Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0085437 (bacterial meningitis)
 4,038 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Seven cases of necrotizing lymphadenitis (NEL) including a pair of male siblings, a female suffering from non-bacterial meningitis, and two cases with the proliferation of monocytes and/or macrophages in the bone marrow are reported. This disease is clinically documented by the occurrence in young adults usually accompanied by painful cervical lymphadenopathy with fever and leukopenia (below 4,000/mm3). Morphological features were characterized by nuclear debris from degenerated lymphocytes and the appearance of blastoid cells and/or immunoblasts and macrophages. Ultrastructurally, tubular inclusions with a close relation to the endoplasmic reticulum were observed in various kinds of cells in the lesion. Immunohistochemical studies revealed that the ratio of helper/suppressor T-lymphocytes became low at the active stage and returned to normal range at the recovery stage. By immuno-histochemical study it was confirmed that suppressor cells mainly corresponded to large transformed lymphocytes and/or immunoblasts and helper cells were degenerated by an unknown agent. Though the pathogenesis of NEL is still uncertain, it is suggested that T-lymphocytes are mainly involved during the course of the disease and lymphocytes show cellular debris or blastoid transformation.
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PMID:Necrotizing lymphadenitis. Electron microscopical and immunohistochemical study. 331 May 16

The importance of death receptor (DR) signaling in embryonic development and physiological homeostasis is well established, as is the existence of several molecules that modulate DRs function, among them Fas Apoptotis Inhibitory Molecules. Although FAIM1, FAIM2, and FAIM3 inhibit Fas-induced cell death, they are not structurally related, nor do they share expression patterns. Moreover, they inhibit apoptosis through completely different mechanisms. FAIM1 and FAIM2 protect neurons from DR-induced apoptosis and are involved in neurite outgrowth and neuronal plasticity. FAIM1 inhibits Fas ligand- and tumor necrosis factor alpha-induced apoptosis by direct interaction with Fas receptor and through the stabilization of levels of X-linked inhibitor of apoptosis protein, a potent anti-apoptotic protein that inhibits caspases. Low FAIM1 levels are found in Alzheimer's disease, thus sensitizing neurons to tumor necrosis factor alpha and prompting neuronal loss. FAIM2 protects from Fas by direct interaction with Fas receptor, as well as by modulating calcium release at the endoplasmic reticulum through interaction with Bcl-xL. Several studies prove the role of FAIM2 in diseases of the nervous system, such as ischemia, bacterial meningitis, and neuroblastoma. The less characterized member of the FAIM family is FAIM3, which is expressed in tissues of the digestive and urinary tracts, bone marrow and testes, and restricted to the cerebellum in the nervous system. FAIM3 protects against DR-induced apoptosis by inducing the expression of other DR-antagonists such as CFLAR or through the interaction with the DR-adaptor protein Fas-associated via death domain. FAIM3 null mouse models reveal this protein as an important mediator of inflammatory autoimmune responses such as those triggered in autoimmune encephalomyelitis. Given the differences between FAIMs and the variety of processes in which they are involved, here we sought to provide a concise review about these molecules and their roles in the physiology and pathology of the nervous system. Even though they share name and inhibit Fas-induced cell death, Fas apoptotic inhibitory molecules (FAIMs) are not structurally related and inhibit apoptosis through completely different mechanisms. In this review, we describe FAIM1, FAIM2, and FAIM3 functions in the nervous system, and their implication in diverse pathologies such as neurodegenerative disease, cancer, or autoimmune diseases.
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PMID:Fas apoptosis inhibitory molecules: more than death-receptor antagonists in the nervous system. 2738 39