Last update 01 Nov 2024

ROMO1

Last update 01 Nov 2024

Basic Info

Synonyms

bA353C18.2, C20orf52, Epididymis tissue protein Li 175

+ [8]

Introduction

Induces production of reactive oxygen species (ROS) which are necessary for cell proliferation. May play a role in inducing oxidative DNA damage and replicative senescence. May play a role in the coordination of mitochondrial morphology and cell proliferation. Has antibacterial activity against a variety of bacteria including S.aureus, P.aeruginosa and M.tuberculosis. Acts by inducing bacterial membrane breakage.

Drugs associated with ROMO1

SUL-121

Target

ROMO1

Mechanism

ROMO1 inhibitors

Active Org.

University of Manitoba [+3]

Originator Org.

Sulfateq BV

Active Indication

Diabetic Nephropathies [+1]

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

PER-3

Target

ROMO1

Mechanism

ROMO1 inhibitors

Active Org.-

Originator Org.

Peroxitech Therapeutics, Inc.

Active Indication-

Inactive Indication

Acute Lung Injury [+2]

Drug Highest PhaseDiscontinued

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

PER-002

Target

ROMO1

Mechanism

ROMO1 modulators

Active Org.-

Originator Org.

Peroxitech Therapeutics, Inc.

Active Indication-

Inactive Indication

Acute Lung Injury

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with ROMO1

NCT02383992 / WithdrawnNot ApplicableIIT

Comparing the Efficacy of Hydrogen Peroxide Versus Normal Saline in Postoperative Care of Sutured Wounds

The primary objective of this study is to compare the efficacy of hydrogen peroxide versus normal saline in postoperative care of sutured wounds. Subjects will be randomly assigned to standard of care hydrogen peroxide or standard of care normal saline in postoperative care of sutured wounds followed by applying petroleum jelly and sterile gauze bandage. Data will be collected at day 0 and between days 7 to14. Subjects will provide irritation scale rating (0-4) with 0 being none/absent and 4 being severe/extreme.

Start Date01 Oct 2015

Sponsor / Collaborator

Northwestern University

100 Clinical Results associated with ROMO1

100 Translational Medicine associated with ROMO1

0 Patents (Medical) associated with ROMO1

135

Literatures (Medical) associated with ROMO1

01 Oct 2024·FEBS Open Bio

Structure prediction analysis of human core TIM23 complex reveals conservation of the protein translocation mechanism

Article

Author: Draczkowski, Piotr ; Maruszczak, Klaudia K. ; Wnorowski, Artur ; Chacinska, Agnieszka

The majority of mitochondrial proteins are encoded in the nucleus, translated on cytosolic ribosomes, and subsequently targeted to the mitochondrial surface. Their further import into the organelle is facilitated by highly specialized protein translocases. Mitochondrial precursor proteins that are destined to the mitochondrial matrix and, to some extent, the inner membrane, utilize translocase of the inner membrane (TIM23). This indispensable import machinery has been extensively studied in yeast. The translocating unit of the TIM23 complex in yeast consists of two membrane proteins, Tim17 and Tim23. In contrast to previous findings, recent reports demonstrate the primary role of Tim17, rather than Tim23, in the translocation of newly synthesized proteins. Very little is known about human TIM23 translocase. Human cells have two orthologs of yeast Tim17, TIMM17A and TIMM17B. Here, using computational tools, we present the architecture of human core TIM23 variants with either TIMM17A or TIMM17B, forming two populations of highly similar complexes. The structures reveal high conservation of the core TIM23 complex between human and yeast. Interestingly, both TIMM17A and TIMM17B variants interact with TIMM23 and reactive oxygen species modulator 1 (ROMO1); a homolog of yeast Mgr2, a protein that can create a channel‐like structure with Tim17. The high structural conservation of proteins that form the core TIM23 complex in yeast and humans raises an interesting question about mechanistic and functional differences that justify existence of the two variants of TIM23 in higher eukaryotes.

