The only national patient waiting list and an online database system, called UNet, that links all of the professionals involved in the donation and transplantation system for the collection, storage, analysis, and publication of all OPTN data pertaining to the patient waiting list, organ matching, and transplants. The system contains data regarding every organ donation and transplant event occurring in the U.S. since October 1, 1987. UNet is a fail-safe, 24/7, secure Internet-based transplant information database created to enable the nation''''s organ transplant institutions to: * register patients for transplants * match donated organs to waiting patients * manage the time-sensitive, life-critical data of all patients, before and after their transplants Data reports are available by type: National Data, Regional Data, State Data, Center Data, Build Advanced Report, and Annual Report Data. UNet is being used right now by all of the nation''''s organ transplant programs, organ procurement organizations, and histocompatibility (tissue typing) laboratories working cooperatively to efficiently share a limited number of donated organs among thousands of patients.

Context

Transplants in the U.S. by Recipient Gender Page 1 of 1 U.S. Transplants Performed : January 1, 1988 - December 31, 2021 For Organ = Liver, Format = Portrait

https://optn.transplant.hrsa.gov/data/view-data-reports/national-data/#

Content

Transplants in the U.S. by Recipient Gender

Acknowledgements

organdonor.gov

https://optn.transplant.hrsa.gov/data/view-data-reports/national-data/#

Inspiration

Transplants and organ donors.

Causes of liver disease and HCC among men who received liver transplant in the U.S. from 2010 to 2019 by frequency and percentage.

Enables K63-linked polyubiquitin modification-dependent protein binding activity. Acts upstream of or within negative regulation of canonical NF-kappaB signal transduction and protein localization. Located in perinuclear region of cytoplasm. Is expressed in several structures, including alimentary system; eye; genitourinary system; musculoskeletal system; and nervous system. Used to study low tension glaucoma. Human ortholog(s) of this gene implicated in Paget's disease of bone; amyotrophic lateral sclerosis (multiple); and glaucoma (multiple). Orthologous to human OPTN (optineurin). [provided by Alliance of Genome Resources, Jul 2025]

Causes of liver disease and HCC among women who received liver transplant in the U.S. from 2010 to 2019 by frequency and percentage.

ENCODES a protein that exhibits identical protein binding (ortholog); TFIIIA-class transcription factor binding (ortholog); ubiquitin binding (ortholog); INVOLVED IN cellular response to hydrogen peroxide (ortholog); cellular response to L-glutamate (ortholog); cellular response to nerve growth factor stimulus (ortholog); PARTICIPATES IN mitochondrial autophagy pathway; ASSOCIATED WITH amyotrophic lateral sclerosis (ortholog); amyotrophic lateral sclerosis type 10 (ortholog); amyotrophic lateral sclerosis type 12 (ortholog); FOUND IN axon (ortholog); neuronal cell body (ortholog); perinuclear region of cytoplasm (ortholog)

Non-traditional data signals from social media and employment platforms for OPTN stock analysis

Causes of liver disease and HCC among adult liver transplant recipients in the U.S. from 2010 to 2019 by frequency and percentage.

Protein-Protein, Genetic, and Chemical Interactions for OPTN (Homo sapiens) curated by BioGRID (https://thebiogrid.org); DEFINITION: optineurin

Protein-Protein, Genetic, and Chemical Interactions for Sirohi K (2013):M98K-OPTN induces transferrin receptor degradation and RAB12-mediated autophagic death in retinal ganglion cells. curated by BioGRID (https://thebiogrid.org); ABSTRACT: Mutations in the autophagy receptor OPTN/optineurin are associated with the pathogenesis of glaucoma and amyotrophic lateral sclerosis, but the underlying molecular basis is poorly understood. The OPTN variant, M98K has been described as a risk factor for normal tension glaucoma in some ethnic groups. Here, we examined the consequence of the M98K mutation in affecting cellular functions of OPTN. Overexpression of M98K-OPTN induced death of retinal ganglion cells (RGC-5 cell line), but not of other neuronal and non-neuronal cells. Enhanced levels of the autophagy marker, LC3-II, a post-translationally modified form of LC3, in M98K-OPTN-expressing cells and the inability of an LC3-binding-defective M98K variant of OPTN to induce cell death, suggested that autophagy contributes to cell death. Knockdown of Atg5 reduced M98K-induced death of RGC-5 cells, further supporting the involvement of autophagy. Overexpression of M98K-OPTN enhanced autophagosome formation and potentiated the delivery of transferrin receptor to autophagosomes for degradation resulting in reduced cellular transferrin receptor levels. Coexpression of transferrin receptor or supplementation of media with an iron donor reduced M98K-induced cell death. OPTN complexes with RAB12, a GTPase involved in vesicle trafficking, and M98K variant shows enhanced colocalization with RAB12. Knockdown of Rab12 increased transferrin receptor level and reduced M98K-induced cell death. RAB12 is present in autophagosomes and knockdown of Rab12 resulted in reduced formation of autolysosomes during starvation-induced autophagy, implicating a role for RAB12 in autophagy. These results also show that transferrin receptor degradation and autophagy play a crucial role in RGC-5 cell death induced by M98K variant of OPTN.

