Vertebrate keratinization evolved into cornification mainly due to transglutaminase and sulfhydryl oxidase activities on epidermal proteins: an immunohistochemical survey

2021 ◽  
Author(s):  
Lorenzo Alibardi
Keyword(s):  
Sulfhydryl Oxidase

scholarly journals Quiescin Sulfhydryl Oxidase 1 (QSOX1) Secreted by Lung Cancer Cells Promotes Cancer Metastasis

2018 ◽  
Vol 19 (10) ◽  
pp. 3213 ◽  
Author(s):  
Hye-Jin Sung ◽  
Jung-Mo Ahn ◽  
Yeon-Hee Yoon ◽  
Sang-Su Na ◽  
Young-Jin Choi ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Cancer Cells ◽  
Cancer Metastasis ◽  
Lung Cancer Cells ◽  
Migration And Invasion ◽  
Sulfhydryl Oxidase ◽  
Lung Cancers ◽  
Normal Tissues ◽  
Cancer Tissues ◽  
Quiescin Sulfhydryl Oxidase

As lung cancer shows the highest mortality in cancer-related death, serum biomarkers are demanded for lung cancer diagnosis and its treatment. To discover lung cancer protein biomarkers, secreted proteins from primary cultured lung cancer and adjacent normal tissues from patients were subjected to LC/MS–MS proteomic analysis. Quiescin sulfhydryl oxidase (QSOX1) was selected as a biomarker candidate from the enriched proteins in the secretion of lung cancer cells. QSOX1 levels were higher in 82% (51 of 62 tissues) of lung cancer tissues compared to adjacent normal tissues. Importantly, QSOX1 serum levels were significantly higher in cancer patients (p < 0.05, Area Under curve (AUC) = 0.89) when measured by multiple reaction monitoring (MRM). Higher levels of QSOX1 were also uniquely detected in lung cancer tissues, among several other solid cancers, by immunohistochemistry. QSOX1-knock-downed Lewis lung cancer (LLC) cells were less viable from oxidative stress and reduced migration and invasion. In addition, LLC mouse models with QSOX1 knock-down also proved that QSOX1 functions in promoting cancer metastasis. In conclusion, 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.

scholarly journals Three Conserved Regions in Baculovirus Sulfhydryl Oxidase P33 Are Critical for Enzymatic Activity and Function

2017 ◽  
Vol 91 (23) ◽  
Author(s):  
Wenhua Kuang ◽  
Huanyu Zhang ◽  
Manli Wang ◽  
Ning-Yi Zhou ◽  
Fei Deng ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Active Site ◽  
Salt Bridge ◽  
Sulfhydryl Oxidase ◽  
Dimer Interface ◽  
Conserved Regions ◽  
Occlusion Bodies ◽  
Budded Virus ◽  
And Function ◽  
Substrate Proteins

ABSTRACT Baculoviruses encode a conserved sulfhydryl oxidase, P33, which is necessary for budded virus (BV) production and multinucleocapsid occlusion-derived virus (ODV) formation. Here, the structural and functional relationship of P33 was revealed by X-ray crystallography, site-directed mutagenesis, and functional analysis. Based on crystallographic characterization and structural analysis, a series of P33 mutants within three conserved regions, i.e., the active site, the dimer interface, and the R127-E183 salt bridge, were constructed. In vitro experiments showed that mutations within the active site and dimer interface severely impaired the sulfhydryl oxidase activity of P33, while the mutations in the salt bridge had a relatively minor influence. Recombinant viruses containing mutated P33 were constructed and assayed in vivo. Except for the active-site mutant AXXA, all other mutants produced infectious BVs, although certain mutants had a decreased BV production. The active-site mutant H114A, the dimer interface mutant H227D, and the salt bridge mutant R127A-E183A were further analyzed by electron microscopy and bioassays. The occlusion bodies (OBs) of mutants H114A and R127A-E183A had a ragged surface and contained mostly ODVs with a single nucleocapsid. The OBs of all three mutants contained lower numbers of ODVs and had a significantly reduced oral infectivity in comparison to control virus. Crystallographic analyses further revealed that all three regions may coordinate with one another to achieve optimal function of P33. Taken together, our data revealed that all the three conserved regions are involved in P33 activity and are crucial for virus morphogenesis and peroral infectivity. IMPORTANCE Sulfhydryl oxidase catalyzes disulfide bond formation of substrate proteins. P33, a baculovirus-encoded sulfhydryl oxidase, is different from other cellular and viral sulfhydryl oxidases, bearing unique features in tertiary and quaternary structure organizations. In this study, we found that three conserved regions, i.e., the active site, dimer interface, and the R127-E183 salt bridge, play important roles in the enzymatic activity and function of P33. Previous observations showed that deletion of p33 results in a total loss of budded virus (BV) production and in morphological changes in occlusion-derived virus (ODV). Our study revealed that certain P33 mutants lead to occlusion bodies (OBs) with a ragged surface, decreased embedded ODVs, and reduced oral infectivity. Interestingly, some P33 mutants with impaired ODV/OB still retained BV productivity, indicating that the impacts on BV and on ODV/OB are two distinctly different functions of P33, which are likely to be performed via different substrate proteins.

