Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.52 (PNGase F)
 1,527 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We are studying a mannose-specific recognition mediating the projection of axons in the synaptic neuropil of the embryonic leech CNS. A functional class of neurons, the sensory afferents, can be distinguished by a mannose-containing epitope that is asparagine-linked to a 130 kDa surface protein and is reactive with the monoclonal antibody Lan3-2. Sensory afferents project as a tightly fasciculated bundle through peripheral nerves but, upon arriving in the CNS, defasciculate into the synaptic neuropil. This defasciculation allows the previously bundled sensory afferents to form an arborization in the synaptic neuropil. Three lines of experimental evidence indicate that the defasciculation is mediated by the sensory afferent's mannose-containing Lan3-2 epitope. The defasciculation is inhibited (1) by blocking the Lan3-2 epitope with Lan3-2 Fab fragments, (2) by cleaving the asparagine-linked carbohydrate moieties from surface proteins with the glycosidase N-glycanase, and (3) by competing for a putative mannose-binding protein with the neoglycoprotein mannose-BSA [albumin, p-aminophenyl alpha-D-mannopyranoside (26 mol monosaccharide/mol albumin)]. In addition to inhibiting the defasciculation, the three perturbation reagents also elicited the refasciculation of axons that had defasciculated prior to their application. These three different experimental approaches provide strong evidence that carbohydrate recognition regulates the projections of sensory afferents in the leech synaptic neuropil. Carbohydrate interactions therefore can play a major role in regulating the neuronal architecture in the CNS.
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PMID:A mannose-specific recognition mediates the defasciculation of axons in the leech CNS. 165 51

In vitro infection by the human immunodeficiency virus (HIV) of CD4+ H9 lymphoblasts is inhibited by a mannose-binding protein (MBP) purified from human serum. In addition, MBP is able to selectively bind to HIV-infected H9 cells and HIV-infected cells from the monocyte cell line U937. These results indicate MBP most likely recognizes high mannose glycans known to be present on gp120 in the domain that is recognized by CD4 and thereby inhibits viral entry to susceptible cells. In support of this contention, recombinant gp120 binds directly to MBP; the binding is saturable, mannan inhibitable, removed by N-glycanase treatment, and dependent on divalent cations.
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PMID:A human serum mannose-binding protein inhibits in vitro infection by the human immunodeficiency virus. 290 56