June 2013
Volume 54, Issue 15
Free
ARVO Annual Meeting Abstract  |   June 2013
Microparticle Delivery of Matrix Metalloproteinase-3 to Trabecular Meshwork Cells
Author Affiliations & Notes
  • Beatrice Yue
    Ophthal & Vis Sciences, Univ of Illinois at Chicago, Chicago, IL
  • Sanja Turturro
    Ophthal & Vis Sciences, Univ of Illinois at Chicago, Chicago, IL
  • Suhair Sunoqrot
    Departments of Biopharmaceutical Sciences and Bioengineering, University of Illinois at Chicago, Chicago, IL
  • Hongyu Ying
    Ophthal & Vis Sciences, Univ of Illinois at Chicago, Chicago, IL
  • Seungpyo Hong
    Departments of Biopharmaceutical Sciences and Bioengineering, University of Illinois at Chicago, Chicago, IL
  • Footnotes
    Commercial Relationships Beatrice Yue, None; Sanja Turturro, None; Suhair Sunoqrot, None; Hongyu Ying, None; Seungpyo Hong, None
  • Footnotes
    Support None
Investigative Ophthalmology & Visual Science June 2013, Vol.54, 3540. doi:
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      Beatrice Yue, Sanja Turturro, Suhair Sunoqrot, Hongyu Ying, Seungpyo Hong; Microparticle Delivery of Matrix Metalloproteinase-3 to Trabecular Meshwork Cells. Invest. Ophthalmol. Vis. Sci. 2013;54(15):3540.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Purpose: To test the feasibility of using microparticles for slow and sustained release of active matrix metalloproteinase-3 (MMP-3) to degrade extracellular matrix (ECM) elements such as fibronectin in cultured human trabecular meshwork (TM) cells. Accumulation of ECM materials in the TM is believed to be a contributing factor to intraocular pressure elevation, a major risk factor/cause of primary open angle glaucoma.

Methods: β-casein, with molecular weight (26 kDa) and hydrophobicity similar to those of the active MMP-3 fragment (19.2 kDa), was used for the initial testing. β-casein (2.2 mg) was encapsulated into poly(lactic-co-glycolic acid) (PLGA) microparticles following a double emulsion procedure. The protein amount encapsulated into the microparticles was measured by Bradford protein assay and the encapsulation efficiency was determined. The release test was conducted in Dulbecco’s Eagle’s minimum essential medium (DMEM) without or with the presence of human TM cells. Encapsulation of active MMP-3 (5 µg) into PLGA microparticles was subsequently carried out. Human TM cells pretreated with 100 nM of dexamethasone (DEX, to induce fibronectin expression) were set up as an assay platform for MMP-3. The fibronectin degradation or reduction of fibronectin levels was used as an indicator of the enzyme activity.

Results: The encapsulation efficiency for β-casein was around 53%. The release test showed a slow and sustained release of β-casein over 20 days. The encapsulation efficiency for MMP-3 was estimated to be approximately 50%. The release medium collected from MMP-3-microparticle treated cultures, compared to that from empty- and β-casein-microparticle controls, markedly reduced the fibronectin staining in DEX-pretreated TM cells. The MMP-3 released to the culture medium was found active, still capable of degrading fibronectin after 9 days of incubation.

Conclusions: This study demonstrated the feasibility of encapsulating MMP-3 into polymeric microparticles and the potential of delivering active enzyme to TM cells.

Keywords: 735 trabecular meshwork • 607 nanotechnology • 519 extracellular matrix  
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