PMID- 9203094 OWN - NLM STAT- MEDLINE DCOM- 19970717 LR - 20061115 IS - 0022-3492 (Print) IS - 0022-3492 (Linking) VI - 68 IP - 6 DP - 1997 Jun TI - Effects of interleukin-1 beta on matrix metalloproteinase-3 levels in human periodontal ligament cells. PG - 517-23 AB - MATRIX METALLOPROTEINASE-3 (MMP-3), or stromelysin-1, is an enzyme responsible for the degradation of a wide range of extracellular matrix proteins. Increases in MMP-3 activity have been found in several chronic inflammatory diseases, and this increased activity is thought to be mediated by interleukin-1 beta (IL-1 beta). Because IL-1 beta has been strongly associated with inflammatory periodontal disease, the purpose of this in vitro study was to investigate the role of IL-1 beta on the regulation of MMP-3 levels in cells derived from the human periodontal ligament (PDL). Human PDL cell cultures were treated with IL-1 beta at varying concentrations (0.01-1.0 ng/ml) for 24 hour prior to analysis at either transcript or protein levels. Following the isolation of total RNA, the relative levels of MMP-3 mRNA were determined using reverse transcription-polymerase chain reaction (RT-PCR) with 32P-end-labeled primers. Immunocytochemical detection of MMP-3 protein was performed using polyclonal antibodies to human MMP-3. The results of RT-PCR analysis demonstrated a concentration-dependent increase in MMP-3 mRNA expression, with IL-1 beta treatments of 0.1 and 1.0 ng/ml significantly (P < 0.01) increased over those cells not treated with IL-1 beta. This increase in mRNA expression was paralleled by significant (P < 0.001) changes at the protein level, with an average of 27.6% of the cells stained positive for MMP-3 following IL-1 beta treatment (1.0 ng/ml), compared with control cells showing no positive staining for MMP-3. In conclusion, the results of this study demonstrate that IL-1 beta upregulates MMP-3 in human PDL cells on both an mRNA and a protein level. These findings suggest possibly important roles for IL-1 beta and MMP-3 in both normal turnover and maintenance of the PDL and in the connective tissue degradation associated with periodontal disease. FAU - Nakaya, H AU - Nakaya H AD - Department of Periodontics, University of Texas Health Science Center at San Antonio, USA. FAU - Oates, T W AU - Oates TW FAU - Hoang, A M AU - Hoang AM FAU - Kamoi, K AU - Kamoi K FAU - Cochran, D L AU - Cochran DL LA - eng PT - Journal Article PL - United States TA - J Periodontol JT - Journal of periodontology JID - 8000345 RN - 0 (Extracellular Matrix Proteins) RN - 0 (Interleukin-1) RN - 0 (RNA, Messenger) RN - 0 (Recombinant Proteins) RN - EC 3.4.24.17 (Matrix Metalloproteinase 3) SB - IM MH - Analysis of Variance MH - Cells, Cultured MH - Enzyme Induction/drug effects/physiology MH - Extracellular Matrix Proteins/metabolism MH - Fibroblasts/drug effects/enzymology MH - Humans MH - Immunoenzyme Techniques MH - Interleukin-1/*pharmacology/*physiology MH - Matrix Metalloproteinase 3/*biosynthesis MH - Periodontal Ligament/cytology/drug effects/*enzymology MH - Periodontitis/enzymology MH - Polymerase Chain Reaction/methods MH - RNA, Messenger/analysis MH - Recombinant Proteins/pharmacology MH - Statistics, Nonparametric MH - Up-Regulation EDAT- 1997/06/01 00:00 MHDA- 1997/06/01 00:01 CRDT- 1997/06/01 00:00 PHST- 1997/06/01 00:00 [pubmed] PHST- 1997/06/01 00:01 [medline] PHST- 1997/06/01 00:00 [entrez] AID - 10.1902/jop.1997.68.6.517 [doi] PST - ppublish SO - J Periodontol. 1997 Jun;68(6):517-23. doi: 10.1902/jop.1997.68.6.517.