Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.17 (MMP-3)
 3,419 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Women are more susceptible to anterior cruciate ligament (ACL) injuries than men performing similar athletic activities. Because tissue remodeling may affect ligament strength, we assessed expression of tissue remodeling effector genes in the human ACL. Specifically, we surveyed ACL for RNAs encoding all known matrix metalloproteases (MMPs) and tissue inhibitors of metalloproteases (TIMPs) by reverse transcription/polymerase chain reaction (RT-PCR). These experiments revealed that mRNAs encoding nine of sixteen MMPs and all four TIMPs are present in the normal ACL. The nine expressed proteases were MMPs 1-3, 7, 9, 11, 14, and 17 (collagenase 1, gelatinase A, stromelysin 1, matrilysin, gelatinase B, stromelysin 3, and membrane types 1 and 4, respectively), and MMP-18. Genes for MMPs 8, 10, 12, 13, 15, and 16 appeared not to be expressed in ACL, as their mRNAs were not detected using RT-PCR conditions that did yield positive signals from other tissues (testis or bone). We conclude that numerous genes encoding tissue remodeling effector proteins are expressedin the human ACL.
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PMID:Expression of matrix metalloprotease and tissue inhibitor of metalloprotease genes in human anterior cruciate ligament. 1151 74

Genetic diseases and knockout mice stress the importance of matrix metalloproteinases (MMPs) in skeletal turnover. Our study aims at clarifying which MMPs are expressed by osteoclasts. Previous analyses of this basic question led to conflicting reports in the literature. In the present study, we used a variety of approaches: PCR, Northern blots, Slot blots, in situ hybridization, and immunohistochemistry. We analyzed osteoclasts in culture as well as osteoclasts in native bone at different locations and compared mouse and rabbit osteoclasts. Osteoclasts express MMP-9 and -14 in all conditions, although to a variable extent, and they are able to synthesize MMP-3, -10, and -12, at least under some circumstances. The induction of a given MMP in osteoclasts is influenced by its environment (e.g., osteoclast culture vs. native bone, and various sites within the same bone) and depends on the species (e.g., mouse vs. rabbit). Osteoclasts show high amounts of MMP-2 and -13 protein presumably made to a large extent by other cells, thereby documenting how proteinases of nonosteoclastic origin may contribute to osteoclast activities and giving insight in why the resorptive activity of purified osteoclasts appears insensitive to MMP inhibitors. Our study shows that the confusion about osteoclastic MMPs in the literature reflects the remarkable ability of osteoclasts to adapt to their environment, as required by the structural or functional diversity of bone tissue. Our observations provide basic information needed for understanding the emerging role of MMPs in controlling cell signaling and bone resorption.
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PMID:A scrutiny of matrix metalloproteinases in osteoclasts: evidence for heterogeneity and for the presence of MMPs synthesized by other cells. 1554 36