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Journal articles on the topic 'Lunapark'

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Author: Grafiati
Published: 11 March 2023

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1

de Almeida-Faria, Juliana, Daniella E. Duque-Guimarães, Thomas P. Ong, Lucas C. Pantaleão, Asha A. Carpenter, Elena Loche, Laura C. Kusinski, et al. "Maternal obesity during pregnancy leads to adipose tissue ER stress in mice via miR-126-mediated reduction in Lunapark." Diabetologia 64, no. 4 (January 27, 2021): 890–902. http://dx.doi.org/10.1007/s00125-020-05357-4.

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Abstract Aims/hypothesis Levels of the microRNA (miRNA) miR-126-3p are programmed cell-autonomously in visceral adipose tissue of adult offspring born to obese female C57BL/6J mice. The spectrum of miR-126-3p targets and thus the consequences of its dysregulation for adipocyte metabolism are unknown. Therefore, the aim of the current study was to identify novel targets of miR-126-3p in vitro and then establish the outcomes of their dysregulation on adipocyte metabolism in vivo using a well-established maternal obesity mouse model. Methods miR-126-3p overexpression in 3T3-L1 pre-adipocytes followed by pulsed stable isotope labelling by amino acids in culture (pSILAC) was performed to identify novel targets of the miRNA. Well-established bioinformatics algorithms and luciferase assays were then employed to confirm those that were direct targets of miR-126-3p. Selected knockdown experiments were performed in vitro to define the consequences of target dysregulation. Quantitative real-time PCR, immunoblotting, histology, euglycaemic–hyperinsulinaemic clamps and glucose tolerance tests were performed to determine the phenotypic and functional outcomes of maternal programmed miR-126-3p levels in offspring adipose tissue. Results The proteomic approach confirmed the identity of known targets of miR-126-3p (including IRS-1) and identified Lunapark, an endoplasmic reticulum (ER) protein, as a novel one. We confirmed by luciferase assay that Lunapark was a direct target of miR-126-3p. Overexpression of miR-126-3p in vitro led to a reduction in Lunapark protein levels and increased Perk (also known as Eif2ak3) mRNA levels and small interference-RNA mediated knockdown of Lunapark led to increased Xbp1, spliced Xbp1, Chop (also known as Ddit3) and Perk mRNA levels and an ER stress transcriptional response in 3T3-L1 pre-adipocytes. Consistent with the results found in vitro, increased miR-126-3p expression in adipose tissue from adult mouse offspring born to obese dams was accompanied by decreased Lunapark and IRS-1 protein levels and increased markers of ER stress. At the whole-body level the animals displayed glucose intolerance. Conclusions/interpretation Concurrently targeting IRS-1 and Lunapark, a nutritionally programmed increase in miR-126-3p causes adipose tissue insulin resistance and an ER stress response, both of which may contribute to impaired glucose tolerance. These findings provide a novel mechanism by which obesity during pregnancy leads to increased risk of type 2 diabetes in the offspring and therefore identify miR-126-3p as a potential therapeutic target. Graphical abstract
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2

Ram, Paul. "Het ‘lunapark’ van Marck Eyck." Huisarts en Wetenschap 51, no. 1 (January 2008): 57–58. http://dx.doi.org/10.1007/bf03086642.

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3

Tran, Pham-Tue-Hung, Naveed Asghar, Magnus Johansson, and Wessam Melik. "Roles of the Endogenous Lunapark Protein during Flavivirus Replication." Viruses 13, no. 7 (June 22, 2021): 1198. http://dx.doi.org/10.3390/v13071198.

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The endoplasmic reticulum (ER) of eukaryotic cells is a dynamic organelle, which undergoes continuous remodeling. At the three-way tubular junctions of the ER, the lunapark (LNP) protein acts as a membrane remodeling factor to stabilize these highly curved membrane junctions. In addition, during flavivirus infection, the ER membrane is invaginated to form vesicles (Ve) for virus replication. Thus, LNP may have roles in the generation or maintenance of the Ve during flavivirus infection. In this study, our aim was to characterize the functions of LNP during flavivirus infection and investigate the underlying mechanisms of these functions. To specifically study virus replication, we generated cell lines expressing replicons of West Nile virus (Kunjin strain) or Langat virus. By using these replicon platforms and electron microscopy, we showed that depletion of LNP resulted in reduced virus replication, which is due to its role in the generation of the Ve. By using biochemical assays and high-resolution microscopy, we found that LNP is recruited to the Ve and the protein interacts with the nonstructural protein (NS) 4B. Therefore, these data shed new light on the interactions between flavivirus and host factors during viral replication.
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4

Kriechbaumer, Verena, Emily Breeze, Charlotte Pain, Frances Tolmie, Lorenzo Frigerio, and Chris Hawes. "Arabidopsis Lunapark proteins are involved in ER cisternae formation." New Phytologist 219, no. 3 (May 25, 2018): 990–1004. http://dx.doi.org/10.1111/nph.15228.

