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J Klein

Publications and source records attributed to J Klein.

At least 901 records · Page 50Linked to original sources
PubMed1977

Relationship between trinitrophenyl and H-2 antigens on trinitrophenyl-modified spleen cells. I. H-2 antigens on cells treated with trinitrobenzene sulfonic acid are derivatized.

Spleen cells were treated with TNBS in order to determine if cell surface H-2 antigens are derivatized with TNP. By labeling the cell membrane of the TNP-modified cells with 125I, followed by detergent lysis and immune precipitation with anti-TNP, it was determined that no H-2 antigenic activity remained in the supernatant. Further, by the use of an antibody-induced antigen redistribution assay it was found that previous exposure to TNP-modified cells to anti-TNP in the absence of complement rendered these cells resistant to lysis by anti-H-2 in the presence of complement. Together these data indicate that at the concentration of TNBS used for modification, H-2 antigens are derivatized with TNP. However, in addition to H-2, other proteins including immunoglobulin were also derivatized with TNP. Anti-TNP cytotoxic effector cells were blocked from their cytotoxic activity by anti-TNP antiserum. These data indicate that TNP directly couples to H-2 antigens on the cell surface of TNP-modified cells and that TNP is associated with the antigenic determinant that the cytotoxic T cell recognizes.

Animals↗
PubMed1977

Histocompatibility-2 system in wild mice. V. Serologic analysis of sixteen B10.W congenic lines.

Sixteen B10.W congenic lines carrying on C57BL/10Sn or B10 background H-2 haplotypes extracted from wild mice are described. The lines were tested serologically in two ways: first by antisera against known H-2K and H-2D private antigens of inbred strains, and second by antisera made in inbred strains against antigens carried by the B10.W lines. Both direct cytotoxicity and absorption tests were used. The analysis resulted in the serologic identification of the H-2 haplotypes carried by the 16 B10.W lines. Lines B10.STA10 and B10.STA12 are serologically indistinguishable; so are lines B10.KPA42, B10.KPA132, and B10.SNA57, whose H-2 haplotypes resemble the H-2v haplotype of B10.SM; all other B10.W lines are different from one another and different from all inbred strains known. In total, 10 new H-2 haplotypes (H-2w11 through H-2w20) and 16 new H-2 antigens (H-2.110 through H-2.125) were identified. One haplotype was discovered carrying new combination of known H-2 antigens: H-2w19, which is H-2K.19, H-2D.2. Known H-2 antigens in combination with new ones were discovered in haplotypes H-2w8 (H-2.23 and 110), H-2w12 (H-2.23 and 112), and H-2w11 (H-2.26 and H-2). The first two of these three haplotypes are probably the result of intra-H-2 crossing over that occurred during the production of B10.W lines; the last one (and the H-2w19 haplotype) is probably a natural recombinant.

Animal Population Groups↗
PubMed1976

Beta 2-microglobulin is selectively associated with H-2 and TL alloantigens on murine lymphoid cells.

We have used a rabbit antiserum prepared against purified rat beta2-microglobulin to immunoprecipitate molecules from lysates of radioiodinated murine thymocytes and splenocytes. All the molecules that are reactive with this serum have subunits of 44,000 and 12,000 and can be identified as H-2 and TL antigens. Thus, the anti-beta2mu serum can deplete lysates of the majority of the TL and H-2 atigens which can be subsequently recognized by alloantisera. If TL and H-2 are precipitated from the lysates before the addition of anti-beta2mu, no beta2mu-reactive molecules remain. Our results indicate that Ia antigens cannot be depleted from the lysates with anti-beta2mu. The studies also suggest that TL and H-2 heavy chains can exist as both monomers and dimers. These observations are discussed with regard to previous studies concerning the native structure of H-2 and TL antigens.

Animals↗
PubMed1976

Histocompatibility antigens controlled by the I region of the murine H-2 complex. I. Mapping of H-2A and H-2C loci.

Skin grafts were reciprocally exchanged in pairs of congenic lines identical in all genes except those located in the central portion of the H-2 complex. Seven such lines were tested: 6R, B10.AQR, A.TL, A.TH, 7R, 9R, and B10.HTT. In all donor-recipient combinations at least some grafts were rejected. In combinations differing at the IA subregion (and other central H-2 regions or subregions), all first-set grafts were rejected within 3 wk after transplantation, and all second-set grafts were rejected within 10 days. In combinations differing at the IC subregion (and other central regions, but not at the IA subregion) between 60 and 100% of first-set grafts were rejected, but some grafts survived for over 100 days. Most of the second-set grafts were rejected within 1 mo after grafting. This behavior of skin grafts indicated the presence of two histocompatibility loci in the I region, a strong one and a weak one. This conclusion was confirmed by genetic mapping which placed the strong locus in the IA subregion and the weak locus in the IC subregion. We designate the former locus H-2A and the latter H-2C. The same strain combinations used for the skin grafting were also used for determination of the capacity of I-region antigens to function as targets in the in vitro cell-mediated lymphocytotoxicity (CML) assay. Spleen cells from mice presensitized in vivo by skin grafting were restimulated in vitro and tested against 51Cr-labeled concanavalin A or lipopolysaccharide blasts. The testing revealed the presence in the I region of two loci coding for CML-target antigens. The two loci comapped with the H-2A and H-2C loci and were most likely identical to them. As in the skin grafting test, in the CML test, the H-2A antigens evoked stronger response than the H-2C antigens. Rejection of skin grafts across the H-2A and H-2C loci was accompanied by the production of Ia antibodies. Direct cytotoxic and absorption tests with Ia antibodies directed against antigens coded for by the IC subregion revealed the presence of IaC antigens on epidermal cells. We suggest that the products of Ia loci might function as transplantation antigens.

