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TIMP

TIMPs, tissue inhibitors of metalloproteinases, are the body's own blockers of MMPs and related enzymes. Humans have four, TIMP-1 to TIMP-4.

Also called tissue inhibitor of metalloproteinases, TIMP-1, TIMP-2, TIMP-3, TIMP-4.

TIMPs are found widely across the animal kingdom, and the human genome carries four TIMP genes (Brew 2010). They were first characterised as MMP inhibitors and also block several ADAM and ADAMTS enzymes, which makes them key regulators of the enzymes that break down the matrix around cells (Brew 2010). They have other roles too, in cell growth, migration and cell death (Brew 2010).

Active MMP13 was inhibited one to one by TIMP-1, TIMP-2 and TIMP-3: each TIMP molecule disables one enzyme molecule (Knäuper 1996).

Some studies measure TIMPs alongside MMPs. AKBA from boswellia raised TIMP-1 while suppressing MMP13 in rats (Abo-Zalam 2025), and chondroitin sulphate raised TIMP-1 and TIMP-2 in a human cartilage cell line (Hsu 2022).

Sources

  1. Brew K, Nagase H. The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity. Biochim Biophys Acta 2010.
  2. Knäuper V, López-Otin C, Smith B et al. Biochemical characterization of human collagenase-3. J Biol Chem 1996.
  3. Abo-Zalam HB, Gendy AM, Ali BM et al. Acetyl-11-keto-beta-boswellic acid ameliorates monosodium iodoacetate-induced osteoarthritis in rats: implications of HMGB1/TLR4/NF-κB and Nrf2/HO-1. Front Pharmacol 2025.
  4. Hsu HC, Ke YL, Lai YH et al. Chondroitin Sulfate Enhances Proliferation and Migration via Inducing β-Catenin and Intracellular ROS as Well as Suppressing Metalloproteinases through Akt/NF-κB Pathway Inhibition in Human Chondrocytes. J Nutr Health Aging 2022.

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Last reviewed 3 November 2026Every study cited here is indexed on PubMed. How we read the evidence