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5

Van Velthoven, Harry. "Signalement van: Het lunapark en andere plekken / Ludo Abicht (2008)." WT. Tijdschrift over de geschiedenis van de Vlaamse beweging 68, no. 1 (January 1, 2009): 105. http://dx.doi.org/10.21825/wt.v68i1.12417.

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6

Chen, Shuliang, Tanvi Desai, James A. McNew, Patrick Gerard, Peter J. Novick, and Susan Ferro-Novick. "Lunapark stabilizes nascent three-way junctions in the endoplasmic reticulum." Proceedings of the National Academy of Sciences 112, no. 2 (December 29, 2014): 418–23. http://dx.doi.org/10.1073/pnas.1423026112.

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The endoplasmic reticulum (ER) consists of a polygonal network of sheets and tubules interconnected by three-way junctions. This network undergoes continual remodeling through competing processes: the branching and fusion of tubules forms new three-way junctions and new polygons, and junction sliding and ring closure leads to polygon loss. However, little is known about the machinery required to generate and maintain junctions. We previously reported that yeast Lnp1 localizes to ER junctions, and that loss of Lnp1 leads to a collapsed, densely reticulated ER network. In mammalian cells, only approximately half the junctions contain Lnp1. Here we use live cell imaging to show that mammalian Lnp1 (mLnp1) affects ER junction mobility and hence network dynamics. Three-way junctions with mLnp1 are less mobile than junctions without mLnp1. Newly formed junctions that acquire mLnp1 remain stable within the ER network, whereas nascent junctions that fail to acquire mLnp1 undergo rapid ring closure. These findings imply that mLnp1 plays a key role in stabilizing nascent three-way ER junctions.
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7

Dobryden, Paul. "The institution of pleasure: From display to environment at the Berlin Lunapark." Studies in European Cinema 10, no. 2 (September 1, 2013): 157–78. http://dx.doi.org/10.1386/seci.10.2-3.157_1.

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8

Zhou, Xin, Yu He, Xiaofang Huang, Yuting Guo, Dong Li, and Junjie Hu. "Reciprocal regulation between lunapark and atlastin facilitates ER three-way junction formation." Protein & Cell 10, no. 7 (November 29, 2018): 510–25. http://dx.doi.org/10.1007/s13238-018-0595-7.

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9

Wang, Songyu, Robert E. Powers, Vicki AM Gold, and Tom A. Rapoport. "The ER morphology-regulating lunapark protein induces the formation of stacked bilayer discs." Life Science Alliance 1, no. 1 (January 2018): e201700014. http://dx.doi.org/10.26508/lsa.201700014.

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Lunapark (Lnp) is a conserved membrane protein that localizes to and stabilizes three-way junctions of the tubular ER network. In higher eukaryotes, phosphorylation of Lnp may contribute to the conversion of the ER from tubules to sheets during mitosis. Here, we report on the reconstitution of purified Lnp with phospholipids. Surprisingly, Lnp induces the formation of stacked membrane discs. Each disc is a bicelle, with Lnp sitting in the bilayer facing both directions. The interaction between bicelles is mediated by the cytosolic domains of Lnp, resulting in a constant distance between the discs. A phosphomimetic Lnp mutant shows reduced bicelle stacking. Based on these results, we propose that Lnp tethers ER membranes in vivo in a cell cycle–dependent manner. Lnp appears to be the first membrane protein that induces the formation of stacked bicelles.
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10

Yuniati, Laurensia, Angela Lauriola, Manouk Gerritsen, Susana Abreu, Eric Ni, Chiara Tesoriero, Jacob O. Onireti, et al. "Ubiquitylation of the ER-Shaping Protein Lunapark via the CRL3KLHL12 Ubiquitin Ligase Complex." Cell Reports 31, no. 7 (May 2020): 107664. http://dx.doi.org/10.1016/j.celrep.2020.107664.

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11

Breuss, Martin W., An Nguyen, Qiong Song, Thai Nguyen, Valentina Stanley, Kiely N. James, Damir Musaev, et al. "Mutations in LNPK, Encoding the Endoplasmic Reticulum Junction Stabilizer Lunapark, Cause a Recessive Neurodevelopmental Syndrome." American Journal of Human Genetics 103, no. 2 (August 2018): 296–304. http://dx.doi.org/10.1016/j.ajhg.2018.06.011.

