Search PubMed⌕ Search

Biomedical subjects

M S Sandrin

Publications and source records attributed to M S Sandrin.

At least 91 records · Page 5Linked to original sources
PubMed1984

A high proportion of hybridomas raised to a plant extract secrete antibody to arabinose or galactose.

A high proportion of hybridomas, obtained from mice immunized with style extracts prepared from mature flowers of an ornamental tobacco, Nicotiana alata, secrete antibody to arabinogalactan protein (AGP). The specificity of the antibodies secreted by three cloned cell lines is primarily directed to beta-d-galactopyranose and alpha-l-arabinofuranose; antibodies from two cell lines preferentially bind beta-d-galactopyranose residues and antibodies from the other cell line preferentially bind alpha-l-arabinofuranose. As AGPs are components of most plant tissues and exudates, it is likely that attempts to raise monoclonal antibodies to other plant extracts will result in hybridomas producing antibodies to AGPs.

Journal Article↗
PubMed1983

Restriction in adoptive transfer of resistance to Listeria monocytogenes. II. Use of congenic and mutant mice show transfer to be H-2K restricted.

Adoptive transfer of cell-mediated immunity to the facultative intracellular bacterium Listeria monocytogenes is restricted by the H-2 complex of mice. Using C57BL/10 and C57BL/6 congenic strains of mice it was shown that compatibility of the H-2K locus, not the I region, was essential and sufficient for adoptive transfer and that H-2D compatibility was not relevant. Mutation at the H-2K locus prevented adoptive transfer, while mutation at the Ia-1 locus, as in the B6.C-H-2bm12 mutant of C57BL/6, did not affect adoptive transfer. The contrast between these findings and the previously accepted I region restriction of adoptive transfer of Listeria immunity is discussed.

Animals↗
PubMed1982

Serological analysis of B6.C-H-2bm12 (I-A mutant).

The B6.C-H-2bm12 has been examined serologically with a new set of reagents and several complementation studies were performed to determine the extent of the mutation. The results show that: (a) the mutation has also affected the site(s) bound by xenogeneic anti-Ia antibodies; (b) the IJb region was not affected; (c) complementation studies with stains bearing a, b, d, k and s haplotypes did not complement bm12 for the expression of the lost I-Ab specificities, suggesting a structural (rather than regulatory) gene alteration in bm12; (d) H-2 haplotypes b and bm12 could complement d to establish the Ia.22 specificity, indicating that Ia-1 and Ae are separate genes in the I-A subregion. In addition, an antibody to the gained specificity on bm12 is described.

Animals↗
PubMed1981

Alterations in the expression of Ia antigens in F1 hybrid mice.

The Ia.8 and 9 specificities detected either by conventional or monoclonal antisera (Ia.m3,4) are present in strains bearing the b H-2 haplotype, but absent from those with the k haplotype. It would be expected that the (b X k)F1 hybrids would have approximately half the amount of these specificities found on the b parent, but the Ia.8 and 9 specificities are absent or reduced in this F1 hybrid, though not on F1 LPS blasts. Examination of appropriate H-2 congenic strains demonstrated that only the k haplotype confers the absence of these specificities on H-2b - it was not observed with b, d, q, or s haplotypes. In the K haplotype the gene(s) responsible for this effect is mapped to the I-Ak subregion. The reason for this "low expression" effect is not clear but the observation has important implications for the relationship of Ia specificities and Ir genes and may serve to explain the "low responder" status of certain F1 hybrids, e.g., to TNP-mouse serum albumin, as observed elsewhere.

Animals↗
PubMed1981

Cross-reactions of Ia antigens between mouse and man.

Murine alloantisera with specificity for the I-region of the MHC were found to cross-react with human B lymphocytes. By using antisera selected for subregion specificity and including monoclonal antibodies, antisera directed to I-E/Ck products were shown to have the greatest cross-reactivity with human cells. In the reciprocal direction, human anti-DRw alloantisera were also found to contain antibodies that reacted with murine B lymphocytes, and by using congenic strains this reaction was shown to be MHC restricted and was of the "Ia type." By studying appropriate intra-H-2 recombinant strains. The reactivity could be mapped to the 1-E subregion (especially to 1-Ek). In addition, antibodies to the murine 1-Ek subregion could specifically block the reaction of the two DRw antisera examined; whereas, anti-I-Ak antisera were without effect. These studies further highlight the unique cross-reactions between two highly polymorphic gene produces in mouse and man, and demonstrate that the 1-E subregion in the mouse codes for the most cross-reactive specificities.

Animals↗
PubMed1981

Reactivity of xenogeneic antihuman Ia antisera with the I-C subregion of the murine major histocompatibility complex. I. Genetic studies.

