The role of makorin ring finger protein-3, kisspeptin, and neurokinin B in the physiology of minipuberty

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Enver Atay ◽  
Suna Kılınç ◽  
Gozde Ulfer ◽  
Turkan Yigitbasi ◽  
Cagri Cakici ◽  
...  
Keyword(s):  
Ring Finger ◽  
Total Testosterone ◽  
Strong Positive Correlation ◽  
Ring Finger Protein ◽  
Neurokinin B ◽  
Positive Correlation ◽  
Finger Protein ◽  
A Prospective Study

Abstract Background There is no data regarding the interrelationships of circulating Makorin Ring Finger Protein-3 (MKRN3), Kisspeptin (KISS1), and Neurokinin B (NKB) concentrations during minipuberty in humans. Objective To determine temporal changes in circulating concentrations of MKRN3, KISS1, NKB, and gonadotropins and investigate interrelationships between them in healthy full-term (FT) and preterm (PT) infants during minipuberty period. Methods A prospective study of 6-month follow-up performed. Eighty-seven healthy newborns, 48 FT (19 boys/29 girls), and 39 PT (21 boys/18 girls) (gestational age 31–37 weeks), were included. Blood samples were taken at 7 days (D7), 2 months (M2), and 6 months (M6) of age. Serum MKRN3, KISS1, NKB, LH, FSH, total testosterone (TT), and estradiol (E2) concentrations were measured. Results Seventy infants completed the study. MKRN3, KISS1, and NKB concentrations were similar in FT girls and boys. PT boys and girls also had similar concentrations of MKRN3, KISS1, and NKB. FT babies had significantly higher NKB concentrations than PT babies at D7, M2, and M6. MKRN3 and KISS1 concentrations do not differ between FT and PT babies. A strong positive correlation was found between MKRN3 and KISS1 at each time point and in all groups. FSH, LH, TT/E2 concentrations decrease while those of MKRN3 and KISS1 have a trend to increase toward the end of minipuberty. No correlation was detected between gonadotropins and MKRN3, KISS1, NKB concentrations. Conclusion Strong positive correlation demonstrated between KISS1 and MKRN3 suggests that interrelationship between molecules controlling minipuberty is not similar to those at puberty.

scholarly journals Arkadia (RING Finger Protein 111) Mediates Sumoylation-Dependent Stabilization of Nrf2 Through K48-Linked Ubiquitination

2018 ◽  
Vol 46 (1) ◽  
pp. 418-430 ◽  
Author(s):  
Deneshia J. McIntosh ◽  
Treniqka S. Walters ◽  
Ifeanyi J. Arinze ◽  
Jamaine Davis
Keyword(s):  
Gene Transcription ◽  
Ring Finger ◽  
Nuclear Body ◽  
Promyelocytic Leukemia ◽  
Heme Oxygenase 1 ◽  
Ring Finger Protein ◽  
Whole Cell ◽  
Cell Lysates ◽  
Finger Protein

Background/Aims: The transcription factor Nrf2 is a master regulator of the antioxidant defense system, protecting cells from oxidative damage. We previously reported that the SUMO-targeted E3 ubiquitin ligase (STUbL), RING finger protein 4 (RNF4) accelerated the degradation rate of Nrf2 in promyelocytic leukemia-nuclear body (PML-NB)-enriched fractions and decreased Nrf2-mediated gene transcription. The mechanisms that regulate Nrf2 nuclear levels are poorly understood. In this study, we aim to explore the role of the second mammalian STUbL, Arkadia/RNF111 on Nrf2. Methods: Arkadia mediated ubiquitination was detected using co-immunoprecipitation assays in which whole cell lysates were immunoprecipated with anti-Nrf2 antibody and Western blotted with anti-hemagglutinin (HA) antibody or anti-Lys-48 ubiquitin-specific antibody. The half-life of Nrf2 was detected in whole cell lysates and promyelocytic leukemia-nuclear body enriched fractions by cycloheximide-chase. Reporter gene assays were performed using the antioxidant response element (ARE)-containing promoter Heme oxygenase-1 (HO-1). Results: We show that Arkadia/RNF111 is able to ubiquitinate Nrf2 resulting in the stabilization of Nrf2. This stabilization was mediated through Lys-48 ubiquitin chains, contrary to traditionally degradative role of Lys-48 ubiquitination, suggesting that Lys-48 ubiquitination of Nrf2 protects Nrf2 from degradation thereby allowing Nrf2-dependent gene transcription. Conclusion: Collectively, these findings highlight a novel mechanism to positively regulate nuclear Nrf2 levels in response to oxidative stress through Arkadia-mediated K48-linked ubiquitination of Nrf2.

scholarly journals Structural basis for role of ring finger protein RNF168 RING domain

Cell Cycle ◽  
2013 ◽  
Vol 12 (2) ◽  
pp. 312-321 ◽  
Author(s):  
Xiaoqin Zhang ◽  
Jie Chen ◽  
Minhao Wu ◽  
Huakai Wu ◽  
Aloysius Wilfred Arokiaraj ◽  
...  
Keyword(s):  
Ring Finger ◽  
Ring Domain ◽  
Structural Basis ◽  
Ring Finger Protein ◽  
Finger Protein

scholarly journals Role of Ring Finger Protein 213 in Moyamoya Disease

2016 ◽  
Vol 129 (20) ◽  
pp. 2497-2501 ◽  
Author(s):  
Yong-Gang Ma ◽  
Qian Zhang ◽  
Le-Bao Yu ◽  
Ji-Zong Zhao
Keyword(s):  
Moyamoya Disease ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Finger Protein

scholarly journals RNF6 as an Oncogene and Potential Therapeutic Target—A Review

BioTech ◽  
2020 ◽  
Vol 9 (4) ◽  
pp. 22
Author(s):  
Paweł Zapolnik ◽  
Antoni Pyrkosz
Keyword(s):  
Ubiquitin Ligase ◽  
Therapeutic Target ◽  
Human Cancer ◽  
Ring Finger ◽  
Model Organisms ◽  
Ring Finger Protein ◽  
Potential Therapeutic Target ◽  
Finger Protein ◽  
Potential Prognostic Factor

The RNF6 gene encodes Ring Finger Protein 6 (RNF6), which functions as a ubiquitin ligase. Its functions are not entirely known, but research shows that it is involved in human cancer development. Initially, this gene was considered to be a tumor suppressor. Numerous statistical analyses on cell lines and animals indicate, however, that RNF6 functions as an oncogene, involved in signaling pathways, including SHP1/STAT3, AKT/mTOR, Wnt/β-catenin, or ERα/Bcl-xL. Due to this fact, it has become a potential prognostic factor and therapeutic target. Studies in tumor cells and model organisms using inhibitors such as total saponins from Paris forrestii (TSPf), ellagic acid, or microRNA molecules show the effectiveness of inhibiting RNF6, and through it, the pathways of tumor cell proliferation. The results of the currently available studies are promising, but the function of RNF6 is not fully understood. More research is needed to assess the role of RNF6 and to check the safety and efficacy of inhibitors.

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