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12

FARIA, JULIANA DE A., DANIELLA DUQUE GUIMARAES, LUCAS PANTALEAO, THOMAS P. ONG, and AUSAN OZANNE. "Lunapark, a Novel Target to miR-126—Its Potential Role in Maintenance of ER and Glucose Homeostasis." Diabetes 67, Supplement 1 (May 2018): 238—LB. http://dx.doi.org/10.2337/db18-238-lb.

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13

Zhao, Yupeng, Ting Zhang, Huanhuan Huo, Yihong Ye, and Yanfen Liu. "Lunapark Is a Component of a Ubiquitin Ligase Complex Localized to the Endoplasmic Reticulum Three-way Junctions." Journal of Biological Chemistry 291, no. 35 (July 7, 2016): 18252–62. http://dx.doi.org/10.1074/jbc.m116.737783.

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14

Chen, Shuliang, Peter Novick, and Susan Ferro-Novick. "ER network formation requires a balance of the dynamin-like GTPase Sey1p and the Lunapark family member Lnp1p." Nature Cell Biology 14, no. 7 (June 24, 2012): 707–16. http://dx.doi.org/10.1038/ncb2523.

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15

Wisesa, Sindhu, Yasunori Yamamoto, and Toshiaki Sakisaka. "TMCC3 localizes at the three-way junctions for the proper tubular network of the endoplasmic reticulum." Biochemical Journal 476, no. 21 (November 11, 2019): 3241–60. http://dx.doi.org/10.1042/bcj20190359.

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The tubular network of the endoplasmic reticulum (ER) is formed by connecting ER tubules through three-way junctions. Two classes of the conserved ER membrane proteins, atlastins and lunapark, have been shown to reside at the three-way junctions so far and be involved in the generation and stabilization of the three-way junctions. In this study, we report TMCC3 (transmembrane and coiled-coil domain family 3), a member of the TEX28 family, as another ER membrane protein that resides at the three-way junctions in mammalian cells. When the TEX28 family members were transfected into U2OS cells, TMCC3 specifically localized at the three-way junctions in the peripheral ER. TMCC3 bound to atlastins through the C-terminal transmembrane domains. A TMCC3 mutant lacking the N-terminal coiled-coil domain abolished localization to the three-way junctions, suggesting that TMCC3 localized independently of binding to atlastins. TMCC3 knockdown caused a decrease in the number of three-way junctions and expansion of ER sheets, leading to a reduction of the tubular ER network in U2OS cells. The TMCC3 knockdown phenotype was partially rescued by the overexpression of atlastin-2, suggesting that TMCC3 knockdown would decrease the activity of atlastins. These results indicate that TMCC3 localizes at the three-way junctions for the proper tubular ER network.
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16

Sun, Jiaqi, Nooshin Movahed, and Huanquan Zheng. "LUNAPARK Is an E3 Ligase That Mediates Degradation of ROOT HAIR DEFECTIVE3 to Maintain a Tubular ER Network in Arabidopsis." Plant Cell 32, no. 9 (July 2, 2020): 2964–78. http://dx.doi.org/10.1105/tpc.18.00937.

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17

Bagchi, Parikshit, Xiaofang Liu, Woo Jung Cho, and Billy Tsai. "Lunapark-dependent formation of a virus-induced ER exit site contains multi-tubular ER junctions that promote viral ER-to-cytosol escape." Cell Reports 37, no. 10 (December 2021): 110077. http://dx.doi.org/10.1016/j.celrep.2021.110077.

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18

Moriya, Koko, Kei Nagatoshi, Yoshimi Noriyasu, Tsuyoshi Okamura, Emi Takamitsu, Takashi Suzuki, and Toshihiko Utsumi. "Protein N-Myristoylation Plays a Critical Role in the Endoplasmic Reticulum Morphological Change Induced by Overexpression of Protein Lunapark, an Integral Membrane Protein of the Endoplasmic Reticulum." PLoS ONE 8, no. 11 (November 4, 2013): e78235. http://dx.doi.org/10.1371/journal.pone.0078235.

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19

Rea, Anne C. "A Once-Hidden Endoplasmic Reticulum Matrix Reveals the Totally Tubular Function of LUNAPARKs in Plants." Plant Cell 32, no. 9 (July 8, 2020): 2679–80. http://dx.doi.org/10.1105/tpc.20.00509.