As a result of a BioID experiment done to identify possible interaction partners of Huntingtin, OPTN was flagged. This purification aims to provide an OPTN sample for future experiments to confirm the possible interaction between these proteins.

optineurin Enables identical protein binding activity; polyubiquitin modification-dependent protein binding activity; and protein-macromolecule adaptor activity. Involved in several processes, including Golgi to plasma membrane protein transport; negative regulation of receptor recycling; and positive regulation of xenophagy. Located in cytosol and trans-Golgi network. Implicated in Paget's disease of bone; amyotrophic lateral sclerosis (multiple); and glaucoma (multiple). Biomarker of Huntington's disease; amyotrophic lateral sclerosis; neuronal intranuclear inclusion disease; and progressive myoclonus epilepsy. This gene encodes the coiled-coil containing protein optineurin. Optineurin may play a role in normal-tension glaucoma and adult-onset primary open angle glaucoma. Optineurin interacts with adenovirus E3-14.7K protein and may utilize tumor necrosis factor-alpha or Fas-ligand pathways to mediate apoptosis, inflammation or vasoconstriction. Optineurin may also function in cellular morphogenesis and membrane trafficking, vesicle trafficking, and transcription activation through its interactions with the RAB8, huntingtin, and transcription factor IIIA proteins. Alternative splicing results in multiple transcript variants encoding the same protein. [provided by RefSeq, Jul 2008]

Liver disease associated with HCC among men and women who received LT in the U.S. between 2010 and 2019.

We previously described a process whereby mitochondria shed by retinal ganglion cell (RGC) axons are transferred to and degraded by surrounding astrocytes in the optic nerve head of mice. Since the mitophagy receptor Optineurin (OPTN) is one of the few large-effect glaucoma genes and axonal damage occurs at the optic nerve head in glaucoma, here we explored whether OPTN mutations perturb the transcellular degradation of mitochondria. Live-imaging of Xenopus laevis optic nerves revealed that diverse human mutant but not wildtype OPTN increase stationary mitochondria and mitophagy machinery and their colocalization within, and in the case of the glaucoma-associated OPTN mutations, also outside of, RGC axons. These extra-axonal mitochondria are degraded by astrocytes. Our studies demonstrate that expression of OPTN carrying a glaucoma-associated mutation results in increased transcellular degradation of axonal mitochondria. , , # Glaucoma-associated optineurin mutations increase transcellular degradation of mitochondria in a vertebrate optic nerve

Dataset DOI: 10.5061/dryad.zkh1893nt

Description of the data and file structure

This dataset contains 5 types of primary data, most of which are live imaging data of tadpole optic nerves. Most data are either time series(t-series) of single focal planes, or single-time sections spanning the thickness of the optic nerve (z-series); both data types were acquired using a spinning disc confocal microscope. There is one image acquired with a stereo-fluorescence microscope. There is one figure containing both a z-series and serial block-face scanning electron microscopy (SBEM)for the same nerve and including an x-ray image of the fixed and embedded tissue block, which was used in the registration of the fluorescence and SBEM data.

T- and z-series fluorescence data were collected using an Andor Dragonfly Spinning Disc Confocal microscope. T...,

Protein-Protein, Genetic, and Chemical Interactions for Wang C (2014):Interaction between optineurin and the bZIP transcription factor NRL. curated by BioGRID (https://thebiogrid.org); ABSTRACT: Although the gene encoding optineurin (OPTN) is a causative gene for glaucoma and amyotrophic lateral sclerosis, it is ubiquitously expressed in all body tissues, including the retina. To study the function of OPTN in retinal ganglion cells as well as the whole retina, we previously isolated OPTN-interacting proteins and identified the gene encoding the bZIP transcription factor neural retina leucine zipper (NRL), which is a causative gene for retinitis pigmentosa. Herein, we investigated the binding between OPTN and NRL proteins in HeLaS3 cells. Co-expression of HA-tagged NRL and FLAG-tagged OPTN in HeLaS3 cells followed by immunoprecipitation and Western blotting with anti-tag antibodies demonstrated the binding of these proteins in HeLaS3 cells, which was confirmed by proximity ligation assay. NRL is the first OPTN-binding protein to show eye-specific expression. A series of partial-deletion OPTN plasmids demonstrated that the tail region (423-577 amino acids [aa]) of OPTN was necessary for binding with NRL. Immunostaining showed that Optn (rat homologue of OPTN) was expressed in rat photoreceptors and localised in the cytoplasm of photoreceptor cells. This is a novel demonstration of Optn expression in photoreceptor cells. OPTN was not detected in photoreceptor nuclei under our experimental conditions. Further analyses are necessary to elucidate the function of OPTN and the significance of its possible binding with NRL in photoreceptor cells.

