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Biomedical subjects

V A Roxburgh

Publications and source records attributed to V A Roxburgh.

3 recordsLinked to original sources

Binding sites for immunoglobulin G in rabbit ciliary processes.

This article demonstrates the presence of selective binding activity for the Fc fragment of IgG on the ciliary processes of rabbit eye. Other parts of the eye, including the cornea, iris, choroid, and retina, were negative for such activity. Binding activity was demonstrated in vitro by the specific adherence of IgG-coated sheep red blood cells (IgGEA) to the ciliary processes in frozen sections of whole rabbit eye. IgGEA binding was specifically blocked by IgG but not by albumin or the F(ab')2 fragment of IgG. The data suggest that the ciliary processes, like the choroid plexus and the renal interstitium, have intrinsic binding activity for Fc IgG, which might be involved in the local entrapment of immune components present either in the circulation or in the aqueous humor.

Animals↗

Binding sites for immune components in human choroid plexus.

In immunologically mediated disorders such as systemic lupus erythematosus and experimental serum sickness, immunoglobulin and complement amy be localized in the choroid plexus. This report demonstrates the presence of binding activity for the Fc fragment of IgG in 34 of 36 samples of human choroid plexus. We suggest that the number, distribution, and avidity of these Ig receptors may modulate the occurrence and/or severity of central nervous system symptoms in patients with immunologically mediated systemic diseases.

Antigen-Antibody Complex↗

Adult polysaccharidosis. Clinicopathological, ultrastructural, and biochemical features.

An abnormal polysaccharide in the form of cytoplasmic spheroids was found in the nervous system and systemic organs of a man with a progressive neurological disorder characterized by onset at 47 years of age, severe weakness, sensory loss, and dementia. Results of biochemical analysis showed a marked increase in brain and heart polysaccharide that was resistant to digestion by a mixture of glucosidases and that exhibited an iodine-complex spectrum higher than that of normal glyocgen. Results of histochemical studies were consistent with the results of biochemical analysis and further defined the branching characteristics of the stored polysaccharide. Electron microscopy showed the cytoplasmic location of the spheroids, which were granular and filamentous.

Amylopectin↗