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20

Ueda, Haruko, Natsumi Ohta, Yoshitaka Kimori, Teruka Uchida, Tomoo Shimada, Kentaro Tamura, and Ikuko Hara-Nishimura. "Endoplasmic Reticulum (ER) Membrane Proteins (LUNAPARKs) are Required for Proper Configuration of the Cortical ER Network in Plant Cells." Plant and Cell Physiology 59, no. 10 (July 14, 2018): 1931–41. http://dx.doi.org/10.1093/pcp/pcy137.

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21

Ueda, Haruko, Natsumi Ohta, Yoshitaka Kimori, Teruka Uchida, Tomoo Shimada, Kentaro Tamura, and Ikuko Hara-Nishimura. "Endoplasmic Reticulum (ER) Membrane Proteins (LUNAPARKs) are Required for Proper Configuration of the Cortical ER Network in Plant Cells." Plant and Cell Physiology 59, no. 10 (October 1, 2018): 2166. http://dx.doi.org/10.1093/pcp/pcy192.

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22

Parashar, Smriti, Ravi Chidambaram, Shuliang Chen, Christina R. Liem, Eric Griffis, Gerard G. Lambert, Nathan C. Shaner, Matthew Wortham, Jesse C. Hay, and Susan Ferro-Novick. "Endoplasmic reticulum tubules limit the size of misfolded protein condensates." eLife 10 (September 1, 2021). http://dx.doi.org/10.7554/elife.71642.

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The endoplasmic reticulum (ER) is composed of sheets and tubules. Here we report that the COPII coat subunit, SEC24C, works with the long form of the tubular ER-phagy receptor, RTN3, to target dominant-interfering mutant proinsulin Akita puncta to lysosomes. When the delivery of Akita puncta to lysosomes was disrupted, large puncta accumulated in the ER. Unexpectedly, photobleach analysis indicated that Akita puncta behaved as condensates and not aggregates, as previously suggested. Akita puncta enlarged when either RTN3 or SEC24C were depleted, or when ER sheets were proliferated by either knocking out Lunapark or overexpressing CLIMP63. Other ER-phagy substrates that are segregated into tubules behaved like Akita, while a substrate (type I procollagen) that is degraded by the ER-phagy sheets receptor, FAM134B, did not. Conversely, when ER tubules were augmented in Lunapark knock-out cells by overexpressing reticulons, ER-phagy increased and the number of large Akita puncta were reduced. Our findings imply that segregating cargos into tubules has two beneficial roles. First, it localizes mutant misfolded proteins, the receptor and SEC24C to the same ER domain. Second, physically restraining condensates within tubules, before they undergo ER-phagy, prevents them from enlarging and impacting cell health.
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23

Kajiho, Hiroaki, Yasunori Yamamoto, and Toshiaki Sakisaka. "CAND1 regulates lunapark for the proper tubular network of the endoplasmic reticulum." Scientific Reports 9, no. 1 (September 11, 2019). http://dx.doi.org/10.1038/s41598-019-49542-x.

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Abstract Endoplasmic reticulum (ER) tubules connect each other by three-way junctions, resulting in a tubular ER network. Oligomerization of three-way junction protein lunapark (Lnp) is important for its localization and the three-way junction stability. On the other hand, Lnp has an N-terminal ubiquitin ligase activity domain, which is also important for the three-way junction localization. To understand the mode of action of Lnp, we isolated Cullin-associated and neddylation-dissociated 1 (CAND1), a regulator of Skp1-Cul1-F-box (SCF) ubiquitin ligase, as a Lnp-binding protein by affinity chromatography. CAND1 and Lnp form a higher-molecular-weight complex in vitro, while they do not co-localize at the three-way junctions. CAND1 reduces the auto-ubiquitination activity of Lnp. CAND1 knockdown enhances proteasomal degradation of Lnp and reduces the tubular ER network in mammalian cells. These results suggest that CAND1 has the potency to promote the formation of the higher-molecular-weight complex with Lnp and reduce the auto-ubiquitination activity of Lnp, thereby regulating the three-way junction stability of the tubular ER network.
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24

Anggrandariyanny, Putri Chynthia, Hiroaki Kajiho, Yasunori Yamamoto, and Toshiaki Sakisaka. "Lunapark ubiquitinates atlastin-2 for the tubular network formation of the endoplasmic reticulum." Journal of Biochemistry, July 26, 2022. http://dx.doi.org/10.1093/jb/mvac060.

