Murine Ia and human DR antigens: homology of amino-terminal sequences.

Allison, James P.; Walker, Leslie E.; Russell, William A.; Pellegrino, M. A.; Ferrone, Soldano; Reisfeld, Ralph A.; Frelinger, J. A.; Silver, Jack

doi:10.1073/pnas.75.8.3953

Cited by 110 publications

(33 citation statements)

References 21 publications

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“…In man, the situation is less clear. Partial NH2-terminal sequences of HLA-DR antigens isolated from B-cell lines show homology only with the I-E/C polypeptides of the mouse and not with I-A products (18,19). Similarly, serological analysis of the cross-reactions of mouse anti-Ia alloantisera on human cells showed a predominant, correlation with L-E/C specificities (20,21).…”

mentioning

confidence: 99%

Cell surface properties of HLA antigens on Epstein-Barr virus-transformed cell lines.

Smith¹,

Petty²,

Parham³

et al. 1982

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

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A number of monoclonal antibodies have been used to investigate the distributions and rates of lateral motion. of the HLA-A,B, and -DR antigens on several Epstein-Barr virustransformed B-cell lines. The lateral diffusion coefficients (D) of fluorescein conjugates of.the monoclonal antibodies bound to the cell surface were determined by fluorescence recovery after pattern photobleaching. Ds of HLA-A and -B were.found to be comparable and of the order of 1009 to 10-1o cm2/sec for each of the seven monoclonal antibodies and four cell lines examined. The HLA antigens. appear to be monomeric on the cell surface based on experiments using mixtures of arsanilic acid-conjugated and fluorescein-conjugated antibodies. Four monoclonal antibodies against DR antigens were examined. Two ofthese, Genox3.53 and L243, labeled the cell surface uniformly and gave Ds comparable to those obtained for the HILA-A and -B antigens. The other two, DA2 and 2.06, rapidly patched on the cell surface and were immobile. The DA2, L243, and Genox 3.53 antibodies bound outside ofthe caps formed with the arsanilic acid-conjugated 2.06 antibody and a second-step rhodamine-conjugated rabbit anti-arsanilate antibody. This is consistent with recent biochemical evidence that there are multiple distinct antigens coded for by the HLA-DR region.The major histocompatability complex codes for a series ofpolymorphic cell surface antigens important for the control of cellular interactions in immunity (1-6). Two different types of glycoprotein complexes provide the molecular basis for the HLA-

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mentioning

confidence: 99%

Cell surface properties of HLA antigens on Epstein-Barr virus-transformed cell lines.

Smith¹,

Petty²,

Parham³

et al. 1982

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

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“…However, serological crossreactivities (33), the presence of two chains (one nearly invariant, the other highly polymorphic), and NH2-terminal sequence homology (34) point to a strict analogy between human DR and mouse IE/C alloantigens. It is therefore possible, as recently demonstrated by Jones et aL (35) for the latter, that the a chains are MHC encoded as well, and their minor differences are the expression of a more limited but real polymorphism.…”

Section: Discussionmentioning

confidence: 99%

“…DR antigens are composed of two noncovalently linked chains, apparently [33][34][35] kDal (heavy or a chain) and [26][27][28][29] kDal (light or 13 chain) (12,13). They appear to be equivalent to the mouse Ta antigens, to which a number of functions in the immune response have been assigned (1,14).…”

mentioning

confidence: 99%

Analysis of HLA-DR polymorphism by two-dimensional peptide mapping.

Corte¹,

Damiani²,

Calabi³

et al. 1981

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

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Two-dimensional peptide mapping was used to study the polymorphism of DR antigens, membrane glycoproteins composed of two chains, a and (3, and encoded by the human major histocompatibility complex (MHC). Four DR antigens were purified by immunoabsorption from four human lymphoblastoid cell lines homozygous at the DR locus. After labeling with 125I, a and j3 chains were separated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate and digested with pepsin. Comparison of the peptide maps showed a marked degree of polymorphism among j3 chains: only 43% of peptides were common to all four chains and 15-21% of the spots were unique to a given chain. By contrast, only a limited variability was observed among a chains. Homology was 75% for the four chains and the percentage of unique peptides was very low. DR7 did not possess even a singe unique peptide. The limited variability among a chains and the lack of "private" peptides in one of them point to the conclusion that the f3 chain is the unique carrier of the alloantigenic specificities. Higher homology within the known crossreactive groups was not observed, suggesting that the determinants responsible for crossreactivity are on different molecules. From a genetic point of view, because f3 chains show allele-associated polymorphism, they are likely to be MHC encoded, whereas the minor differences among a chains do not allow a similar conclusion. The available data point to an analogy between these DR antigens and the mouse I-E/C antigens.

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“…Recent immunogenetic studies indicate that a common link between the 2 diseases may be the HLADRw4 locus, since the frequency of this allele has been reported to be increased in psoriatic atthritis (34) as well as in rheumatoid arthritis (35,36). Human immune response (Ir) genes appear to be localized near the D locus (37,38). Although Smolen et al (25) have reported that thymidine incorporation responses to denatured type I collagen by cells from patients with RA are not associated with the presence of HLA-DRw4, we have initiated a study to determine whether the capacity to respond immunologically to native type I1…”

Section: Discussionmentioning

confidence: 99%

Autoimmunity to Collagen

Trentham

Kammer

McCune

et al. 1981

Arthritis & Rheumatism

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Thirty-one patients with seronegative psoriatic arthritis, 27 patients with rheumatoid arthritis, 10 with psoriasis alone, and 20 normal volunteers were studied for autoimmunity to human collagens. Cellular and humoral responses were frequently observed in the 2 groups with arthritis, but the subjects without arthritis did not display reactivity to native collagens. These data demonstrate that collagens function as autoantigens in both psoriatic and rheumatoid arthritis.Psoriatic arthritis is an inflammatory arthritis of unknown etiology that occurs in approximately 5 to 7% of persons with psoriasis (1). The disorder is characterized by an asymmetric distribution of arthritis at onset of disease, the frequent coexistence of dystrophy of the nails and spondylitis, an increased an tissues. Types I and I11 collagens are widely distributed in dermal and organ parenchyma; type I1 collagen appears to be restricted to cartilaginous and ocular tissues; and types IV and V collagens are recently isolated species accounting for a small proportion of the collagen content of some connective tissues (29). In this article, we report that some of these collagens function as cellular and humoral autoantigens in psoriatic arthritis as well as in RA. MATERIALS AND METHODS PatientsPsoriatic arthritis. We studied 3 1 patients with psoriatic arthritis (mean age, 54 years; range, 28-72) who were part of a larger population that we recently analyzed (I).

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Murine Ia and human DR antigens: homology of amino-terminal sequences.

Abstract: Murine Ia and human DR antigens were isolated and purified by immunoprecipitation and sodium dodecyl sulfate/polyacrylamide gel electrophoresis with allo-and xenoantisera, respectively. The I-A subregon antigen consists of two chains, designated Aa

Cited by 110 publications

References 21 publications

Cell surface properties of HLA antigens on Epstein-Barr virus-transformed cell lines.

Cell surface properties of HLA antigens on Epstein-Barr virus-transformed cell lines.

Analysis of HLA-DR polymorphism by two-dimensional peptide mapping.

Autoimmunity to Collagen

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