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Biomedical subjects

G J Gleich

Publications and source records attributed to G J Gleich.

At least 433 records · Page 24Linked to original sources
PubMed1975

Changes in the antigenic composition of the short ragweed plant during maturation.

Whole ragweed plants were collected before and during the ragweed pollination season and extracts of various portions of the plants were analyzed for antigen E (AgE) and for their inhibitory potency in the radioallergosorbent test (RAST). Ragweed stems and roots contained very low, if any, AgE. AgE was present in very small amounts in anthers prior to pollination season, increased with anther and pollen grain maturation, peaked with the appearance of significant airborne pollen grains in mid-August, and fell slowly through late September. Leaf AgE content also rose during mid- and late August, but brief rinsing reduced antigen E content by almost 50%. Significant RAST inhibitory activity was found only in anthers and the activity paralleled the content of AgE.

Absorption↗
PubMed1975

Maximal rise in IgE antibody following ragweed pollination season.

Patients allergic to ragweed pollen who did not receive immunotherapy had an increase in ragweed-specific IgE antibodies associated with seasonal exposure. Of 17 such patients, 15 reached peak levels between mid-September and mid-October. Two had peak values after mid-October; the levels were only slightly higher than earlier values. Our study shows that serum obtained in mid-October reflects approximately the maximal IgE antibody level attained 0y ragweed-sensitive patients in our area and that this value can be used as a baseline in monitoring the subsequent decline in antibodies. In addition, our data support an earlier observation that the magnitude of seasonal rise in IgE antibody is related to the preseasonal value. The significantly positive correlation of the results of carefully performed skin tests (end point titration) with radioallergosorbent test (RAST) values suggests the possibility that the RAST can be employed as a reliable diagnostic aid, perhaps even replacing the skin test.

Adolescent↗
PubMed1975

Ragweed hay fever: treatment by local passive administration of IgG antibody.

To determine whether the local administration of IgG antibodies might reduce the symptoms of ragweed hay fever, we tested the effect of this treatment in fourteen patients in a double-blind pilot trial. The patients were randomly divided into two groups, treatment and placebo, and their symptoms and medication usage were determined during the ragweed pollination season. One group used a nasal spray consisting of phosphate-buffered saline (PBS) containing human serum albumin, whereas the other used PBS containing purified IgG from a subject with a high titre of IgG antibody to partially purified ragweed antigen E. Treated and control groups used comparable quantities of nasal spray, and neither noted any ill effects. Comparison of individual symptoms of hay fever, medication usage, and total symptom scores showed no significant differences between the groups except a lessening of eye symptoms (P less than 0.05) in the treated group. The results suggest that nasal administration of IgG antibody up to five times daily does not alter the severity of symptoms in ragweed hay fever. Furthermore, total serum IgE protein and specific IgE levels increased comparably in both groups, suggesting that passive administration of IgG antibody does not suppress the production of IgE antibody during the pollination season.

Administration, Intranasal↗
PubMed1975

The effect of immune milk as a treatment for ragweed pollinosis.

The effect of treating ragweed hay fever with oral hyperimmune milk globulin was evaluated in a double-blind study. Thirteen matched patient pairs were treated with capsules containing either specific protein isolated from the colostrum of cows that had been hyperimmunized with fall pollen allergens or with placebo. The results suggest that immune milk treatment did not alter IgE antibody response after pollen exposure; neither was immune milk markedly better than placebo in controlling symptoms.

Animals↗
PubMed1975

Reactivity of rabbit antiserum to guinea pig eosinophils.

Although the eosinophil has been recognized as a distinctive cell type for almost 100 years, the major functions of these cells remain unknown. As an approach to defining these functions we have treated guinea pigs with rabbit antiserum to eosinophils (AES) in an attempt to ablate these cells from tissues. Rabbits were immunized thrice with purified eosinophils and the antisera were absorbed with peripheral blood cells from guinea pigs made eosinopenic with methyprednisolone to remove antibodies reactive with serum proteins and erythrocytes. The resulting sera reacted strongly with eosinophils in cytotoxicity tests and had weak or no reactivity with neutrophils. However, absorption of AES with purified neutrophils removed antieosinophil activity. Intraperitoneal injection of potent AES into guinea pigs resulted in complete absence of eosinophils from the peripheral blood and from the peritoneal cavity with only transient or no reduction in circulating neutrophils. Eosinophils were also reduced in bone marrow, spleen, and intestine. The ability of neutrophils to absorb AES activity in spite of weak reactivity in cytotoxicity tests may reflect a quantitative difference in antigenic determinants between eosinophils and neutrophils.

