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Biomedical subjects

G M Liuzzi

Publications and source records attributed to G M Liuzzi.

27 records · Page 2Linked to original sources
PubMed1991

Detection of cerebrospinal fluid antibodies against myelin basic protein in patients with AIDS dementia complex.

We evaluated cerebrospinal fluid (CSF) antibody levels against a lipid-free, denatured form of myelin basic protein (LF-MBP) in 11 patients with AIDS dementia complex (ADC) by using an enzyme-linked immunosorbent assay (ELISA). In 9 out of 11 patients, anti-LF-MBP antibody levels were significantly higher than those observed both in 15 human immunodeficiency virus (HIV)-infected patients without neurological disorders and in 9 anti-HIV-negative subjects affected by other neurological diseases. Furthermore, we followed up anti-MBP levels in 5 out of the 11 ADC patients and detected a strict relationship with the encephalopathy progression. At the same time, with the aim to detect early demyelinating events we investigated CSF antibody levels against a lipid-bound, native-like form of MBP (LB-MBP). Results did not show any significant difference between LF-MBP and LB-MBP in terms of antibody reactivity. The detection of anti-MBP antibodies in CSF may provide the opportunity to assess a diagnostic tool for discovering demyelinating lesions in ADC patients.

AIDS Dementia Complex↗
PubMed1991

Purification of lipid-associated basic protein from guinea pig spinal-cord myelin.

Myelin basic protein (MBP) was purified from guinea pig spinal-cord in a native-like form retaining the binding to all the myelin lipids. Since the guinea pig MBP was found to be much more labile than the corresponding MBP from bovine brain, the original procedure based on the use of hydroxyapatite and detergents was slightly modified as reported here. The product of this purification, lipid-bound MBP, may represent an alternative to lipid-free MBP for the induction, the study and the treatment of experimental allergic encephalomyelitis.

Animals↗
PubMed1991

Myelin basic protein in lipid-bound form induces experimental allergic encephalomyelitis and demyelination in Lewis rat.

Myelin basic protein (MBP) was isolated from guinea-pig spinal cord in a form retaining the binding to all the myelin lipids. This new, lipid-bound and native-like preparation was used to immunize Lewis rats in complete Freund's adjuvant (CFA) in order to produce experimental allergic encephalomyelitis (EAE). The clinical features were compared with those of Lewis rats immunized with lipid-free MBP (LF-MBP), myelin, LF-MBP + octyl-POE (the non-ionic detergent used for the purification of LB-MBP) and octyl-POE alone. The clinical observation indicate that LB-MBP exerts an encephalitogenic activity on Lewis rats which is more intense than LF-MBP and includes demyelinating lesions in the central nervous system (CNS). The data suggest that LB-MBP is a new encephalitogenic antigen, which may induce more intensive immunization in rats and may be relevant in humans for autoimmune demyelinating diseases of the CNS.

Animals↗
PubMed1991

Zinc as an inhibitor of myelin basic protein proteolytic breakdown in the central nervous system.

It is known that central nervous system myelin contains proteolytic enzymes which degrade the myelin basic protein (MBP). We have found that zinc acetate is able to inhibit MBP cleavage at concentrations of 1 mM or higher. Furthermore, the Zn-inhibitable MBP-degrading activity was found to be water-soluble and able to recognize MBP also if this protein was protected by its lipidic environment in the native-like, lipid-bound form. Data presented here suggest a Zn-dependent metallo-protease which recognize MBP as a substrate probably even in the myelin sheath, when the protein is not yet released from the membrane.

Animals↗
PubMed1990

Lipid-bound, native-like, myelin basic protein. Batch-wise preparation and perspectives for use in demyelinating diseases.

Batch purification of the myelin basic protein (MBP) in the lipid-bound form was obtained from bovine brain white matter by using the slightly polydisperse nonionic detergent, n-octyl-pentaoxyethylene (octyl-POE) and hydroxyapatite. This large-scale procedure can also be carried out in laboratories without chromatographic equipment, and is applicable to small amounts of myelin. More interestingly, removal and inhibition of the proteolytic activity associated with myelin allowed us to obtain more stable and intact forms of the protein when compared with MBP isolated in the lipid-bound form by our previous method. Since it retains binding to all myelin lipids, this purified MBP may be considered as being in a native-like form. In this article, we suggest why this more intact form of MBP could be used to advantage as an alternative to lipid-free, water-soluble MBP in the study, detection, and treatment of myelin damage in pathology.

Animals↗