SIX BALB/c IgA MYELOMA PROTEINS THAT BIND ß-(1 → 6)-<scp>D</scp>-GALACTAN

Rudikoff, Stuart; Mushinski, Elizabeth B.; Potter, Michael; Glaudemans, Cornelis P.J.; Jolley, Michael E.

doi:10.1084/jem.138.5.1095

Cited by 45 publications

(13 citation statements)

References 30 publications

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“…Proteins that bind /3(1 -6)-D-galactan are especially intriguing since they show similar sequences in both their heavy and light chains (10,12,13) . Perhaps the most pertinent to the present study, since they arose in genetically different individuals, are the human monoclonal cold agglutinins and antigamma globulins studied by Kunkel, Capra, and their colleagues (44,45) .…”

Section: Discussionmentioning

confidence: 99%

“…Amino-terminal sequence analysis was performed on a Beckman 890 C sequencer (Beckman Instruments, Inc., Spinco Div., Palo Alto, Calif.) using the standard dimethylallylamine program. Thiazolinone derivatives obtained after each degradation cycle were converted to phenyltbiohydantoins (PTH) as previously described (13) . PTH amino acids were identified by gas chromatography on SP400 columns (28) and/or by amino acid analysis after hydrolysis in hydriodic acid (29) .…”

Section: Methodsmentioning

confidence: 99%

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Structural, functional, and idiotypic characteristics of a phosphorylcholine-binding IgA myeloma protein of C57BL/ka allotype.

Claflin¹,

Rudikoff²,

Potter³

et al. 1975

The Journal of Experimental Medicine

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An IgA phosphorylcholine (PC)-binding myeloma protein with IgCH allotypic determinants different from those of BALB/c mice is characterized. The myeloma, CBPC 2, was induced in the CB-20 strain of mice which is congenic to BALB/c but differs from it by carrying the A15 allotypic determinant of C57BL/ka mice. Sequence analysis of the CBPC 2 light chain through the first hypervariable region, as well as isoelectric point analysis, show that this chain is indistinguishable from that of T15, a PC-binding myeloma protein of BALB/c origin. The heavy chains of CBPC 2 and T15 differ by only two amino acids (positions 14 and 16) through the first hypervariable region. As measured by inhibition of precipitation, both CBPC 2 and T15 have the same specificity for PC, glycerophosphorylcholine, acetylcholine, and choline. In addition, CBPC 2 possesses the binding site-associated idiotypic determinant which is present on T15. However, like normal or induced C57BL/6 anti-PC antibody, it does not possess the nonbinding site idiotypic determinant.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Structural, functional, and idiotypic characteristics of a phosphorylcholine-binding IgA myeloma protein of C57BL/ka allotype.

Claflin¹,

Rudikoff²,

Potter³

et al. 1975

The Journal of Experimental Medicine

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“…These proteins have been studied in detail with respect to structure and hapten-binding [78]. Structural studies show that all belong to the same VK and VH isotype group [V~c-4, VH-1B], but the diversity of this group is shown by differences in the fluorescence changes resulting from interaction with hapten [62].…”

Section: Vh-gal[67]mentioning

confidence: 99%

The genetic control of antibody variable regions in the mouse

Weigert¹,

Riblet²

1978

Springer Semin Immunopathol

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The genetic control of the variable (V) 1 regions of mouse antibodies is being analysed at several levels. The direct chemical analysis of V-region genes is underway [87]; antibody V-genes have been isolated from the D N A of differentiated and undifferentiated mouse cells and are now being sequenced. These studies already provide support for the conclusions based on analysis of amino acid sequences of V-regions and the genetic analysis of V-region genes using markers such as idiotype. In this chapter, we will concentrate on what has been learned from the latter kinds of studies such as the approximate size of VL and V H loci, the organization of VH genes and the relationship of V-region and C-region loci. Our purpose will be to bring to date the information on mouse V regions from a variety of sources using as a basis several recent reviews of this field by Eichmann [27], M~ikel~i and Karjalainen 1-59], Potter [74] and the summaries of the H o m o g e n e o u s Immunoglobulin Workshops [90].V-region genetic studies in the mouse owe their rapid development to two systems: the first of these is the mouse plasmacytoma developed by Michael Potter and co-workers. As Melvin Cohn points out, "The mouse system bears the stamp of Michael Potter who systematically developed the methods for provoking and characterizing mouse myelomas and who established a collection of cell lines which are to this field what the T-phages were to molecular biology" [24]. These plasmacytomas have been the source of the homogeneous antibodies used for ~-To whom offprint requests should be sent 1 Antibody structures will be abbreviated throughout this review as follows: the variable regions (V) o f heavy and light chains, VH and VL, and their constant regions, CH and CL. The structures as they relate to types of antibody subunits are abbreviated as V~c and CK (kappa chain) and VZ (lambda chain), V~c-t, etc.; VH-1, etc. (kappa or heavy chain variable region isotype), CH-y2a, etc. (heavy chain constant region isotype)The abbreviations for the gene or locus controlling these structures are for V-regions: Vh, V~c, and V2, for C regions of light chains, C~c and C2; and for heavy chains, the entire locus is designated Ch and specific genes, Ig-1 to Ig-6 according to ref. [34] 0344-4325/78/0001/0133/$ 7.40

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“…Results mRNAsfrom an IgA-producing plasmacytoma encode two a chains The BALB/c plasmacytoma, XRPC 24, synthesizes and secretes IgA(x) which has anti-:-(1 -6)-D-galactan activity (Rudikoff et al, 1973). Immunofluorescent analysis of XRPC 24 cell membrane Ig using anti-IgA revealed a low but 15 16 ( MM , 92fK: (15,16) of a sucrose gradient was translated in a rabbit reticulocyte lysate system containing [35S]methionine.…”

Section: Introductionmentioning

confidence: 99%

The murine immunoglobulin alpha gene expresses multiple transcripts from a unique membrane exon.

Word¹,

Mushinski²,

Tucker³

1983

The EMBO Journal

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Immunoglobulin heavy chains of each class exist in two forms, membrane (m) and secreted (s), which have different carboxy‐terminal sequences encoded by different gene segments. We have sequenced the DNA spanning the coding region for the carboxy‐terminal end of the alpha m chain in a BALB/c genomic clone and have examined alpha mRNA expression in transformed and normal B cells. Unlike the other murine heavy chain genes, which have two membrane exons (M1 and M2), the alpha gene has only one membrane exon (alpha M1). This unusual exon encodes a highly conserved transmembranal peptide plus flanking amino acids singular to IgA. The complexity of the alpha gene transcription is also unusual. Downstream of alpha M1, three AATAAA hexanucleotides are used to terminate as many as six distinct alpha membrane mRNAs. These appear to differ only in length and splicing pattern of their 3′‐untranslated regions, and thus, encode the same alpha m protein. The alpha s protein is approximately 4000 daltons smaller than alpha m as judged by in vitro translation and is coded by a single 2.0‐kb alpha s mRNA. We propose that the expression of alpha s and the multiple alpha m mRNAs is differentially controlled at the level of transcriptional termination.

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SIX BALB/c IgA MYELOMA PROTEINS THAT BIND ß-(1 → 6)-D-GALACTAN

Cited by 45 publications

References 30 publications

Structural, functional, and idiotypic characteristics of a phosphorylcholine-binding IgA myeloma protein of C57BL/ka allotype.

Structural, functional, and idiotypic characteristics of a phosphorylcholine-binding IgA myeloma protein of C57BL/ka allotype.

The genetic control of antibody variable regions in the mouse

The murine immunoglobulin alpha gene expresses multiple transcripts from a unique membrane exon.

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