OdysseusBot: Новая страница: «Regucalcin (RC) (Gluconolactonase) (EC 3.1.1.17) (GNL) (Senescence marker protein 30) (SMP-30) [SMP30] ==Publications== {{medline-entry |title=Effect of senesce...»

2021-04-29T19:04:17Z

Новая страница: «Regucalcin (RC) (Gluconolactonase) (EC 3.1.1.17) (GNL) (Senescence marker protein 30) (SMP-30) [SMP30] ==Publications== {{medline-entry |title=Effect of senesce...»

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Regucalcin (RC) (Gluconolactonase) (EC 3.1.1.17) (GNL) (Senescence marker protein 30) (SMP-30) [SMP30]

==Publications==

{{medline-entry
|title=Effect of senescence marker protein 30 on the proliferation and apoptosis of human lens epithelial cells SRA01/04.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/29675370
|abstract=To study the effect of senescence marker protein 30 (SMP30) on the proliferation and apoptosis of human lens epithelial cell (HLEC) SRA01/04. SMP30 overexpression (OE) and knock down (KD) type cell lines were cultivated by using two groups regucalcin ([[RGN]]; SMP30) lentiviral vectors (LV-[[RGN]], LV-[[RGN]]-RNAi) and the respective negative control virus infect SRA01/04 cells. Western blot and real-time quantitative polymerase chain reaction (q-PCR) analysis were used to determine [[RGN]] overexpression and knock down efficiency. We use cell counting kit-8 (CCK8) assay to measure cell viability and 5-bromodeoxyuridine (BrdU) assay to test cell proliferation. Cell cycle was measured by PI FACS assay and cell apoptosis was tested by Annexin V-[[APC]] assay through flow cytometry. We use Western blot to measure the content of caspase-3 in SRA01/04. We used PCR and Western blot techniques to determine the successful transfection of SMP30 OE and KD SRA01/04 cell lines. By CCK8, Brdu and PI FACS cell cycle assay, it was found that the SMP30 OE group promoted cell proliferation ([i]P[/i]<0.05) compared with the control group, and the KD group inhibited cell proliferation ([i]P[/i]<0.05). The results of Annexin V-[[APC]] signal staining detection indicated that compared with respective control group, the cell apoptosis rate was higher in KD group ([i]P[/i]<0.05) but lower in OE group ([i]P[/i]<0.01). The expression of caspase-3 was down-regulated in OE group through Western blot assay and up-regulated in KD group compared with respective control group. Proliferation of SRA01/04 was promoted by SMP30 OE and apoptosis was suppressed. Increasing the expression of SMP30 may protect HLEC SRA01/04 against apoptosis in cataract.

|keywords=* SRA01/04
* apoptosis
* cell proliferation
* human lens epithelial cell
* senescence marker protein 30
|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5902356
}}
{{medline-entry
|title=Effect of supplementation of recombinant Regucalcin in extender on cryopreservation of spermatozoa of water buffalo (Bubalus bubalis).
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/28782859
|abstract=Elevated intracellular calcium concentration and oxidative damage are two major factors contributing to the poor fertility of cryopreserved spermatozoa. Regucalcin ([[RGN]]), also known as Senescence marker protein-30 (SMP-30), is a calcium-binding protein with multiple roles that include calcium homeostasis, anti-oxidative, anti-apoptosis, and anti-proliferation. In Drosophila, [[RGN]] is reportedly a putative cold-tolerance gene and a cytoprotective role for [[RGN]] against intracellular calcium elevation and oxidative stress was reported in P19 cell lines. Given that [[RGN]] has anticapacitatory effect and abundant in the male reproductive tract, we hypothesized that it may play a cryoprotective role for spermatozoa. We investigated this by including [[RGN]], at three different concentrations (20, 40, and 60 μg/ml), as a supplement for Tris-egg yolk-based semen extender. Post-thaw metrics of progressive motility, acrosome integrity, and zona pellucida binding of spermatozoa were evaluated for three ejaculates of three clinically normal, breeding Murrah buffaloes. A concentration of 40 μg/ml of recombinant [[RGN]] supplemented during sperm freezing resulted in significant increases in the post-thaw progressive motility of spermatozoa (50.6 ± 3.5% vs 40.6 ± 2.6%; p < 0.01), acrosome integrity (53.3 ± 7.4 vs 75.6 ± 6.8; p < 0.05), and zona pellucida binding (31.6 ± 14.0 vs 191.9 ± 12.3 bound spermatozoa; p < 0.01) compared to control conditions without [[RGN]]. Thus, ∼1 μM recombinant [[RGN]], which retains the ability to bind calcium, has a cryoprotective effect for buffalo spermatozoa in extender.
|mesh-terms=* Acrosome Reaction
* Animals
* Buffaloes
* Calcium-Binding Proteins
* Cryopreservation
* Cryoprotective Agents
* Dose-Response Relationship, Drug
* Male
* Recombinant Proteins
* Spermatozoa
|keywords=* Senescence marker protein-30
* calcium homeostasis
* reactive oxygen species
|full-text-url=https://sci-hub.do/10.1002/mrd.22873
}}
{{medline-entry
|title=Aging-associated changes in oxidative stress, cell proliferation, and apoptosis are prevented in the prostate of transgenic rats overexpressing regucalcin.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/26397424
|abstract=Regucalcin ([[RGN]]) is a calcium (Ca(2 ))-binding protein that displays a characteristic downregulated expression with aging in several tissues. Besides its role in regulating intracellular Ca(2 ) homeostasis, [[RGN]] has been associated with the control of oxidative stress, cell proliferation, and apoptosis. Thus, the diminished expression of [[RGN]] with aging may contribute to the age-associated deterioration of cell function. In the present study, we hypothesized that the maintenance of high expression levels of [[RGN]] may prevent age-related alterations in the processes mentioned previously. First, we confirmed that [[RGN]] expression is significantly diminished in the prostate of 8-, 9-, 12-, and 24-months wild-type rats. Then, the effect of aging on lipid peroxidation, antioxidant defenses, cell proliferation, and apoptosis in the prostate of wild-type controls and transgenic rats overexpressing [[RGN]] (Tg-[[RGN]]) was investigated. The activity of glutathione and the antioxidant capacity were increased in Tg-[[RGN]] rats in response to the age-associated increase in thiobarbituric acid reactive substances levels, an effect not seen in wild type. Overexpression of [[RGN]] also counteracted the effect of aging increasing prostate cell proliferation. In contrast to wild-type animals, the prostate weight of Tg-[[RGN]] did not change with aging and was underpinned by the diminished expression of stem cell factor and c-kit, and increased expression of p53. In addition, aged Tg-[[RGN]] animals displayed increased expression (activity) of apoptosis regulators, therefore not showing the age-induced resistance to apoptosis observed in wild type. Altogether, these findings indicate the protective role of [[RGN]] against the development of age-related pathologies, such as, for example, prostate cancer.
|mesh-terms=* Aging
* Animals
* Apoptosis
* Calcium-Binding Proteins
* Carboxylic Ester Hydrolases
* Cell Proliferation
* Intracellular Signaling Peptides and Proteins
* Male
* Organ Size
* Oxidative Stress
* Prostate
* Rats
* Rats, Sprague-Dawley
* Rats, Transgenic

