Comparison of three types of chondrocytes in collagen scaffolds for cartilage tissue engineering

Biomed Mater. 2009 Aug;4(4):045012. doi: 10.1088/1748-6041/4/4/045012. Epub 2009 Jul 28.

Abstract

The objective of this study was to compare the chondrogenesis in type I and II collagen scaffolds seeded with chondrocytes from three types of cartilage, after four weeks of culture: auricular (AU), articular (AR) and meniscal (ME). Related aims were to investigate the expression of a contractile muscle actin isoform, alpha-smooth muscle actin (SMA), in the cells in the scaffold and to determine the presence of a lubricating glycoprotein, lubricin, in the constructs. Adult goat AU, AR and ME chondrocytes were seeded into two types of collagen scaffolds: type II collagen and type I/III collagen. After four weeks of culture, the constructs were prepared for histochemical and immunohistochemical analysis of the distribution of glycosaminoglycan (GAG), types I and II collagen, elastin, SM and lubricin. AU constructs contained substantially more tissue than the AR and ME samples. The AU constructs exhibited neocartilage, but no elastin. There were no notable differences between the type I and II collagen scaffolds. Novel findings were the expression of SMA by the AU cells in the scaffolds and the presence of lubricin in the AR and AU constructs. AU cells have the capability to produce cartilage in collagen scaffolds under conditions in which there is little histogenesis by AR and ME cells.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Animals
  • Cartilage / cytology*
  • Cartilage / metabolism*
  • Chondrocytes* / cytology
  • Chondrocytes* / metabolism
  • Chondrocytes* / physiology
  • Chondrogenesis
  • Collagen / metabolism*
  • Collagen Type II / metabolism
  • Extracellular Matrix / metabolism
  • Glycosaminoglycans / metabolism
  • Goats
  • Muscle Contraction
  • Tissue Engineering / methods*

Substances

  • Actins
  • Collagen Type II
  • Glycosaminoglycans
  • Collagen