Peroxisome degradation, known as pexophagy, is essential for eliminating surplus and dysfunctional peroxisomes, with dysregulation linked to various diseases. Previous research revealed that ectopic expression of optineurin (OPTN), a versatile autophagy adaptor involved in multiple autophagic pathways (e.g., mitophagy, aggrephagy, and xenophagy), triggers pexophagy in HEK-293 cells. However, the underlying mechanism remained elusive. Here, we demonstrate that OPTN-mediated pexophagy is a cell type-specific process. In addition, using proximity labeling, we identified PEX14, a peroxisomal membrane protein, as an OPTN-interacting partner. GFP-Trap analyses confirmed this interaction and revealed that PEX14 and OPTN interact through their respective coiled-coil and C-terminal ubiquitin-binding domains, independently of ubiquitin. Furthermore, our results indicate that the C-terminal half of OPTN-GFP induces pexophagy by oligomerization with endogenous OPTN. Overall, these findings propose PEX14 as a docking factor for OPTN at the peroxisomal membrane, facilitating the connection between peroxisomes and the autophagic membrane scaffold during OPTN-mediated pexophagy.

Linear regression slope estimates by year and p-values for proportion of liver transplants caused by each disease etiology in general population, men, and women.

Association of fluorescent Mycobacterium marinum bacteria with Ubiquitin immunolabelling and GFP-Lc3 signal in zebrafish larvae carrying mutations in the selective autophagy receptors optnineurin and p62. Data deposited are Leica LIF files belonging bioRxiv 415463; doi: https://doi.org/10.1101/415463

Protein-Protein, Genetic, and Chemical Interactions for Gleason CE (2011):Polyubiquitin binding to optineurin is required for optimal activation of TANK-binding kinase 1 and production of interferon β. curated by BioGRID (https://thebiogrid.org); ABSTRACT: TANK-binding kinase (TBK1) is essential for transcription of the interferon (IFN) β gene in response to lipopolysaccharide (LPS) and double-stranded RNA, but the molecular mechanisms that underlie the activation of TBK1 are incompletely understood. Previously, we identified the NF-κB essential modulator (NEMO)-related polyubiquitin-binding protein, optineurin (OPTN), as a novel binding partner of TBK1. To determine whether the ubiquitin-binding function of OPTN is involved in regulating TBK1 and IFNβ production, we generated a mouse in which wild-type optineurin was replaced by the polyubiquitin binding-defective mutant, OPTN(D477N/D477N). In this study, we found that LPS or poly(I:C)-induced TBK1 activity was significantly reduced in bone marrow-derived macrophage (BMDM) from OPTN(D477N/D477N) mice. Consistent with this, the phosphorylation of IFN regulatory factor 3 (IRF3) and the production of IFNβ mRNA and secretion were reduced. Stimulation of BMDMs with LPS triggered the phosphorylation of OPTN, which was reversed by phosphatase treatment and prevented by pharmacological inhibition of both the canonical IκB kinases (IKKα/β) and the IKK-related kinases (TBK1/IKKε). In contrast, LPS-stimulated phosphorylation of OPTN(D477N) was markedly reduced in BMDMs from OPTN(D477N/D477N) mice, and inhibition of the canonical IKKs alone prevented phosphorylation, providing further evidence that ubiquitin binding to OPTN contributes to LPS-induced TBK1 activation. TBK1 and IKKβ phosphorylated OPTN preferentially at Ser-177 and Ser-513, respectively, in vitro. In conclusion, our results suggest that OPTN binds to polyubiquitylated species formed in response to LPS and poly(I:C), enhancing the activation of TBK1 that is required for optimal phosphorylation of IRF3 and production of IFNβ.

Protein-Protein, Genetic, and Chemical Interactions for Morton S (2008):Enhanced binding of TBK1 by an optineurin mutant that causes a familial form of primary open angle glaucoma. curated by BioGRID (https://thebiogrid.org); ABSTRACT: TANK-binding kinase 1 (TBK1) was identified as a binding partner for Optineurin (OPTN) in two-hybrid screens, an interaction confirmed by overexpression/immunoprecipitation experiments in HEK293 cells and by coimmunoprecipitation of endogenous OPTN and TBK1 from cell extracts. A TBK1 binding site was located between residues 1-127 of OPTN, residues 78-121 displaying striking homology to the TBK1-binding domain of TANK. The OPTN-binding domain was localised to residues 601-729 of TBK1, while TBK1[1-688] which cannot bind to TANK, did not interact with OPTN. The OPTN[E50K] mutant associated with Primary Open Angle Glaucoma (POAG) displayed strikingly enhanced binding to TBK1, suggesting that this interaction may contribute to familial POAG caused by this mutation.