01 Sep 2024·Cryobiology

Effect of naringenin on post-thaw quality, fertility-associated gene expression and fertilization potential of buffalo (Bubalus bubalis) bull sperm

Article

Author: Khan, Ghulam Shabbir ; Zahoor, Muhammad Yasir ; Riaz, Amjad ; Hifz-Ul-Rahman ; Tahir, Muhammad Zahid

Our objectives were to explore the effect of naringenin addition in the semen extender on the post-thaw 1) sperm quality, 2) fertility-associated gene expression, and 3) fertilization potential of buffalo bull sperm. In experiment 1, semen samples (n = 32) from four Nili-Ravi buffalo bulls were pooled (n = 8) and diluted with the tris-citric acid (TCF-EY) extender containing different concentrations of naringenin, i.e., placebo (DMSO), 0 (control), 50, 100, 150 and 200 μM naringenin. After dilution, semen samples were packed in 0.5 mL French straws, cryopreserved and analyzed for post-thawed sperm quality and gene expression. Computer-assisted Semen Analysis, Hypo-osmotic Swelling test, Normal Apical Ridge assay, Rhodamine 123, Acridine orange, Propidium iodide staining and Thiobarbituric Acid Reactive Substances assay were performed to assess sperm motility parameters, plasma membrane functionality, acrosome integrity, mitochondrial membrane potential, DNA integrity, viability and lipid peroxidation, respectively. Expression levels of sperm acrosome-associated SPACA3, DNA condensation-related PRM1, anti-apoptotic BCL2, pro-apoptotic BAX, and oxidative stress-associated ROMO1 genes were evaluated through qPCR. Results revealed that total and progressive motility, plasma membrane functionality, acrosome integrity, mitochondrial membrane potential, DNA integrity and viability were higher (P < 0.05) with 50, 100 and 150 μM naringenin compared to 200 μM naringenin, placebo and control groups. Moreover, all naringenin-treated groups improved catalase activity, and reduced lipid peroxidation compared to placebo and control groups (P < 0.05). Relative expression levels of SPACA3 and PRM1 genes were higher (P < 0.05) with 150μM naringenin compared to all groups except 100 μM (P > 0.05). No difference (P > 0.05) in the expression level of BCL2 gene was observed among all groups. Furthermore, BAX gene was expressed higher (P < 0.05) in the 200 μM naringenin group, whereas no difference (P > 0.05) in expression was noticed among the remaining groups. In addition, ROMO1 gene was expressed lower (P < 0.05) in all naringenin-treated groups compared to the control. In experiment 2, the in vivo fertility of semen doses (n = 400; 200/group) containing optimum concentration of naringenin (150 μM; depicted better in vitro sperm quality in experiment 1) was compared with control during the breeding season. Buffaloes were inseminated 24 h after the onset of natural estrus and palpated transrectal for pregnancy at least 60 days post-insemination. The fertility rate of 150 μM naringenin group was higher (P = 0.0366) compared to the control [57.00 ± 0.03% (114/200) vs. 46.50 ± 0.04% (93/200), respectively]. Taken together, it is concluded that naringenin supplementation in semen extender improves post-thaw quality, fertility-associated gene expression and fertilization potential of buffalo bull sperm, more apparently at 150 μM concentration.

01 Aug 2024·Biopreservation and Biobanking

Effect of Trehalose Supplementation in Egg-Yolk-Free Extender on Conventional Parameters and Gene Expression Related to Reactive Oxygen Species, Apoptosis, and Motility of Frozen Dog Spermatozoa

Article

Author: Jeon, Yubyeol ; Yu, Il-Jeoung ; Ibrahim, Saddah ; Talha, Nabeel Abdelbagi Hamad ; Shin, Sangmin

The present study was conducted to evaluate the effects of trehalose supplementation in egg-yolk (EY)-free tris extender on dog spermatozoa. Pooled spermatozoa were diluted with extender 1 (EY-free tris extender supplemented with 0, 10, 15, 20, or 30 mM trehalose) and cooled (2 × 10⁸ sperm/mL) for 1 hour at 4°C. After that, extender 2 (extender 1 containing 1 M glycerol) was added (v:v) to the diluted sperm, loaded in 0.5-mL straws (1 × 10⁸ sperm/mL), and incubated at 4°C for 30 minutes. The sperm straws were frozen over liquid nitrogen (LN₂) vapor for 20 minutes and then plunged directly into LN₂. After thawing at 37°C for 25 seconds, sperm progressive motility (CASA), viability (SYBR-14/PI), apoptosis (Annexin V/PI), and reactive oxygen species (ROS; H₂DCFDA/PI) were evaluated. Thereafter, the optimal concentrations of trehalose were selected, and the gene expression of BAX, BCL2, NOX5, SMOX, OGG1, and ROMO1 was evaluated after freeze-thawing. Supplementation with 20 and 30 mM trehalose significantly increased sperm progressive motility and viability compared to the control. However, trehalose had no significant effect on sperm ROS or phosphatidylserine translocation index. There were minor numerical increases and decreases in gene expression when the selected optimal concentrations of trehalose (20 and 30 mM) were compared to the control. However, there were no significant differences. We conclude that the addition of trehalose (20 and 30 mM) in EY-free extender could improve sperm motility and viability without significant effects on ROS, apoptosis, or gene expression.

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