The only exception was a residue change at position 309, serine in protein GAL compared to glycine in protein OU. The sequence determination of the Fc regions of four additional monoclonal IgM proteins [3] as well as the (Fc)Sp fragment of a pool of normal polyclonal IgM [4] suggested a lack of variability of the constant part of the human p chain. During the studies made by two of us on the covalent structure of a deleted p-chain protein (BOT) [5], we have described a limited number of amino acid changes restricted to the constant region as compared with the known reference p-chain sequences. Protein BOT is a p-chaindisease protein, which lacks light chains and consists of incomplete heavy chains. The p-chain disease appears to be relatively rare : 15 cases have been reported since its first description [6] in contrast with the 50 y-heavychain diseases and the 150 a-chain diseases presently known to us [7]. Only scare structural data are available on p-chain-disease proteins (GLI, BUR, BOT) [X-lo]. Our present work had two aims: first, to establish the precise amino acid sequence of protein BOT and to look for its homology to those of the presently known complete p chains (GAL and OU) ; second, to examine several monoclonal human IgMs in order to find out if the constant domains of Our results show that the structural homology of protein BOT implicates the CH2, CH3 and CH4 domains. However, in the two positions (309 and 333) different amino acid residues were found in contrast to p-chain GAL: 309 = Ser -+ Gly and 333 = Val + Gly. We also present the amino acids found at the same position in two other monoclonal p chains (SCO and CO). MATERIALS AND METHODS ProteinsThe isolation and purification of protein BOT was previously described [lo]. The proteins SCO and CO are monoclonal IgM from patients with Waldenstrom's macroglobulinemia. The methods used for their isolation and purification were : (a) gel filtration chromatography on Sepharose 6B in 0.1 M Tris/HCl pH 8.0, 1 M NaCl; (b) zone electrophoresis of the 19-S peak on a Pevikon block. Reduction and CurhoxymethylutionThe mild reduction of proteins BOT, SCO and CO was performed as described previously [5]. In order to...

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Immunochemical and biochemical study of a human Fcμ fragment (μ‐chain disease)

Cited by 18 publications

References 34 publications

μ‐heavy chain disease: Presentation as a benign monoclonal gammopathy

μ‐heavy chain disease: Presentation as a benign monoclonal gammopathy

The Primary Structure of μ-Chain-Disease Protein BOT. Peculiar Amino-Acid Sequence of the N-Terminal 42 Positions

The Primary Structure of the Constant Part of μ‐Chain‐Disease Protein BOT

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