|full-text-url=https://sci-hub.do/10.1016/j.trsl.2015.08.009
}}
{{medline-entry
|title=Effects of regenerative radioelectric asymmetric conveyer treatment on human normal and osteoarthritic chondrocytes exposed to IL-1β. A biochemical and morphological study.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/23682210
|abstract=Osteoarthritis (OA) is a degenerative disease characterized by a progressive loss of articular cartilage extracellular matrix and is due to functional impairments occurring in chondrocytes. In previous works, we highlighted that Regenerative Tissue Optimization (TO-[[RGN]]) treatment with radioelectric asymmetric conveyer (REAC) technology influenced the gene expression profiles controlling stem cell differentiation and the pluripotency of human skin-derived fibroblasts in vitro. Since interleukin-1 beta signaling has been implicated in the induction and progression of this disease (through metalloproteinase-3 synthesis and nitric oxide production), we investigated whether REAC TO-[[RGN]] might influence the biochemical and morphological changes induced by interleukin-1 beta in normal and OA chondrocytes. The induction of metalloproteinase-3 and proteoglycan synthesis was evaluated by a solid-phase enzyme-amplified sensitivity immunoassay, and nitric oxide production was evaluated with the Griess method. Ultrastructural features were observed by transmission electron microscopy. REAC TO-[[RGN]] treatment decreased nitric oxide and metalloproteinase-3 production in normal and OA chondrocytes, while inducing an increase in proteoglycan synthesis. OA chondrocytes were more affected by REAC TO-[[RGN]] treatment than were normal chondrocytes. Ultrastructural changes confirmed that REAC TO-[[RGN]] may counteract the negative effects of interleukin-1 beta incubation. The results of this in vitro study suggest that REAC TO-[[RGN]] treatment may represent a new, promising approach for the management of OA.
|mesh-terms=* Adult
* Aged
* Aging
* Cartilage, Articular
* Chondrocytes
* Electric Stimulation
* Extracellular Matrix
* Female
* Humans
* Immunoassay
* Interleukin-1beta
* Male
* Matrix Metalloproteinase 3
* Nitric Oxide
* Osteoarthritis
* Proteoglycans
* Radio Waves
* Sensitivity and Specificity
* Statistics, Nonparametric
|keywords=* REAC TO-RGN treatment
* human chondrocytes ultrastructure
* metalloproteinase
* nitric oxide
* proteoglycans
|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3653677
}}

RGN - История изменений

OdysseusBot: Новая страница: «Regucalcin (RC) (Gluconolactonase) (EC 3.1.1.17) (GNL) (Senescence marker protein 30) (SMP-30) [SMP30] ==Publications== {{medline-entry |title=Effect of senesce...»