Stoichiometry of the Reaction Catalyzed by Skin Sulfhydryl Oxidase

1994 ◽  
Vol 21 (6) ◽  
pp. 394-396 ◽  
Author(s):  
Hiromichi Yamada ◽  
Yasushi Suga ◽  
Kenji Takamori ◽  
Hideoki Ogawa
Keyword(s):  
Sulfhydryl Oxidase

scholarly journals The Quiescin Sulfhydryl Oxidase (hQSOX1b) Tunes the Expression of Resistin-Like Molecule Alpha (RELM-α or mFIZZ1) in a Wheat Germ Cell-Free Extract

PLoS ONE ◽  
2013 ◽  
Vol 8 (1) ◽  
pp. e55621 ◽  
Author(s):  
Wael Gad ◽  
Meera G. Nair ◽  
Karolien Van Belle ◽  
Khadija Wahni ◽  
Henri De Greve ◽  
...  
Keyword(s):  
Germ Cell ◽  
Wheat Germ ◽  
Cell Free Extract ◽  
Sulfhydryl Oxidase ◽  
Quiescin Sulfhydryl Oxidase

Mammalian Sulfhydryl Oxidase

2002 ◽  
Author(s):  
Violeta Janolino ◽  
Harold Swaisgood
Keyword(s):  
Sulfhydryl Oxidase

Expression of the sulfhydryl oxidase ALR (Augmenter of Liver Regeneration) in adult rat brain

2005 ◽  
Vol 1048 (1-2) ◽  
pp. 87-97 ◽  
Author(s):  
Anna Tury ◽  
Georges Mairet-Coello ◽  
Thomas Lisowsky ◽  
Bernadette Griffond ◽  
Dominique Fellmann
Keyword(s):  
Liver Regeneration ◽  
Rat Brain ◽  
Sulfhydryl Oxidase ◽  
Adult Rat ◽  
Augmenter Of Liver Regeneration ◽  
Adult Rat Brain

scholarly journals Characterization of recombinant rice quiescin sulfhydryl oxidase and its improvement effect on wheat flour-processing quality

2020 ◽  
Vol 333 ◽  
pp. 127492
Author(s):  
Nian Du ◽  
Zhen-Cheng Wei ◽  
Yuan-Yuan Deng ◽  
Yan Zhang ◽  
Xiao-Jun Tang ◽  
...  
Keyword(s):  
Wheat Flour ◽  
Processing Quality ◽  
Sulfhydryl Oxidase ◽  
Improvement Effect ◽  
Quiescin Sulfhydryl Oxidase

Nonidentity of sulfhydryl oxidase and γ-glutamyltransferase in bovine milk

1981 ◽  
Vol 211 (2) ◽  
pp. 731-737 ◽  
Author(s):  
Mary B. Sliwkowski ◽  
Mark X. Sliwkowski ◽  
Harold E. Swaisgood ◽  
H.Robert Horton
Keyword(s):  
Bovine Milk ◽  
Sulfhydryl Oxidase
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