Deux nouveaux facteurs dans les syst�mes h�r�ditaires de gamma-globuline: Le Gm(e) et l�Inv(l)

Ropartz, C; Rivat, L; Rousseau, Philippe

doi:10.1159/000426587

Cited by 19 publications

(26 citation statements)

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“…More than 99 per cent of Europeans are either Inv(a+l+) or Inv(a-1-) (32). The current hypothesis has been that Inv(a) and Inv0) are formed by one and the same gene, Inv ~l (32). The findings on the anti-Rh antibodies of three Inv(a+l+) sera (see Results) suggest that Inv(a) and Inv(1) occur in separate molecules and therefore that they are formed by different genes.…”

Section: Anti-rh Antibodies and Their Properties As Components In The Gmmentioning

confidence: 91%

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ON THE RELATIONSHIPS BETWEEN THE γ-GLOBULIN GENES OF THE GM SYSTEM

Mårtensson

1964

The Journal of Experimental Medicine

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Gm types of sera from Caucasians and Negroes, of myeloma globulins, and of specific antibodies were investigated. In particular the relationship between the recently identified gene Gmf and other Gm genes was analyzed. 1. Caucasians were, with rare exceptions, either Gm(b+f+) or Gm(b-f-). 2. In Negroes, on the other band, type Gm(b+f-) was found to be common. 3. No myeloma globulins appeared to contain the product of more than 1 of the 3 genes Gma, Gmb, and Gmf, even though the large majority of normal individuals, as well as myeloma patients, possess 2 or all 3 of these genes. 4. The types Gm(a+b-f-) and Gm(a-b-f+) represented the 2 major groups among the γ2-myeloma globulins; each comprised roughly 40 per cent. The types Gm(a- b+f-) and Gm(a-b-f-) are minor groups. 5. All Gm(x+) myeloma globulins were also Gm(a+). Approximately half of the Gm(a+) myeloma globulins were Gm(x+). 6. In the majority, but not in all, of Gm(a+) sera the anti-Rh antibodies were clearly Gm(a+). Similarly, the anti-Rh antibodies of Gm(f+) sera were most often, but not always, also Gm(f+). In contrast, only a minor proportion of Gm(b+) anti-Rh sera sensitized red cells to anti-Gm(b).

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Section: Anti-rh Antibodies and Their Properties As Components In The Gmmentioning

confidence: 91%

“…Inv(a) and Inv(1) are characters which, like Gm(b) and Gin(f), generally occur together in Caucasians (32). More than 99 per cent of Europeans are either Inv(a+l+) or Inv(a-1-) (32).…”

Section: Anti-rh Antibodies and Their Properties As Components In The Gmmentioning

confidence: 99%

ON THE RELATIONSHIPS BETWEEN THE γ-GLOBULIN GENES OF THE GM SYSTEM

Mårtensson

1964

The Journal of Experimental Medicine

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“…Much information bearing on this question has been derived from studies of human K-type light polypeptide chains. Two phenotypic variants of K-chains are designated Inv (1) and Inv (3), and sera of all normal individuals contain light chains that can be serologically typed as Inv (1,-3), Inv (1,3), or Inv (-1,3).1, 2 Since the Inv factors are inherited as codominant Mendelian traits, these antigenic variants appear to be allelic forms of a single structural gene.…”

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confidence: 99%

“…The amino acid interchange at position 191 correlates perfectly with the Inv type of the myeloma light chains and BenceJones proteins. All Inv (1) In order to eliminate the possibility that a lambda common region peptide might be superimposed on either the Inv (1) or Inv (3) peptide, a mixed tryptic peptide map (1 mg kappa-Bence-Jones Ha plus 1 mg lambda-Bence-Jones HS-5) was prepared. No lambda common region peptides were located in the region of the Inv peptides.…”

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confidence: 99%

“…All available specificity (variable) region sequences have been examined in an attempt to find other amino acid residues that correlate with Inv type. [12][13][14][15][16][17][18] Positions containing residues that are identical il Inv (1) 63,1969 it has been postulated that there are three Inv alleles: Inv3, Inv' 2, and the rarely occurring Inv'. The Inv (1) proteins reported in this paper have not been assessed for the Inv (2) antigen, but statistically they are most likely to be Inv (1,2).…”

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GENETICS OF IMMUNOGLOBULIN Κ-Chains: CHEMICAL ANALYSIS OF NORMAL HUMAN LIGHT CHAINS OF DIFFERING INV TYPES

Terry

Hood

Steinberg

1969

Proc. Natl. Acad. Sci. U.S.A.

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Abstract.-The relationship between Inv phenotype and the amino acid residue at position 191 in K-type light polypeptide chains derived from the immunoglobulins of ten normal human sera was investigated. In each case, the amino acid present at position 191 correlated with the Inv phenotype of the individual. Kappa chains of seven Inv (-1,3) homozygotes had valine, while those of three Inv (1,3) heterozygotes had some chains with leucine and some with valine at this position. Genes encoding the Inv (1) and Inv (3) variants appear to be expressed equally in the heterozygous state, since approximately equal amounts of each gene product was recovered from heterozygotes.The correlation between Inv phenotype and the amino acid residue present at position 191 is identical to that previously established for K-type Bence-Jones proteins and myeloma protein light chains. These observations support the hypothesis that the valine-leucine interchange is encoded by two allelic forms of a single K-chain common region gene.One goal in the investigation of the genetics of immunoglobulin proteins has been to determine the number of copies of each structural gene in the germ line of a single individual. Much information bearing on this question has been derived from studies of human K-type light polypeptide chains. Two phenotypic variants of K-chains are designated Inv (1) and Inv (3), and sera of all normal individuals contain light chains that can be serologically typed as Inv (1,-3), Inv (1,3), or Inv (-1,3).1, 2 Since the Inv factors are inherited as codominant Mendelian traits, these antigenic variants appear to be allelic forms of a single structural gene.A likely chemical basis for these serologic variants was revealed by the amino acid sequence analysis of homogeneous myeloma light chains and Bence-Jones proteins.3-5 The kappa immunoglobulin chain consists of two distinct regions. There is an amino terminal specificity or variable region (approximately residues 1-107) which shows variation in many positions, and a carboxyl terminal region (approximately residues

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