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Biomedical subjects

R M Bashir

Publications and source records attributed to R M Bashir.

25 records · Page 2Linked to original sources
PubMed1980

Molecular features of immunoreactive myelin basic protein in cerebrospinal fluid of persons with multiple slcerosis.

The molecular weight of the myelin basic protein (BP)-like material appearing in cerebrospinal fluid (CSF) of 2 persons with active-phase multiple sclerosis (MS) and 3 with recent cerebral infarctions was determined by gel filtration chromatography under acidic conditions. Column fractions were examined by radioimmunoassay for BP peptide 43-88 antigen as well as for binding activity to BP. Material cross-reactive with BP peptide 43-88 eluted over a wide spectrum of molecular weights. Greater representation of lower molecular weight species occurred in MS. Fractionated CSF from 2 patients with MS and 2 with cerebral infarction contained binding activity, presumably antibody, to BP which was greater than that in unfractionated CSF. Binding to BP was also examined in unfractionated CSF from 70 persons, including 16 with MS and 36 with other neurological diseases. Although CSF from MS patients showed higher binding, the presence of BP binding activity was not specific for MS. Our findings suggest that the antigen cross-reacting with BP and its fragments in CSF appears in a spectrum of molecular weight species, with lower forms predominating in MS. The detection of binding activity to BP as well as its enhancement by treatment at low pH suggest that the BP-like antigen in CSF may exist in free as well as in complexed forms.

Adolescent↗
PubMed1980

Immunoreactive myelin basic protein in the cerebrospinal fluid in neurological disorders.

Cerebrospinal fluid from 582 persons was analyzed by a double-antibody radioimmunoassay for the presence of material cross-reactive with peptide 43-88 of human myelin basic protein (BP). In a group of 104 patients with multiple sclerosis (MS), 23 of 33 individuals clinically judged to have had an exacereation within two weeks prior to the time CSF was obtained had detectable material ranging from 2 to 200 ng/ml. In the remaining 71 MS patients who either were stable or had had an exacerbation more than two weeks before, only 1 patient had a marginally elevated level of immunoreactive material. CSF from 53 persons with cerebrovascular disease was studied, and 13 of 29 with recent infarctions had values of 2 to 540 ng/ml. The degree of elevation in strokes generally paralleled the predicted volume of the lesion, but the amounts detected did not correlate quite so closely temporally with onset as they did with the periods of active disease in MS. Of the remaining 425 patients, 29 had immunoreactive material of 2 to 400 ng/ml in their CSF. Most of these patients with detectable material had acute diseases known to affect the myelin sheath. Eight of 10 persons with acute disseminated encephalomyelitis had no detectable material. The presence in CSF of material cross-reactive with BP peptide 43-88 does not have diagnostic specificity for MS but can be used as a means for determining recent myelin injury. The type of BP peptide formed and mechanisms for clearance of BP and BP peptides may be important in determining the biological consequences following release of this potentially immunogenic material from the central nervous system.

Antigen-Antibody Reactions↗
PubMed1980

Metabolism of a peptide of human myelin basic protein in the rabbit.

Material cross-reactive with myelin basic protein (BP) peptide 43-88 has been identified as a major BP-like antigen appearing in human cerebrospinal fluid during acute myelin injury. In an effort to develop a means for detecting this material in the more accessible body fluids of blood and urine, as well as to determine its metabolic fate, the manner in which rabbits handle human BP peptide 43-88 was investigated. Unlabeled peptide was administered intravenously, and its concentration in plasma was monitored by radioimmunoassay. In studies of 10 rabbits, the peptide disappeared from blood in two phases, the first showing a half-life of 6.0 +/- 1.2 minutes and the second a half-life of 51.6 +/- 5.4 minutes. Organ-exclusion experiments indicated a rapid clearance, predominantly by the kidney, for the peptide, with tubular reabsorption and cleavage into smaller peptide fragments a probable catabolic mechanism.

Animals↗
PubMedDate not supplied

Neurotrophins and their receptors in nerve injury and repair.

Cytokines are a heterogenous group of polypeptide mediators that have been associated with activation of numerous functions, including the immune system and inflammatory responses. The cytokine families include, but are not limited to, interleukins (IL-I alpha, IL-I beta, ILIra and IL-2-IL-15), chemokines (IL-8/ NAP-I, NAP-2, MIP-I alpha and beta, MCAF/MCP-1, MGSA and RANTES), tumor necrosis factors (TNF-alpha and TNF-beta), interferons (INF-alpha, beta and gamma), colony stimulating factors (G-CSF, M-CSF, GM-CSF, IL-3 and some of the other ILs), growth factors (EGF, FGF, PDGF, TGF alpha, TGF beta and ECGF), neuropoietins (LIF, CNTF, OM and IL-6), and neurotrophins (BDNF, NGF, NT-3-NT-6 and GDNF). The neurotrophins represent a family of survival and differentiation factors that exert profound effects in the central and peripheral nervous system (PNS). The neurotrophins are currently under investigation as therapeutic agents for the treatment of neurodegenerative disorders and nerve injury either individually or in combination with other trophic factors such as ciliary neurotrophic factor (CNTF) or fibroblast growth factor (FGF). Responsiveness of neurons to a given neurotrophin is governed by the expression of two classes of cell surface receptor. For nerve growth factor (NGF), these are p75NTR (p75) and p140trk (referred to as trk or trkA), which binds both BDNF and neurotrophin (NT)-4/5, and trkC receptor, which binds only NT-3. After binding ligand, the neurotrophin-receptor complex is internalized and retrogradely transported in the axon to the soma. Both receptors undergo ligand-induced dimerization, which activates multiple signal transduction pathways. These include the ras-dependent pathway utilized by trk to mediate neurotrophin effects such as survival and differentiation. Indeed, cellular diversity in the nervous system evolves from the concerted processes of cell proliferation, differentiation, migration, survival, and synapse formation. Neural adhesion and extracellular matrix molecules have been shown to play crucial roles in axonal migration, guidance, and growth cone targeting. Proinflammatory cytokines, released by activated macrophages and monocytes during infection, can act on neural targets that control thermogenesis, behavior, and mood. In addition to induction of fever, cytokines induce other biological functions associated with the acute phase response, including hypophagia and sleep. Cytokine production has been detected within the central nervous system as a result of brain injury, following stab wound to the brain, during viral and bacterial infections (AIDS and meningitis), and in neurodegenerative processes (multiple sclerosis and Alzheimer's disease). Novel cytokine therapies, such as anticytokine antibodies or specific receptor antagonists acting on the cytokine network may provide an optimistic feature for treatment of multiple sclerosis and other diseases in which cytokines have been implicated.

Animals↗