Animals↗
PubMed1976

Structural studies on protein products of murine chromosome 17: partial amino acid sequence of an H-2Kb molecule.

By use of single internal radiolabels, 17 of the NH2-terminal 27 amino acids of the murine H-2Kb molecule have been assigned. When the amino acid sequence is compared to that of the murine H-2Kk molecule, there is a minimum of six amino acid differences in 19 positions. This high degree of structural diversity confirms, at the level of amino acid sequence, the known polymorphism of the murine H-2 complex. Significant primary str-ctural homology is evident when the murine H-2Kk and H-2Kb sequences are compared to the recently reported partial amino acid sequences of human transplantation antigens. There is modest homology with beta2-mictoglobulin and immunoglobulins, but the available sequence information is insufficient for a satisfactory evaluation of its significance.

Alleles↗
PubMed1976

The partial amino-acid sequence of an H-2K molecule.

Eighteen of the NH2-terminal 27 amino acids of a murine H-2K molecule have been assigned. The approach used was to label murine splenocytes with a single radioactive amino acid, isolate the H-2K molecule by specific immunoprecipitation, electrophorese the dissolved precipitate on sodium dodecyl sulfate polyacrylamide gels, and subject the isolated H-2K peak to amino-acid analysis and automated sequencing.

Amino Acid Sequence↗
PubMed1976

Histocompatibility-2 system in wild mice. II. H-2 haplotypes of t-bearing mice.

As a first step in the study of the possible relationship between the T/t and H-2 complexes, the H-2 antigenic composition of the strains carrying factors t12, tw32, tw2, tw8, t1, t0, t6, tw1, tw71, tw73, tw12, tw5, tw75, and t38 was studied by using a battery of antisera containing antibodies against inbred-derived H-2 antigens. In addition, five t strains (t12, t6, tw5, tw1, and tw2) were selected for the production of antisera against the H-2 complexes carried by t chromosomes. Spleen, lymph node, and thymus cells from H-2b/t heterozygotes and tw2/tw2 homozygotes were injected into appropriate F1 hybrids between two inbred strains that carried the inbred-derived H-2 antigens of the donor. Four new H-2 antigens and one Ia antigen were uncovered and were assigned the symbols H-2.106 through H-2.109, and Ia.101, respectively. Three new H-2 haplotypes were also described, based upon the H-2 antigenic pattern of three t factors, t12, tw1, and tw5. These new haplotypes were given the symbols H-2t12, H-2tw1, and H-2tw5. When the t factors were grouped according to their H-2 haplotypes, their distribution, with certain exceptions, corresponded to the complementation groups. Thus, t chromosomes in the same complementation group carried similar, if not identical, H-2 haplotypes, despite the fact that these chromosomes were derived from widely separated geographic areas. Such an association between the t and H-2 complexes is most unusual in light of what is known of the polymorphism of H-2 haplotypes in wild mice populations. It suggests more than a casual relationship, at least at the population level, between the t and H-2 loci.

Animals↗
PubMed1976

Participation of H-2 regions in heart-transplant rejection.

Hearts of newborn mice were cut into small pieces, the fragments transplanted under the ear skin of adult recipients, and the graft survival followed visually (pulsating fragments were considered viable). Donor-recipient combinations were chosen from H-2 congenic (recombinant and mutant) strains in such a way as to provide differences in the entire H-2 complex or in only a small portion of it. The data obtained indicate that a difference between the donor and the recipient in either K, D, or I regions suffices for the rejection of the heart fragments. The rejection is often accompanied by the production of antibodies against classical H-2 antigens (in the case of K- or D-region disparities) or Ia antigens (in the case of I region disparities). In some instances, the antibodies persist in the recipient for more than 50 days. We conclude from these experiments that the same loci that cause acute skin graft rejection (H-2K, H-2D, and H-2I) are responsible for heart graft rejection. Furthermore, we also conclude that serologically Ia-negative tissues may carry Ia antigens in sufficient quantities to stimulate the production of Ia antibodies.

Animals↗
PubMed1976

Immunogenetic analysis of H-2 mutations. V. Serological analysis of mutations H-2da, H-2ra, and H-2ka1.

