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3D poly(1,8 Octanediol-co-Citrate) (POC) scaffold pore shape and permeability effects on sub-cutaneous in vivo chondrogenesis using primary chondrocytes.

07:11 EDT 18th May 2013 | BioPortfolio

Summary of "3D poly(1,8 Octanediol-co-Citrate) (POC) scaffold pore shape and permeability effects on sub-cutaneous in vivo chondrogenesis using primary chondrocytes."

The objective of this study was to evaluate the coupled effects of 3D POC scaffold pore shape and permeability on chondrogenesis using primary chondrocytes in vivo. Chondrogenesis was characterized by cartilage matrix formation via sulfated glycosaminoglycan (sGAG) quantification, relative mRNA expressions of cartilage related proteins type 1, 2, 10 collagens, aggrecan, and matrix metalloproteinase 13 & 3 (MMP13, MMP3), and tissue/scaffold construct compressive mechanical properties. The low permeable design with spherical pore shapes showed a significantly higher increase in cartilage matrix formation over 6 weeks in vivo than the high permeable design with a cubical pore shape. This increase in cartilage matrix synthesis corresponded with increases in mechanical compressive nonlinear elastic properties and histological data demonstrating darker red Safranin-O staining. There were higher mRNA expressions for both cartilage specific proteins and matrix degradation proteins in the high permeable design, resulting in overall less sGAG retained in the high permeable scaffold compared with the low permeable scaffold. Controlled POC scaffold spherical pore shape and low permeability correlated with significantly increased cartilage matrix production using primary seeded chondrocytes. These results indicate that the low permeable design with spherical pore shape provided a better microenvironment for chondrogenesis than the high permeable design with cubical pore shape. Thus, scaffold architecture design and material may have significant impact on the success of matrix based clinical cartilage repair strategies.

Affiliation

Department of Biomedical Engineering, University of Michigan, Ann Arbor, Michigan, 48109-2125, USA.

Journal Details

This article was published in the following journal.

Name: Acta biomaterialia
ISSN: 1878-7568
Pages:

Links

Medical and Biotech [MESH] Definitions

Poly(a)-binding Protein Ii

A poly(A) binding protein that is involved in promoting the extension of the poly A tails of MRNA. The protein requires a minimum of ten ADENOSINE nucleotides in order for binding to mRNA. Once bound it works in conjunction with CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR to stimulate the rate of poly A synthesis by POLY A POLYMERASE. Once poly-A tails reach around 250 nucleotides in length poly(A) binding protein II no longer stimulates POLYADENYLATION. Mutations within a GCG repeat region in the gene for poly(A) binding protein II have been shown to cause the disease MUSCULAR DYSTROPHY, OCULOPHARYNGEAL.

Atp Citrate (pro-s)-lyase

An enzyme that, in the presence of ATP and COENZYME A, catalyzes the cleavage of citrate to yield acetyl CoA, oxaloacetate, ADP, and ORTHOPHOSPHATE. This reaction represents an important step in fatty acid biosynthesis. This enzyme was formerly listed as EC 4.1.3.8.

Nucleocytoplasmic Transport Proteins

Proteins involved in the process of transporting molecules in and out the cell nucleus. Included here are: NUCLEOPORINS, which are membrane proteins that form the NUCLEAR PORE COMPLEX; KARYOPHERINS, which carry molecules through the nuclear pore complex; and proteins that play a direct role in the transport of karyopherin complexes through the nuclear pore complex.

Poly(a)-binding Protein I

A poly(A) binding protein that has a variety of functions such as mRNA stabilization and protection of RNA from nuclease activity. Although poly(A) binding protein I is considered a major cytoplasmic RNA-binding protein it is also found in the CELL NUCLEUS and may be involved in transport of mRNP particles.

Citrate (si)-synthase

Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and coenzyme A. This enzyme was formerly listed as EC 4.1.3.7.

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