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Sequencing of the purified bovine enzyme showed it to be a member of the Quiescin-sulfhydryl oxidase (QSOX) family. Bovine milk QSOX1 is highly active toward reduced RNase and with the model substrate dithiothreitol.
QSOX1 might be a lung cancer tissue-derived biomarker and be involved in the promotion of lung cancers, and thus can be a therapeutic target for lung cancers.
This study provides a key example of the effect of glycosylation on Golgi exit and contributes to an understanding of late secretory sorting and quality control.
High QSOX1 expression correlates with tumor invasiveness
High QSOX1 expression is a strong and independent factor of reduced survival in breast cancer and may represent a biomarker for aggressive disease and a potential treatment target
Data indicate ebselen as an in vitro inhibitor of quiescin sulfhydryl oxidase 1 (QSOX1) enzymatic activity.
QSOX1 immunoexpression was observed in the non-neoplastic cerebellum samples and the medulloblastoma samples
High levels of QSOX1 RNA expression is associated with breast cancer.
these studies suggest that QSOX1 is a predictive biomarker for luminal cancers and that it may be a useful target for elusive luminal B disease
QSOX1 may be revealed as an important player in cancer detection and prognosis. Defining the mechanism(s) of QSOX1 activity in tumors and in in vivo models will provide important insights into how to target QSOX1 with anti-neoplastic agents.
Examination of the unusual kinetics of QSOX1 toward cysteine and glutathione at low micromolar concentrations suggests that circulating QSOX1 is unlikely to significantly contribute to the oxidation of these monothiols in plasma
QSOX1 may be involved in neuroblastoma differentiation and regression and may thus function as a biomarker for identifying risk groups for this neoplasm.
QSOX1 is induced by hypoxic stimuli and identified that QSOX1 is a direct target of HIF-1.
Data suggest that isoenzyme QSOX1A is secreted from mammalian cells despite transmembrane domain; QSOX1A is cleaved at internal sites and processed within Golgi apparatus to yield soluble enzyme that forms dimer upon cleavage of C-terminal domain.
QSOX1 is a potential new prognostic marker which may prove of use in the staging of breast tumours and the stratification of breast cancer patients.
QSOX1 activity was required for incorporation of laminin into the extracellular matrix (ECM) synthesized by fibroblasts, and ECM produced without QSOX1 was defective in supporting cell-matrix adhesion.
These results propose for the first time possible roles for QSOX1 in atherosclerosis.
Taken together, our results suggest that the mechanism of QSOX1-mediated tumor cell invasion is by activation of MMP-2 and MMP-9.
Data suggested that the C449-C452 motif was essential for the activity of human QSOX 1b; the C70-C73 motif was fundamental in electron transfer from thiol-containing substrate including reduced proteins, DTT, GSH.
A partial QSOX1 crystal structure reveals a single-chain pseudo-dimer mimicking the quaternary structure of Erv enzymes.
Serum thioredoxin reductase is highly increased in mice with hepatocellular carcinoma and its activity is restrained by several mechanisms, in particular, by the serum QSOX1.
QSOX1 inhibits autophagy in breast cancer cells.
cloned skin SOx cDNA and characterized it as one of the disulfide (S-S) cross-linking enzymes
In seminiferous tubules, where a high level of expression was noticed, QSOX might play an important physiological role in sperm function and serve as a marker for the diagnosis of male infertility.
This gene encodes a protein that contains domains of thioredoxin and ERV1, members of two long-standing gene families. The gene expression is induced as fibroblasts begin to exit the proliferative cycle and enter quiescence, suggesting that this gene plays an important role in growth regulation. Two transcript variants encoding two different isoforms have been found for this gene.
quiescin Q6 sulfhydryl oxidase 1
, sulfhydryl oxidase 1
, quiescin Q6 sulfhydryl oxidase 2
, quiescin Q6-like 1
, sulfhydryl oxidase 1-like
, FAD-dependent sulfhydryl oxidase-2
, skin sulfhydryl oxidase
, FAD-dependent sulfhydryl oxidase-3
, glandular epithelial cells protein 3