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In vitro growth and differentiated activities of human periodontal ligament fibroblasts cultured on salmon collagen gel
Author(s) -
Nagai Nobuhiro,
Mori Kazuo,
Satoh Yasuharu,
Takahashi Noritaka,
Yunoki Shunji,
Tajima Kenji,
Munekata Masanobu
Publication year - 2007
Publication title -
journal of biomedical materials research part a
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.849
H-Index - 150
eISSN - 1552-4965
pISSN - 1549-3296
DOI - 10.1002/jbm.a.31110
Subject(s) - periodontal fiber , osteocalcin , alkaline phosphatase , vinculin , in vitro , immunostaining , microbiology and biotechnology , type i collagen , materials science , biochemistry , chemistry , cytoskeleton , biology , immunology , dentistry , immunohistochemistry , medicine , cell , enzyme , endocrinology
Marine‐derived collagen is expected to be a much safer alternative to calf collagen, which in medical applications carries the risk of bovine spongiform encephalopathy. In this study, acid‐soluble collagen was extracted from salmon skin and crosslinked with 1‐ethyl‐3‐(3‐dimethylaminopropyl)‐carbodiimide during fibril formation to produce a crosslinked salmon collagen (SC) gel. The growth rates and the differentiated functions of human periodontal ligament fibroblasts (HPdLFs) cultured on the SC gel were investigated. Growth was faster on the SC gel than on porcine collagen (PC) gel. In addition, the HPdLFs cultured on the SC gel exhibited higher alkaline phosphatase (ALP) activity than those cultured on the PC gel. Quantitative RT‐PCR revealed higher mRNA expression of type I collagen, ALP, and osteocalcin in the HPdLFs cultured on the SC gel. HPdLFs had a flat shape on the SC gel and a spindle shape on the PC gel, as revealed by observation with scanning electron microscopy and immunostaining with cytoskeletal protein and vinculin. The results showed that HPdLFs could grow and show highly differentiated activity on the SC gel as well as on the PC gel. © 2007 Wiley Periodicals, Inc. J Biomed Mater Res, 2007