Animals↗
PubMed1975

Differences between IgA and IgE as secretory proteins.

IgA is the prototype of a secretory immunoglobulin and usually is present in external fluids in proportions greater than in serum. Previous studies have suggested that IgE also is a secretory immunoglobulin. We measured IgE, IgA and albumin levels in nasal washings (NW), parotid fluids (PF) and serum in seventeen individuals. In secretions, all of these proteins were measured by radioimmunoassay (RIA). In serum, IgE was measured by RIA, IgA by a turbidimetric method, and albumin by radial immunodiffusion. IgA was detected in NW and PF in all individuals and IgA/total protein ratios in both of these secretions exceeded the corresponding ratios in serum (P less than 0-01). In contrast, IgE was detected only in NW from atopic subjects and IgE/total protein ratios were less than those in serum (P less than 0-02). IgE was not detected in the PF in any of the seventeen subjects. When the proportion (protein/total protein) of IgA, IgE, or albumin in NW was expressed as a percentage of the proportion in serum, IgA and IgE were increased when compared to albumin (P less than 0-01 and P less than 0-03, respectively). These results support the view that IgE is a secretory immunoglobulin in that it is present in NW in proportions greater than expected if it diffused from serum. However, IgE differs from secretory IgA in that ratios of IgE to total protein are greater in serum than in NW. This difference is discussed in terms of local production of IgE and passive diffusion into serum and nasal secretions. Finally, the observation that IgE is present in one external secretion while absent from another indicates that external secretions may be subdivided into two classes on the basis of their content of IgE.

Adult↗
PubMed1974

Physiochemical and biological properties of the major basic protein from guinea pig eosinophil granules.

Guinea pig eosinophil granules are characterized by the presence of a basic protein of low molecular weight which accounts for greater than 50% of granule protein. This protein, termed the major basic protein (MBP), readily aggregates and becomes insoluble, and the formation of aggregates is dependent on the establishment of disulfide bonds. Analysis of concentrated preparations of MBP often revealed a series of bands which were multiples of a monomeric unit with a mol wt of approximately 11,000. Analysis of reduced and alkylated MBP on a 10% agarose column equilibrated with 6 M guanidinium chloride revealed a single polypeptide chain with a mol wt of 10,800. Amino acid analysis of the protein revealed the presence of 13% arginine, consistent with the basic character of the molecule. Four residues of tryptophan, were present, indicating that MBP is not a histone. The MBP did not increase vascular permeability when injected into the skin of guinea pigs, nor did it antagonize the effect of histamine and bradykinin in the skin. MBP also did not contract the isolated guinea pig ileum and when mixed with histamine or bradykinin did not inhibit their activity on the gut. MBP had only weak, if any, antihistaminic activity. MBP possessed weak bactericidal activity when compared to histone and then only with one strain of E. coli. MBP precipitated DNA, neutralized heparin, and activated papain. On a molar basis MBP was more active than cysteine in activating papain. These results do not point to any unique biological activity associated with MBP other than those expected of a protein as basic as it is and one which possesses reactive sulfhydryl groups. Possible functions of eosinophils based on the properties of the MBP are discussed.

Amino Acids↗
PubMed1973

Identification of a major basic protein in guinea pig eosinophil granules.

Elucidation of the functions of the eosinophil might be accomplished by analysis of the granule constituents. We have purified eosinophils (93% or greater) from the peritoneal cavity of the guinea pig and have investigated a variety of methods to disrupt cells and liberate intact granules. Lysis in 0.34 M sucrose gave the best yield of granules and these had the characteristic morphology of eosinophil granules when examined by electron microscopy. Granules were solubilized by a variety of treatments and the solutions analyzed by polyacrylamide electrophoresis at pH 3 in 6 M urea. Comparison of the electrophoretic patterns of solubilized eosinophil and neutrophil granules revealed a difference: a major portion (53+/-3%; x +/-1 SE) of the protein from the eosinophil granule migrated as a single component. This major band protein has a molecular weight between 6,000 and 12,000 daltons and a pI of 10 or greater. Analysis of eosinophil granule constituents on Sephadex G-50 revealed two main peaks; peak 1 possessed peroxidase activity and peak 2 contained the major band protein. These studies indicate that eosinophil granules contain a cationic protein of low molecular weight which lacks peroxidase activity and which accounts for greater than 50% of granule protein.

Animals↗