Search PubMed⌕ Search

Biomedical subjects

C Cunningham-Rundles

Publications and source records attributed to C Cunningham-Rundles.

At least 127 records · Page 7Linked to original sources

Bovine antigens and the formation of circulating immune complexes in selective immunoglobulin A deficiency.

We have shown that levels of circulating immune complexes are closely associated with the presence of precipitating antibodies to bovine milk proteins in individuals with selective immunoglobin (Ig)A deficiency. To test whether milk proteins are involved in immune complex formation, sera of seven IgA-deficient individuals were studied for the appearance of complexes after milk ingestion. In three of the seven, an initial fall in the level of complexes was followed by an increasing value, which peaked at 120-150 min. In another three, there was a tendency toward the formation of two peaks of complexes, the first at 30-60 min and the second at 120-150 min after drinking milk. One subject, who had had recent treatment for two separate neoplasms, had a steady level of complexes that did not change during the course of this test. After drinking milk, the molecular weight of the complexes found in the sera of one individual at the start of the milk test fell from >19S to 7-11S, and in vitro additions of progressively increasing amounts of a mixture of milk proteins or bovine gamma globulin, to sera that contained complexes produced a progressive reduction in the level of complexes detectable. We conclude that the circulating immune complexes found in some patients who lack IgA contain bovine milk proteins and that periodic fluctuation of the molecular weight of such complexes, depending upon antigen ingestion, appears likely. It remains uncertain what effect the chronic circulation of complexes has upon the clinical state of this group of patients.

Adult↗

Milk precipitins, circulating immune complexes, and IgA deficiency.

Twenty-two patients with selective IgA deficiency were studied for the presence of serum precipitins to bovine milk, bovine and fetal calf serum, and circulating immune complexes. Fifty-nine percent had circulating immune complexes, 50% had milk precipitins, 23% had precipitins to bovine serum, and 13% had precipitins to fetal calf serum. All patients with precipitating antibodies against milk or against bovine or fetal calf serum had circulating immune complexes and the precipitin titers correlated with the amount of circulating immune complexes. After one IgA-deficient patient had drunk 100 ml of milk, studies of sequential serum samples showed the presence of casein in the circulation at 60 min and the appearance of increasing amounts of immune complexes for 120 min. These findings are interpreted to indicated that in human beings the IgA system may provide a major barrier to absorption of immunogens from the gastrointestinal tract.

Adult↗

Reactive half-cystine peptides of the secretory component of human exocrine immunoglobulin A.

On the basis of previous work the two forms of human secretory component, namely that which is covalently bound as a part of the exocrine immunoglobulin A molecule and the free form, are probably different states of the same protein. From autoradiographs of trypic peptide maps of bound and free secretory components which were radioactively alkylated after partial reduction, it was concluded that the same half-cystines in each are sensitive to reduction. in the present work the easily reduced half-cystines of the bound and free secretory components have been studies in more detail. In each form there are two such half-cystines. In the case of bound secretory component they provide the linkage to the remainder of the exocrine immunoglobulin A molecule. Peptides from the sensitive half-cystines were isolated from tryptic-peptic digests of free secretory component and sequenced. By diagonal electrophoresis these two peptides were shown to be joined in an intrachain disulfide bridge. Therefore, it is proposed that the exocrine immunoglobulin A molecule becomes fully assembled when a single, reactive intrachain disulfide bridge in free secretory component rearranges to yeild two interchain bridges with dimeric serum-type immunoglobulin A. This process is thought to occur within the epithelial lining cells of mucous membranes.

Amino Acids↗

Evidence for tryosine peptide homologies in the HLA antigens system.

The tetrameric HLA antigens are composed of two heavier chains which carry the alloantigenic determinants and two lighter chains identified as beta2-microglobulin. Although at least 40 different antisera are required to define the varying HLA specificities, it appears that these antigens may be closely related to each other and to the immunoglobulins. Through the use of a new electrophoretic technique, which is able to compare simultaneously the tyrosine peptides produced from radioiodinated cell surface proteins, this report gives evidence that HLA antigens of the three chromosomal loci may have similar amino-acid sequences. Since the retention of homologous tyrosine residues and a tendency for sequence preservation surrounding these residues are features of immunoglobulin structure, this may indicate that similarly conservative evolutionary mechanisms have been operative in the HLA allelelic proteins or that immunoglobulins and HLA antigens may indeed have a common evolutionary origin.

Antigen-Antibody Reactions↗

Detection of measles antibodies in cerebrospinal fluid and serum by a radioimmunoassay.

Evidence that different structural components of the measles virus may act as antigens has been provided by the serologic methods of hemagglutination inhibition hemolysin inhibition, and nucleocapsid complement fixation. Using radioiodinated measles viral antigens, and immune precipitation assay has been designed that is capable of discriminating among various reactivities to measles viral structural components in serum or cerebrospinal fluid (CSF) and of distinguishing whether IgG and IgM antibody is involved. This technique has been applied to the study of measles antibodies in CSF and sera of patients with multiple sclerosis (MS) and other neurologic diseases. From data presented here, it was found that both groups of patients have individual reactivity to measles proteins, present in CSF and serum, whereas three normal CSF samples were found not to have such antibodies. It appears that oligoclonal immunoglobulins in CSF of MS patients may be detected by this method, and one patient with MS was found to have CSF IgM anti-measles antibodies.

Antibodies, Viral↗