Rice hypersensitivity associated with serum complement depression.

R C Strunk; J L Pinnas; T J John; R C Hansen; J L Blazovich

doi:10.1111/j.1365-2222.1978.tb00447.x

Home/Archive/PubMed

PubMed · 627042

Rice hypersensitivity associated with serum complement depression.

R C Strunk·J L Pinnas·T J John·R C Hansen·J L Blazovich

View original source ↗Export metadata ↓

Abstract

The source did not provide an abstract. Follow the original record for more information.

Explore related subjects

Antibodies Child, Preschool Complement C3 Complement C4 Complement Factor B Complement System Proteins Food Hypersensitivity Histamine Humans Infant Oryza Radioallergosorbent Test Case Reports Journal Article Research Support, U.S. Gov't, P.H.S.

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

R C Strunk, J L Pinnas, T J John, R C Hansen, J L Blazovich. 1978. Rice hypersensitivity associated with serum complement depression.. https://doi.org/10.1111/j.1365-2222.1978.tb00447.x

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2021

ERBB3 overexpression due to miR-205 inactivation confers sensitivity to FGF, metabolic activation, and liability to ERBB3 targeting in glioblastoma.

In glioblastoma (GBM), the most frequent and lethal brain tumor, therapies suppressing recurrently altered signaling pathways failed to extend survival. However, in patient subsets, specific genetic lesions can confer sensitivity to targeted agents. By exploiting an integrated model based on patient-derived stem-like cells, faithfully recapitulating the original GBMs in vitro and in vivo, here, we identify a human GBM subset (∼9% of all GBMs) characterized by ERBB3 overexpression and nuclear accumulation. ERBB3 overexpression is driven by inheritable promoter methylation or post-transcriptional silencing of the oncosuppressor miR-205 and sustains the malignant phenotype. Overexpressed ERBB3 behaves as a specific signaling platform for fibroblast growth factor receptor (FGFR), driving PI3K/AKT/mTOR pathway hyperactivation, and overall metabolic upregulation. As a result, ERBB3 inhibition by specific antibodies is lethal for GBM stem-like cells and xenotransplants. These findings highlight a subset of patients eligible for ERBB3-targeted therapy.

Antibodies↗

PubMed1992

Dissociation of complexes between 70 kDa stress proteins and presecretory proteins is facilitated by a cytosolic factor.

Members of the 70 kDa stress protein family were shown previously to facilitate the posttranslational translocation of presecretory proteins into the endoplasmic reticulum and protein precursors into mitochondria. To identify proteins that interact with 70 kDa stress proteins during the early steps of posttranslational translocation, polyclonal antibodies were raised against purified yeast cytosolic stress proteins. They were used to immunoprecipitate complexes between 70 kDa stress proteins and a radiolabeled presecretory protein, prepro-alpha-factor, that was translated in vitro. Complexes between prepro-alpha-factor and 70 kDa stress proteins were stable, but could be dissociated in the presence of ATP and crude cytosolic extracts from yeast. These results are consistent with the idea that 70 kDa stress proteins act as molecular chaperones in translocation by binding to precursor proteins before or during their passage across membranes.

Antibodies↗

PubMed1992

The bioactivation of 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954)--II. A comparison of an Escherichia coli nitroreductase and Walker DT diaphorase.

A nitroreductase enzyme that has been isolated from Escherichia coli B is capable of bioactivating CB1954 [5-(aziridin-1-yl)-2,4-dinitrobenzamide] to a cytotoxic agent, a property shared with the mammalian enzyme Walker DT diaphorase [NAD(P)H dehydrogenase (quinone), EC 1.6.99.2] as isolated from Walker cells. In contrast to Walker DT diaphorase, which can only reduce the 4-nitro group of CB1954, the E. coli nitroreductase can reduce either (but not both) nitro groups of CB1954 to the corresponding hydroxylamino species. The two hydroxylamino species are formed in equal proportions and at the same rates. CB1954 is reduced much more rapidly by the E. coli nitroreductase than by Walker DT diaphorase. If the reduction of CB1954 was carried out in the presence of V79 cells (which are insensitive to CB1954) a large cytotoxic effect was evident. This cytotoxicity was only observed under conditions in which the E. coli nitroreductase or Walker DT diaphorase reduced the drug. It is proposed that E. coli B nitroreductase would be a suitable enzyme for antibody-directed enzyme prodrug therapy (ADEPT) in combination with CB1954.

Antibodies↗