期刊论文详细信息
BMC Musculoskeletal Disorders
High glucose concentration up-regulates the expression of matrix metalloproteinase-9 and -13 in tendon cells
Jong-Hwei S Pang3  Hsiang-Hung Chen1  Shih-Chieh Chang2  Li-Ping Lin1  Ju-Wen Cheng1  Fang-Chen Liang1  Wen-Chung Tsai4 
[1] Department of Physical Medicine and Rehabilitation, Chang Gung Memorial Hospital at Linkou, Taoyuan, Taiwan;School of Medicine, Chung Shan Medical University, Taichung, Taiwan;Graduate Institute of Clinical Medical Sciences, Chang Gung University, Taoyuan, Taiwan;College of Medicine, Chang Gung University, Taoyuan, Taiwan
关键词: Tendon;    Matrix metalloproteinase;    Glucose;   
Others  :  1129870
DOI  :  10.1186/1471-2474-14-255
 received in 2013-03-19, accepted in 2013-08-23,  发布年份 2013
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【 摘 要 】

Background

Diabetes mellitus is associated with tendinopathy or tendon injuries. However, the mechanism underlying diabetic tendinopathy is unclear. The purpose of this study was to examine the effects of high glucose concentrations on the activity and expression of matrix metalloproteinases, type I collagen, and type III collagen in tendon cells.

Methods

Tendon cells from rat Achilles tendons were treated with 6 mM, 12 mM, and 25 mM glucose, and then cell proliferation was evaluated by the 3-[4,5-Dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide (MTT) assay. Messenger RNA (mRNA) expression of MMP-2, MMP-8, MMP-9, and MMP-13 and type I and type III collagen was assessed by quantitative real-time polymerase chain reaction (PCR). The enzymatic activity of MMP-2 and MMP-9 was measured by gelatin zymography.

Results

The MTT assay results showed that the glucose concentration did not affect tendon cell proliferation. The results of the real-time PCR assay revealed that the mRNA expression of MMP-9 and MMP-13 was up-regulated by treatment with 25 mM glucose, whereas the mRNA expression of type I and III collagen was not affected. Gelatin zymography showed that 25 mM glucose increased the enzymatic activity of MMP-9.

Conclusions

High glucose concentration up-regulates the expression of MMP-9 and MMP-13 in tendon cells, which may account for the molecular mechanisms underlying diabetic tendinopathy.