The H-2 and Ia antigenic composition of strain pairs B10.D2 (H-2d) and M504 (H-2da). A.CA (H-2f) and M506 (H-2fa), and CBA (H-2k) and M523 (H-2ka) was compared by testing their cells against a battery of oligospecific antisera, by performing absorption analysis, and by cross-immunization. The two strains of each pair are congenric and differ in taht the second strain of the pair carries a mutation that occurred in the H-2 haplotype of the first strain. The Ia composition of each mutant haplotype was found to be the same as that of the haplotype from which the mutant was derived. Several differences in the serologically detectable H-2 antigens were found. The H-2d and H-2da haplotypes were found to differ in that the latter lost at least one and gained another antigen. The affected antigens were demonstrated to be classic H-2 antigens controlled by the H-2D locus. The H-2t and H-2fa haplotypes were found to differ in that antigens 26, 37, and 39, controlled by the latter, bound their respective antibodies less firmly than those controlled by the former haplotype. Since all three antigens are coded for by the H-2K locus, since no change was found in the D-region controlled antigens, and since the H-2fa mutation maps in the K end, we conclude that most likely the mutation occurred in the K region. The H-2k and H-2ka haplotypes were found to differ in that the latter lost one antigen encoded by the H-2Kk allele. This mutation, therefore, must have occurred in the H-2K locus. The data tip the scale of evidence in favor of the interpretation that each of the H-2 mutations occurred in a single region, either K or D. No evidence for a second mutation within any of the other H-2 regions was found.

Animals↗
PubMed1976

Immunogenetic analysis of H-2 mutations. IV. Mapping of and immune reactions to the H-2fa mutation.

H-2fa is a spontaneous mutation that occurred in an (A.CA X A)F1 female mouse and was later transferred on an A-strain background [congenic line A.CA (M506) or M506]. Skin grafts exchanged between M506 and A.CA strains are rejected within 4 weeks after grafting. Significant reaction is observed when these two strains are used as responders and stimulators in mixed lymphocyte culture or in a splenomegaly graft-versus-host assay. The mutant antigen induces strong cell-mediated lymphocytotoxicity. The mutation maps in the K end of the H-2 complex. The capacity of mutant antigens to induce relatively strong lymphocyte proliferation is explained by hypothesizing that the T-cell receptors reacting with K- or D-region products can more easily recognize subtle than drastic alloantigenic differences.

Animals↗
PubMed1976

Immune response of mice to the Thy-1.1 antigen: intra-H-2 mapping of the complementary Ir-Thy-1 loci.

The primary immune response to the Thy-1.1 antigen was measured by a plaque assay that detected cells producing antibodies lytic for AKR thymocytes. F1 hybrids which were b/d heterozygous at the entire H-2 complex or at only some of its regions were studied. All F1 hybrids which were b/d heterozygotes at the K, IA and possibly IB regions displayed a complementary effect of the alleles at the Ir-Thy-1A and Ir-Thy-1B loci. The complementary effect was indicated by the significantly higher responses of the F1 hybrids than the responses of their parental strains. No complementary effect could be demonstrated in F1 hybrids which were b/d heterozygous at the IB, IC, S and D regions, but not at the K and IA regions. The results excluded participation of the IC, S and D regions in the phenomenon of the complementation. Furthermore, one of the Ir-Thy-1 loci could be mapped to the left of the IB subregion, most likely in the IA subregion of the H-2 complex. The second Ir-Thy-1 locus could be mapped to the left of the IC subregion in either the IA or IB subregion.

Animals↗
PubMed1976

Characterization of Ia antigens in mouse serum.

Sera obtained from normal B10.BR mice were shown to inhibit selectively a specific anti-Ia alloantiserum. Partial purification of the Ia antigenic activity was accomplished by isolation of the high density lipoproteins from these sera by fractional precipitation with sodium phosphotungstate and MgCL2. Both H-2.23 and Iak antigens present in this high density lipoprotein fraction were completely adsorbed by rabbit anit-rat beta2-microglobulin immunoadsorbents, whereas specific anti-H-2.23 immunoadsorbents removed only the H-2 activity. These data deomnstrate that Ia antigens, like H-2 antigens in the sera of B10.BR mice are associated with high density lipoproteins and further suggest that both H-2 and Ia antigens are associated with a beta2-microglobulin-like molecule.

Animals↗
PubMed1976

Relationship between beta2-microglobulin and cell-surface alloantigens of the mouse.

Molecular relationships between beta2m and other cell surface antigens (H-2, Tla, Ia, and Thy-1) were studied with the double immunofluorescence method. Cells were incubated with an antiserum against one antigen capped, and then tested with an antiserum against a second antigen. Capping of beta2m on thymocytes led to simultaneous capping of H-2 and Tla but not Thy-1 antigens; capping of H-2 and TIa (but not Thy-1) antigens resulted in capping of all beta2m detectable by the immunofluorescence method. Similarly, capping of beta2m on B or T lymphocytes resulted in capping of H-2 and vice versa. Ia antigens on B lymphocytes were not capped after the redistribution of beta2m. We conclude from these data that, in the cell membrane of thymocytes, virtually all the beta2m molecules are associated with H-2 and Tla, but not with Thy-1, and that on the cell surface of T or B lymphocytes, virtually all beta2m is associated with H-2 but not with Ia. We found no evidence of any significant free beta2m on either thymocytes or splenocytes.

Animals↗