Cartilage tissue engineering using human auricular chondrocytes embedded in different hydrogel materials.
To seek a suitable scaffold for cartilage tissue engineering, we compared various hydrogel materials originating from animals, plants, or synthetic peptides. Human auricular chondrocytes were embedded in atelopeptide collagen, alginate, or PuraMatrix, all of which are or will soon be clinically available. The chondrocytes in the atelopeptide collagen proliferated well, while the others showed no proliferation. A high-cell density culture within each hydrogel enhanced the expression of collagen type II mRNA, when compared with that without hydrogel. By stimulation with insulin and BMP-2, collagen type II and glycosaminoglycan were significantly accumulated within all hydrogels. Chondrocytes in the atelopeptide collagen showed high expression of beta1 integrin, seemingly promoting cell-matrix signaling. The N-cadherin expression was inhibited in the alginate, implying that decrease in cell-to-cell contacts may maintain chondrocyte activity. The matrix synthesis in PuraMatrix was less than that in others, while its Young's modulus was the lowest, suggesting a weakness in gelling ability and storage of cells and matrices. Considering biological effects and clinical availability, atelopeptide collagen may be accessible for clinical use. However, because synthetic peptides can control the risk of disease transmission and immunoreactivities, some improvement in gelling ability would provide a more useful hydrogel for ideal cartilage regeneration.
Yamaoka
Hisayo
H
Department of Fujisoft ABC Cartilage and Bone Regeneration, Graduate School of Medicine, The University of Tokyo, Hongo 7-3-1, Bunkyo-Ku, Tokyo 113-0033, Japan.
Asato
Hirotaka
H
Ogasawara
Toru
T
Nishizawa
Satoru
S
Takahashi
Tsuguharu
T
Nakatsuka
Takashi
T
Koshima
Isao
I
Nakamura
Kozo
K
Kawaguchi
Hiroshi
H
Chung
Ung-il
UI
Takato
Tsuyoshi
T
Hoshi
Kazuto
K
D020517:Atrial Appendage / Q000166:cytology / Q000502:physiology; D055396:Bone Morphogenetic Protein 2; D019485:Bone Morphogenetic Proteins / Q000494:pharmacology; D002356:Cartilage / Q000166:cytology / Q000502:physiology; D002450:Cell Communication / Q000187:drug effects / Q000502:physiology; D002478:Cells, Cultured; D019902:Chondrocytes / Q000166:cytology; D024043:Collagen Type II / Q000096:biosynthesis; D005786:Gene Expression Regulation / Q000187:drug effects / Q000502:physiology; D006025:Glycosaminoglycans / Q000494:pharmacology; D006801:Humans; D020100:Hydrogels / Q000737:chemistry; D007004:Hypoglycemic Agents / Q000494:pharmacology; D007328:Insulin / Q000494:pharmacology; D023822:Tissue Engineering; D016212:Transforming Growth Factor beta / Q000494:pharmacology
C525718:BMP2 protein, human; D055396:Bone Morphogenetic Protein 2; D019485:Bone Morphogenetic Proteins; D024043:Collagen Type II; D006025:Glycosaminoglycans; D020100:Hydrogels; D007004:Hypoglycemic Agents; D007328:Insulin; D016212:Transforming Growth Factor beta; C020341:glucosaminoglycans