【 授权许可】

   
2013 Tsai et al.; licensee BioMed Central Ltd.

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【 参考文献 】
  • [1]Balci N, Balci MK, Tuzuner S: Shoulder adhesive capsulitis and shoulder range of motion in type II diabetes mellitus: association with diabetic complications. J Diabetes Complications 1999, 13:135-140.
  • [2]Mavrikakis ME, Drimis S, Kontoyannis DA, Rasidakis A, Moulopoulou ES, Kontoyannis S: Calcific shoulder periarthritis (tendinitis) in adult onset diabetes mellitus: a controlled study. Ann Rheum Dis 1989, 48:211-214.
  • [3]Pal B, Anderson J, Dick WC, Griffiths ID: Limitation of joint mobility and shoulder capsulitis in insulin- and non-insulin-dependent diabetes mellitus. Br J Rheumatol 1986, 25:147-151.
  • [4]Ramchurn N, Mashamba C, Leitch E, Arutchelvam V, Narayanan K, Weaver J, Hamilton J, Heycock C, Saravanan V, Kelly C: Upper limb musculoskeletal abnormalities and poor metabolic control in diabetes. Eur J Intern Med 2009, 20:718-721.
  • [5]Cagliero E, Apruzzese W, Perlmutter GS, Nathan DM: Musculoskeletal disorders of the hand and shoulder in patients with diabetes mellitus. Am J Med 2002, 112:487-490.
  • [6]Leadbetter WB: Cell-matrix response in tendon injury. Clin Sports Med 1992, 11:533-578.
  • [7]Amiel D, Frank C, Harwood F, Fronek J, Akeson W: Tendons and ligaments: a morphological and biochemical comparison. J Orthop Res 1984, 1:257-265.
  • [8]Jones GC, Corps AN, Pennington CJ, Clark IM, Edwards DR, Bradley MM, Hazleman BL, Riley GP: Expression profiling of metalloproteinases and tissue inhibitors of metalloproteinases in normal and degenerate human achilles tendon. Arthritis Rheum 2006, 54:832-842.
  • [9]Vu TH, Werb Z: Matrix metalloproteinases: effectors of development and normal physiology. Genes Dev 2000, 14:2123-2133.
  • [10]Ireland D, Harrall R, Curry V, Holloway G, Hackney R, Hazleman B, Riley G: Multiple changes in gene expression in chronic human Achilles tendinopathy. Matrix Biol 2001, 20:159-169.
  • [11]Sharma P, Maffulli N: Tendon injury and tendinopathy: healing and repair. J Bone Joint Surg Am 2005, 87:187-202.
  • [12]Matrisian LM: The matrix-degrading metalloproteinases. Bioessays 1992, 14:455-463.
  • [13]Nagase H, Woessner JF Jr: Matrix metalloproteinases. J Biol Chem 1999, 274:21491-21494.
  • [14]Aimes RT, Quigley JP: Matrix metalloproteinase-2 is an interstiti collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments. J Biol Chem 1995, 270:5872-5876.
  • [15]Oshiro W, Lou J, Xing X, Tu Y, Manske PR: Flexor tendon healing in the rat: a histologic and gene expression study. J Hand Surg Am 2003, 28:814-823.
  • [16]Chen J, Cui X, Zacharek A, Cui Y, Roberts C, Chopp M: White matter damage and the effect of matrix metalloproteinases in type 2 diabetic mice after stroke. Stroke 2011, 42:445-452.
  • [17]Tarallo S, Beltramo E, Berrone E, Dentelli P, Porta M: Effects of high glucose and thiamine on the balance between matrix metalloproteinases and their tissue inhibitors in vascular cells. Acta Diabetol 2010, 47:105-111.
  • [18]Uemura S, Matsushita H, Li W, Glassford AJ, Asagami T, Lee KH, Harrison DG, Tsao PS: Diabetes mellitus enhances vascular matrix metalloproteinase activity: role of oxidative stress. Circ Res 2001, 88:1291-1298.
  • [19]Hao F, Yu JD: High glucose enhance expression of matrix metalloproteinase-2 in smooth muscle cells. Acta Pharmacol Sin 2003, 24:534-538.
  • [20]Lee SJ, Bae SS, Kim KH, Lee WS, Rhim BY, Hong KW, Kim CD: High glucose enhances MMP-2 production in adventitial fibroblasts via Akt1-dependent NF-kappaB pathway. FEBS Lett 2007, 581:4189-4194.
  • [21]Zhang L, Li X, Bi LJ: Alterations of collagen-I, MMP-1 and TIMP-1 in the periodontal ligament of diabetic rats under mechanical stress. J Periodontal Res 2011, 46:448-455.
  • [22]Bedi A, Fox AJ, Harris PE, Deng XH, Ying L, Warren RF, Rodeo SA: Diabetes mellitus impairs tendon-bone healing after rotator cuff repair. J Shoulder Elbow Surg 2010, 19:978-988.
  • [23]Vogt BW, Schleicher ED, Wieland OH: Epsilon-Amino-lysine-bound glucose in human tissues obtained at autopsy. Increase in diabetes mellitus. Diabetes 1982, 31:1123-1127.
  • [24]Kislinger T, Fu C, Huber B, Qu W, Taguchi A, Du-Yan S, Hofmann M, Yan SF, Pischetsrieder M, Stern D, Schmidt AM: N(epsilon)-(carboxymethyl)lysine adducts of proteins are ligands for receptor for advanced glycation end products that activate cell signaling pathways and modulate gene expression. J Biol Chem 1999, 274:31740-31749.
  • [25]Nah SS, Choi IY, Yoo B, Kim YG, Moon HB, Lee CK: Advanced glycation end products increases matrix metalloproteinase-1, -3, and -13, and TNF-alpha in human osteoarthritic chondrocytes. FEBS Lett 2007, 581:1928-1932.
  • [26]Liu JQ, Liu HC, Wang Y, Feng Y, Gao H: The biological effect of high glucose on human periodontal ligament fibroblast. Shanghai Kou Qiang Yi Xue 2011, 20:225-229.
  • [27]Higuchi C, Sanaka T, Sato T, Omata M, Watanabe M, Mine S, Inuzuka N, Nihei H: The effect of glucose on the proliferation of peritoneal fibroblasts. Adv Perit Dial 1997, 13:253-256.
  • [28]Lan CC, Liu IH, Fang AH, Wen CH, Wu CS: Hyperglycaemic conditions decrease cultured keratinocyte mobility: implications for impaired wound healing in patients with diabetes. Br J Dermatol 2008, 159:1103-1115.
  • [29]Karousou E, Ronga M, Vigetti D, Passi A, Maffulli N: Collagens, proteoglycans, MMP-2, MMP-9 and TIMPs in human achilles tendon rupture. Clin Orthop Relat Res 2008, 466:1577-1582.
  • [30]Choi HR, Kondo S, Hirose K, Ishiguro N, Hasegawa Y, Iwata H: Expression and enzymatic activity of MMP-2 during healing process of the acute supraspinatus tendon tear in rabbits. J Orthop Res 2002, 20:927-933.
  • [31]Pasternak B, Schepull T, Eliasson P, Aspenberg P: Elevation of systemic matrix metalloproteinases 2 and 7 and tissue inhibitor of metalloproteinase 2 in patients with a history of Achilles tendon rupture: pilot study. Br J Sports Med 2010, 44:669-672.
  • [32]Jain A, Brennan F, Troeberg L, Nanchahal J: The role of matrix metalloproteinases in rheumatoid tendon disease. J Hand Surg Am 2002, 27:1059-1064.
  • [33]Danielsen PL, Holst AV, Maltesen HR, Bassi MR, Holst PJ, Heinemeier KM, Olsen J, Danielsen CC, Poulsen SS, Jorgensen LN, Agren MS: Matrix metalloproteinase-8 overexpression prevents proper tissue repair. Surgery 2011, 150:897-906.
  • [34]Lakemeier S, Braun J, Efe T, Foelsch C, Archontidou-Aprin E, Fuchs-Winkelmann S, Paletta JR, Schofer MD: Expression of matrix metalloproteinases 1, 3, and 9 in differing extents of tendon retraction in the torn rotator cuff. Knee Surg Sports Traumatol Arthrosc 2011, 19:1760-1765.
  • [35]Lo IK, Marchuk LL, Hollinshead R, Hart DA, Frank CB: Matrix metalloproteinase and tissue inhibitor of matrix metalloproteinase mRNA levels are specifically altered in torn rotator cuff tendons. Am J Sports Med 2004, 32:1223-1229.
  • [36]Thomas K, Kiwit M, Kerner W: Glucose concentration in human subcutaneous adipose tissue: comparison between forearm and abdomen. Exp Clin Endocrinol Diabetes 1998, 106:465-469.
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