It has been suggested that sleep may have a positive effect on morning motor symptoms in Parkinson's disease (PD). We examined this possibility and also looked at common sleep disorders in PD. Seventy-eight PD patients and 43 normal elderly subjects answered a questionnaire. Of the PD patients, 43.6% reported improved motor symptoms in the morning, 37.2% worse, and 19.2% unchanged compared to the rest of the day. No difference was found between morning-better and -worse groups with respect to age, duration or stage of PD; antiparkinsonian medications utilized, and predominant motor symptoms. However, the morning-same group had a shorter duration of PD and less severe disease and required fewer dopaminergic medications. Sleep disorders were seen with equal frequency in the morning-better and -worse groups. Our results suggest that sleep does not have a direct effect on morning motor function. Alterations in morning motor symptomatology probably represent a manifestation of motor fluctuations. Sleep fragmentation and spontaneous daytime dozing occurred much more frequently in PD patients than controls. In addition, nocturnal vocalizations and daytime hallucinations occurred only in the PD group.

Using immunofluorescence microscopy we found that gp120 binds to the surface of rat dorsal root ganglia neurons and human neuroblastoma cells but not to rat fibroblasts or glial cells. The binding of gp120 to neurons was eliminated by pretreatment with trypsin, which removes cell-surface proteins, but not with chloroform: methanol, which removes glycolipids. As control, neuronal staining by antisulfatide antibodies was eliminated by pretreatment with chloroform: methanol but not with trypsin. The gp120 binding to neurons was also inhibited by the mouse monoclonal antibody 01, which binds to galactocerebroside and cross-reactive glycoproteins. These studies suggest that the receptor for gp120 on the surface of the dorsal root ganglia neurons is a glycoprotein. This interaction may mediate the effects of human immunodeficiency virus type 1 in sensory neuropathy.

We examined the binding of the gp120 envelope glycoprotein (gp120) of the human immunodeficiency virus (HIV-1) to sulfatide (GalS), galactocerebroside (GalC), and GM1-ganglioside (GM1). The gp120 glycoprotein bound to GalS but not to GalC or GM1 by enzyme-linked immunosorbent assay (ELISA) and by an immunospot assay on nitrocellulose paper. However, it bound to all three glycolipids by an immunospot assay on thin layer chromatography (TLC) plates. In studies to determine whether GalS could be a receptor for gp120 on the surface of cells, gp120 bound to GalS incorporated into the plasma membrane of lymphoid cells as determined by cytofluorometric analysis and immunofluorescence microscopy. These studies indicate that GalS may function as a receptor for gp120 and HIV-1.

Patients infected with HIV-1 frequently have a sensory neuropathy, but the cause is unknown. We found that the gp120 glycoprotein of HIV-1 bound to the surface of cultured rat dorsal root ganglia (DRG) neurons, and activated the complement cascade to lyse the neuronal cells. Cytotoxicity was measured by a 51Cr-release assay, and deposits of the C5b-9 complement complex were detected on the affected cells. As controls, gp120 or complement alone, or rgp120 plus deactivated complement, did not damage the neuronal cells, and fibroblasts were unaffected. The gp120 glycoprotein can thereby damage DRG neurons by complement dependent mechanisms. This interaction may contribute to the development of the sensory neuropathy in AIDS.

We report the presence of antisulfatide antibodies in a patient with type I Gaucher's disease and peripheral neuropathy. The association of Gaucher's disease with hypergammaglobulinemia and monoclonal gammopathy is well documented whereas its association with peripheral neuropathy is rare. We discuss whether antibodies directed against the sulfatide antigen are related to Gaucher's disease or are a coincidental association.