KaydedilenlerDerginizi ekleyin

Dergiler / art / 2015 / Cilt: 30 - Sayı: 2

ADAMTS12 Depletion by Insulin in OUMS-27 Human Chondrosarcoma Cells

Aynur ALTUNTAŞ
Sümeyya AKYOL
Bahattin ADAM
Özlem ÇAKMAK
Veli UĞURCU
Gönül ERDEN
Yunus YÜKSELTEN
Kadir DEMİRCAN
Dergi
art
Sayfa
96–103
DOI
—
🏛️Bu makalenin bibliyografik verileri ve tam metin bağlantısı DergiPark üzerinden sağlanmıştır.
DergiPark Kaydı ↗
✨

Yapay Zeka Hızlı Bakış & Çıkarımlar

AI Insight
⚡ TL;DR(1 Cümlede Hızlı Çıkarım)

This reduction due to insulin treatment may contribute to recovery of cartilage tissue.

📌 3 Maddede Bu Makale

🎯
Amaç & Hipotez:Objectives: In this study, we aim to investigate the association between articular damage in diabetes and a disintegrin-like and metalloproteinase with thrombospondin motifs 12 (ADAMTS12) at gene expression and protein levels.
📊
Temel Bulgular & Veri:Materials and methods: OUMS-27 human chondrosarcoma cells were used to investigate how ADAMTS12 levels changed in vitro condition in presence and absence of insulin.
💡
Sonuç & Katkı:This reduction due to insulin treatment may contribute to recovery of cartilage tissue.
🔬Tür:Araştırma Makalesi
📍Kapsam:Genişletilmiş Akademik Örneklem
⚙️Değişkenler:Alan Parametreleri

Abstract

Objectives: In this study, we aim to investigate the association between articular damage in diabetes and a disintegrin-like and metalloproteinase with thrombospondin motifs 12 (ADAMTS12) at gene expression and protein levels. Materials and methods: OUMS-27 human chondrosarcoma cells were used to investigate how ADAMTS12 levels changed in vitro condition in presence and absence of insulin. The study included three groups of cells treated with 10 μg/mL of insulin, and a control group. Cells were incubated with insulin in medium for one day, three days, and seven days. The effects of insulin on ADAMTS12 were investigated at both gene expression and protein levels. The relationships between the variables were tested by Mann-Whitney U test. Results: ADAMTS12 expression was significantly lower in the groups treated with insulin medium for one day and seven day periods (p=0.008 and p=0.008, respectively) compared to the control group. No significant difference was detected in the expression level between the groups kept in insulin medium for three days and the control group (p=0.55). In addition, protein amounts of the groups exposed to insulin medium for one, three, and seven day periods were lower. Conclusion: Insulin reduces the amount of ADAMTS12 which causes delayed recovery of cartilage tissue in the OUMS-27 cell lines utilized in our study for their chondrocytic properties. This reduction due to insulin treatment may contribute to recovery of cartilage tissue.

🔖

Bu Makaleye Atıf Yap

ALTUNTAŞ, A., AKYOL, S., ADAM, B., ÇAKMAK, Ö., UĞURCU, V., ERDEN, G., YÜKSELTEN, Y., DEMİRCAN, K. (2015). ADAMTS12 Depletion by Insulin in OUMS-27 Human Chondrosarcoma Cells. art, Cilt: 30 - Sayı: 2, 96–103. https://ajindex.com/articles/351695

📄 Tam Metin PDF Okuyucu

📄

PDF görüntüleyici hazırlanıyor...

Kaynakça (14)

  1. Close DR. Matrix metalloproteinase inhibitors in rheumatic diseases. Ann Rheum Dis 2001;60:62-7
  2. Demircan K, Hirohata S, Nishida K, Hatipoglu OF, Oohashi T, Yonezawa T, et al. ADAMTS-9 is synergistically induced by interleukin-1beta and tumor necrosis factor alpha in OUMS-27 chondrosarcoma cells and in human chondrocytes. Arthritis Rheumatol 2005;52:1451-60
  3. Nagase H, Kashiwagi M. Aggrecanases and cartilage matrix degradation. Arthritis Res Ther 2003;5:94-103
  4. Koshy PJ, Lundy CJ, Rowan AD, Porter S, Edwards DR, Hogan A, et al. The modulation of matrix metalloproteinase and ADAM gene expression in human chondrocytes by interleukin-1 and oncostatin M: a time-course study using real-time quantitative reverse transcription-polymerase chain reaction. Arthritis Rheumatol 2002;46:961-7
  5. Apte SS. A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family. Int J Biochem Cell Biol 2004;36:981-5
  6. Melching LI, Fisher WD, Lee ER, Mort JS, Roughley PJ. The cleavage of biglycan by aggrecanases. Osteoarthritis Cartilage 2006;14:1147-54
  7. Cal S, Arguelles JM, Fernandez PL, Lopez-Otin C. Identification, characterization, and intracellular processing of ADAM-TS12, a novel human disintegrin with a complex structural organization involving multiple thrombospondin-1 repeats. J Biol Chem 2001;276:17932-40
  8. Liu CJ, Kong W, Xu K, Luan Y, Ilalov K, Sehgal B, et al. ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein. J Biol Chem 2006;281:15800-8
  9. Kurz T, Hoffjan S, Hayes MG, Schneider D, Nicolae R, Heinzmann A, et al. Fine mapping and positional candidate studies on chromosome 5p13 identify multiple asthma susceptibility loci. J Allergy Clin Immunol 2006;118:396-402
  10. Lin EA, Liu CJ. The role of ADAMTSs in arthritis. Protein Cell 2010;1:33-47
  11. Zhang Q, Huang M, Wang X, Xu X, Ni M, Wang Y. Negative effects of ADAMTS-7 and ADAMTS-12 on endplate cartilage differentiation. J Orthop Res 2012;30:1238-43
  12. Yu H, Zhu Y. Expression of ADAMTS-7 and ADAMTS-12 in the nucleus pulposus during degeneration of rat caudal intervetebral disc. J Vet Med Sci 2012;74:9-15
  13. Moncada-Pazos A, Obaya AJ, Llamazares M, Heljasvaara R, Suarez MF, Colado E, et al. ADAMTS-12 metalloprotease is necessary for normal inflammatory response. J Biol Chem 2012;287:39554-63
  14. Paulissen G, El Hour M, Rocks N, Gueders MM, Bureau F, Foidart JM, et al. Control of allergen- induced inflammation and hyperrespon