Differential induction of collagens by mechanical stress in human periodontal ligament cells.
OBJECTIVE
Excessive mechanical stress (MS) during hyperocclusion is known to result in destruction of periodontal tissues and alveolar bone, leading to occlusal trauma. Collagens are extracellular matrix components that are encoded by more than 30 different genes. They are classified into three types: fibril-forming, fibril-associated with interrupted triple helices (FACIT), and non-fibril forming collagens. Although MS is known to affect COL I, little is known about its effects on other types of collagens in the periodontal ligament (PDL). We hypothesised that MS could induce expression of the three different types of collagens, thus protecting against occlusal trauma.


METHODS
The aim of this study was to investigate intermittent uniaxial stretching-induced collagen expression in PDL cells using DNA microarray, polymerase chain reaction, and western blotting analysis. We compared changes in collagen expression caused by MS stimulation and osteogenic stimulation, and examined relationships between expression of collagen and their digestive enzymes, matrix metalloproteases (MMPs).


RESULTS
Expression of both fibril-forming and FACIT collagens was transiently decreased in the initial phase after MS, while the expression of non-fibril-forming collagens was gradually increased. MS for 3-7 days resulted in gradual upregulation of all three types of collagen. Furthermore, the expression of fibril- and non-fibril-forming collagens was reciprocally related to expression of MMPs. In contrast, expression of all three types of collagen was slightly upregulated during osteogenesis.


CONCLUSIONS
The MS-induced expression patterns of fibril-forming and FACIT collagens suggest changes in the composition of the extracellular matrix to increase the resistance of PDL cells to hyperocclusal force.
Nemoto
Tetsuomi
T
Department of Physiological Science and Molecular Biology, Fukuoka Dental College, Tamura 2-15-1, Sawara-ku, Fukuoka 8140193, Japan.
Kajiya
Hiroshi
H
Tsuzuki
Takashi
T
Takahashi
Yutaka
Y
Okabe
Koji
K
D000328:Adult; D001696:Biomechanical Phenomena; D015153:Blotting, Western; D018929:Cell Culture Techniques; D002478:Cells, Cultured; D003094:Collagen / Q000096:biosynthesis*; D024042:Collagen Type I / Q000096:biosynthesis; D024141:Collagen Type IV / Q000096:biosynthesis; D024082:Collagen Type XII / Q000096:biosynthesis; D024021:Fibril-Associated Collagens / Q000096:biosynthesis; D024022:Fibrillar Collagens / Q000096:biosynthesis; D020869:Gene Expression Profiling; D006801:Humans; D020781:Matrix Metalloproteinase 1 / Q000378:metabolism; D019278:Matrix Metalloproteinase 3 / Q000378:metabolism; D020782:Matrix Metalloproteinases / Q000378:metabolism; D024041:Non-Fibrillar Collagens / Q000096:biosynthesis; D020411:Oligonucleotide Array Sequence Analysis; D010012:Osteogenesis / Q000502:physiology; D010513:Periodontal Ligament / Q000166:cytology / Q000378:metabolism*; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013314:Stress, Mechanical; D013997:Time Factors; D015854:Up-Regulation; D055815:Young Adult
D024042:Collagen Type I; D024141:Collagen Type IV; D024082:Collagen Type XII; D024021:Fibril-Associated Collagens; D024022:Fibrillar Collagens; D024041:Non-Fibrillar Collagens; D003094:Collagen; D020782:Matrix Metalloproteinases; C511768:MMP3 protein, human; D019278:Matrix Metalloproteinase 3; C522360:MMP1 protein, human; D020781:Matrix Metalloproteinase 1