Linked Life Data

8807600

Source:http://linkedlifedata.com/resource/pubmed/id/8807600

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-11-22
pubmed:abstractText
Staphylococcal neutral phosphatase (NPtase) is a highly cationic bacterial surface bound protein. It has significant affinity for human and rat immunoglobulins in vitro and an electrostatic interaction may be involved. Radioisotopic studies showed that NPtase had a high affinity for the polyanionic structures of the rat renal glomerulus. When the left kidneys of germ-free or naive (non-immune) Wistar rats were perfused with 80 micrograms of I125 NPtase, 21 micrograms of NPtase were found in the left kidneys and 11 micrograms in the isolated glomeruli 15 minutes after perfusion. Deposits of autologous immunoglobulin and C3 were seen in the glomeruli of rats immediately after perfusion with NPtase (15 min) and persisted throughout the 14-day observation period. Histologically, neutrophil influx into the glomerulus was seen at 15 minutes and increased until three hours; subepithelial electron-dense deposits were found after three days and were still visible on day 14. Proteinuria started within the first 24 hours despite the absence of an immune response at this time and was still present on day 14. Similar results were observed in immune deficient athymic nude rats in the early phase. Perfusion of heparin after NPtase inhibited the deposition of IgG and C3 and prevented proteinuria in naive but not in actively immunized rats. This result provides further evidence that specific antibodies to NPtase were not involved in the immune complex-like deposits seen in the early phase. NPtase is a novel molecule, as it reveals both high affinity for the GBM and binding of circulating immunoglobulins, by a non-antigen-antibody mechanism, to form IC-like deposits on the GBM. These deposits are capable of activating the complement system, thus triggering a series of events leading to glomerulonephritis. These results delineate an additional pathway for the pathogenesis of ICGN related to bacterial infection.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0085-2538
pubmed:author
pubmed:issnType
Print
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
290-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Induction of glomerulonephritis in rats with staphylococcal phosphatase: new aspects in post-infectious ICGN.
pubmed:affiliation
Department of Immunology, Institute of Medical Microbiology, Freiburg University, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't