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Abstract Endoplasmic reticulum (ER) tubules are interconnected by three-way junctions, resulting in the formation of a tubular ER network. Lunapark (Lnp) localizes to and stabilizes the three-way junctions. The N-terminal cytoplasmic domain in Lnp has a ubiquitin ligase activity. However, the molecular mechanism of how the ubiquitin ligase activity of Lnp is involved in the formation of the tubular ER network remains unknown. In this study, we examined whether the ER membrane proteins responsible for the formation of the tubular ER network are ubiquitinated by Lnp. We found that atlastin-2 (ATL2), an isoform of the ATL family mediating the generation of the three-way junctions by connecting the ER tubules, is a novel substrate for ubiquitination by Lnp. The localization of Lnp at the three-way junctions is important for ubiquitination of ATL2. Lysine 56, 57, 282, and 302 are the potential ubiquitination sites by Lnp. Silencing ATL2 decreased the number of the three-way junctions, and the expression of the ATL2 mutant in which the lysine residues are substituted with arginine failed to rescue the decrease of the three-way junctions in the ATL2 knocked-down cells. These results suggest that Lnp ubiquitinates ATL2 at the three-way junctions for the proper tubular ER network formation.
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25

Wang, Songyu, Hanna Tukachinsky, Fabian B. Romano, and Tom A. Rapoport. "Cooperation of the ER-shaping proteins atlastin, lunapark, and reticulons to generate a tubular membrane network." eLife 5 (September 13, 2016). http://dx.doi.org/10.7554/elife.18605.

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In higher eukaryotes, the endoplasmic reticulum (ER) contains a network of membrane tubules, which transitions into sheets during mitosis. Network formation involves curvature-stabilizing proteins, including the reticulons (Rtns), as well as the membrane-fusing GTPase atlastin (ATL) and the lunapark protein (Lnp). Here, we have analyzed how these proteins cooperate. ATL is needed to not only form, but also maintain, the ER network. Maintenance requires a balance between ATL and Rtn, as too little ATL activity or too high Rtn4a concentrations cause ER fragmentation. Lnp only affects the abundance of three-way junctions and tubules. We suggest a model in which ATL-mediated fusion counteracts the instability of free tubule ends. ATL tethers and fuses tubules stabilized by the Rtns, and transiently sits in newly formed three-way junctions. Lnp subsequently moves into the junctional sheets and forms oligomers. Lnp is inactivated by mitotic phosphorylation, which contributes to the tubule-to-sheet conversion of the ER.
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26

TAPAN, İrfan. "Orduzu-Pınarbaşı (Malatya-Battalgazi) Mesire Alanının Rekreasyon Faaliyetleri Kapsamında Değerlendirmesi." Batman Üniversitesi Yaşam Bilimleri Dergisi, June 13, 2022. http://dx.doi.org/10.55024/buyasambid.1086846.

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Bu çalışmada Malatya ilinin Battalgazi ilçesine bağlı Orduzu Mahallesi’nin Pınarbaşı mevkiinde bulunan Orduzu-Pınarbaşı Mesire Alanı’nın özellikleri, rekreasyon faaliyetleri, bölgenin potansiyeli, sorunları ve çözüm önerileri belirlenmeye çalışılmıştır. Bu çalışma için kullanılan materyaller çeşitli makale çalışmaları, internet ortamındaki kaynaklar, Malatya Büyükşehir Belediyesi ve Malatya Valiliği’nin çeşitli kaynaklarıdır. Bu araştırma için bölgede gözlem yöntemi kullanılarak bölge hakkında detaylı bir araştırma ve gözlemler yapılarak ulaşılan bulgular not edilip çalışmaya dâhil edilmiştir. Toplanılan veriler ve yapılan gözlemler neticesinde elde edilen bulgular derlenerek yorumlanmıştır. Yapılan araştırma ve gözlemler neticesinde Orduzu-Pınarbaşı bölgesinin Malatya ilinde en yoğun şekilde ziyaret edildiği mesire alanı olduğu tespit edilmiştir. Bu mesire alanının sınırları içerisinde fuar alanı, lunapark, hayvanat bahçesi, tabiat parkı, kent ormanı, olimpik yüzme havuzu, kır düğün salonları, Malatya Spor Kulübü antrenman tesisleri, piknik yerleri, kafe ve restoranlar bulunmaktadır. Ayrıca mesire alanın içinde Orduzu-Pınarbaşı Gölet’i de yer almakta olup, bu gölette turistik sandal gezileri gerçekleştirilmektedir. Sonuç olarak Orduzu-Pınarbaşı Mesire Alanı’nda yaşanılan yoğun nüfus hareketliliğinden dolayı bölgede bir takım sorunların meydana geldiği görülmüş ve bu sorunların çözümü için çeşitli önerilerde bulunulmuştur.
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