Several rabbit xenoantisera raised against human serum Ia antigens have been shown to detect murine lymphocyte antigens. The murine system detected was shown to be polymorphic and expressed on B cells and not T cells. Serological analysis of recombinant H-2 strains demonstrated that two of the antisera recognized products of the I-Cd subregion, and one antiserum recognized products of the I-Cb subregion, thus clearly establishing the existence of the I-C subregion in these two haplotypes. However, as the I-Cd subregion is classically described by the Ia.6 specificity present on T cells and xenoantisera detect a product on B cells, the indication is that the I-C region, like I-A and I-J, complex and contains genes coding for specificities on T cells or B cells.

Absorption↗
PubMed1981

Reactivity of xenogeneic antihuman Ia antisera with the I-C subregion of the murine major histocompatibility complex. II. Biochemical studies.

The biochemical nature of the cross-reactive antigens on murine B cells, detected with xenogeneic antihuman Ia (H.Ia) sera, were examined. These antigens, coded for by the I-C subregion, were found to be carbohydrate in nature and probably exist as glycolipids on the cell surface. Furthermore, sugar inhibition studies demonstrated that the anti-H.Ia sera recognized identical monosaccharide residues on murine and human B cells.

Animals↗
PubMed1981

Serum Ia levels during tumor growth in mice and humans.

Antigen stimulation in mice such as occurs with the rejection of an allogeneic tumor graft caused a substantial rise in serum glycolipid Ia levels. However, mice bearing a measurable syngeneic tumor had no detectable Ia antigens in their sera; this observation was made in several different strains of inbred mice with 5 different tumors. In each instance the serum Ia level fell as the tumor grew progressively, reached zero at about the time the tumor was visible, and remained at this zero level until the mouse died. Similar results were found in humans: Tumor-bearing patients had markedly suppressed serum Ia levels. The mechanism of the fall in serum Ia glycolipid levels is not known, but the measurement of the serum Ia glycolipid content appears to reflect the level of activation of the immune system, and the suppression of serum glycolipid Ia levels found in tumor-bearing mice and patients may have important clinical implications.

Animals↗
PubMed1979

B6.C-H-2bm12. A new H-2 mutation in the I region in the mouse.

The B6.C-H-2bm12 mutant is described and evidence is presented for the mutational site occurring in the IA subregion. The mutant is of the gain and loss type as bm12 in equilibrium or formed from C57BL/6 grafts are rejected in 14-16 d. Mapping studies by the gene-complementation method using H-2 recombinant strains place the mutation in the K or IA regions of the H-2 complex and furthermore, the use of this test and the use of other H-2 mutants indicate that H-2Kb is not the site of the mutation, making the IA region the most likely site. Serological analysis with a battery of H-2b, Iab, and other Ia sera, both by cytotoxicity, rosetting, and also by absorption analysis, indicated no alteration in H-2 specificities, particularly in H-2.K33. By contrast, all of the Iab specificities coded for by the IA subregion (Ia.3, 8, 9, 15, and possibly 20) are extensively altered and are either absent or greatly reduced in amount indicating an extensive alteration in the Ia-bearing molecule. The bm12 mutant strongly stimulates the parental C57BL/6 strain in an mixed lymphocyte reaction (MLR), and the reciprocal also occurs, the degree of stimulation being similar to that obtained with K + IA differences originating in another H-2 haplotype and points to the mutation effecting the Lad-1 locus. The presence of an extensive histocompatibility change, a marked alteration in the serologically detected Ia specificities, and a strong MLR, all produced by the one mutation, provides strong evidence for the identity of the Ia-1, Lad-1, and H-2(IA) loci in the IA subregion. The bm12 mutant should be of value in determining the relationship of Ia specificities, Ir genes, and other phenomena effected by the I region.

Animals↗
PubMed1978

Detection of mouse alloantibodies by rosetting with protein A-coated sheep red blood cells.

Staphylococcal protein A has an affinity for the Fc portion of the IgG molecule of different species and can therefore be used to detect cell-bound immunoglobulin. Using this property, protein A coupled to sheep red blood cells via chromic chloride can detect alloantibodies to mouse H-2, Thy-1, Ly-1, 2, 4, 5, 6, and 7, and Ia antigenic specificities bound to the surface of lymphocytes by the formation of rosettes. In comparison with other rosetting and cytotoxicity assays, the protein A assay shows a greater sensitivity than does cytotoxicity using spleen cells as the target, as does the sheep anti-mouse Ig rosetting assay, whereas cytotoxicity shows greater sensitivity with some antisera on thymocytes. The major advantages of the protein A assay are that constant low reproducible backgrounds are obtained, there is no need to remove surface Ig by capping prior to antiserum treatment, and that viable cells can be recovered.

Animals↗