Topic
Hemoglobin complex
About: Hemoglobin complex is a research topic. Over the lifetime, 47 publications have been published within this topic receiving 631 citations.
Papers
TL;DR: Classifying 532 cancers, representing six tissue-based types, into ten proteome-based, pan-cancer subtypes that cut across tumor lineages finds two distinct subtypes both involve the immune system and one associated with the adaptive immune response and T-cell activation.
Abstract: Mass-spectrometry-based proteomic profiling of human cancers has the potential for pan-cancer analyses to identify molecular subtypes and associated pathway features that might be otherwise missed using transcriptomics. Here, we classify 532 cancers, representing six tissue-based types (breast, colon, ovarian, renal, uterine), into ten proteome-based, pan-cancer subtypes that cut across tumor lineages. The proteome-based subtypes are observable in external cancer proteomic datasets surveyed. Gene signatures of oncogenic or metabolic pathways can further distinguish between the subtypes. Two distinct subtypes both involve the immune system, one associated with the adaptive immune response and T-cell activation, and the other associated with the humoral immune response. Two additional subtypes each involve the tumor stroma, one of these including the collagen VI interacting network. Three additional proteome-based subtypes-respectively involving proteins related to Golgi apparatus, hemoglobin complex, and endoplasmic reticulum-were not reflected in previous transcriptomics analyses. A data portal is available at UALCAN website.
496 citations
TL;DR: Recombinant AOP2 prevented induced as well as noninduced methemoglobin formation in erythrocyte hemolysates, indicating its antioxidant properties, and is part of a sophisticated system developed to protect and support ery Throcytes in their many physiological functions.
Abstract: Antioxidant protein 2 (AOP2) is a member of a family of thiol-specific antioxidants, recently renamed peroxiredoxins, that evolved as part of an elaborate system to counteract and control detrimental effects of oxygen radicals. AOP2 is found in endothelial cells, erythrocytes, monocytes, T and B cells, but not in granulocytes. AOP2 was found solely in the cytoplasm and was not associated with the nuclear or membrane fractions; neither was it detectable in plasma. Further experiments focused on the function of AOP2 in erythrocytes where it is closely associated with the hemoglobin complex, particularly with the heme. An investigation of the mechanism of this interaction demonstrated that the conserved cysteine-47 in AOP2 seems to play a role in AOP2-heme interactions. Recombinant AOP2 prevented induced as well as noninduced methemoglobin formation in erythrocyte hemolysates, indicating its antioxidant properties. We conclude that AOP2 is part of a sophisticated system developed to protect and support erythrocytes in their many physiological functions.
53 citations
TL;DR: It is shown that the intact hemoglobin complex can be sampled directly from thin tissue sections of mouse liver and correlated to a visible vascular feature, paving the way for native mass spectrometry imaging.
Abstract: Native mass spectrometry seeks to probe noncovalent protein interactions in terms of protein quaternary structure, protein-protein and protein-ligand complexes. The ultimate goal is to link the understanding of protein interactions to the protein environment by visualizing the spatial distribution of noncovalent protein interactions within tissue. Previously, we have shown that noncovalently bound protein complexes can be directly probed via liquid extraction surface analysis from dried blood spot samples, where hemoglobin is highly abundant. Here, we show that the intact hemoglobin complex can be sampled directly from thin tissue sections of mouse liver and correlated to a visible vascular feature, paving the way for native mass spectrometry imaging.
39 citations
Patent•
4 May 1983TL;DR: In this paper, a method for the production of stroma-free, non-heme protein-free hemoglo by use of zinc ion to promote precipitation of a zinc ion-bound insoluble hemoglobin complex, followed by membrane ultrafiltration of the zinc-hemoglobin complex from the filtrate fluid medium, preferably with a saline dialyzate.
Abstract: A method for the production of stroma-free, non-heme protein-free hemoglo by use of zinc ion to promote precipitation of a zinc ion-bound insoluble hemoglobin complex, followed by membrane ultrafiltration of the zinc-hemoglobin complex from the filtrate fluid medium, preferably with a saline dialyzate.
37 citations
TL;DR: This study is the first to report proteome response of carp intestinal mucosa against A. hydrophila infection; information obtained contribute to understanding defence mechanisms of carpestinal mucosa.
34 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2021 | 2 |
| 2020 | 3 |
| 2019 | 2 |
| 2018 | 1 |
| 2017 | 2 |
| 2016 | 2 |