The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2.
Open accessAbstract
Simian virus 40 (SV40)-transformed human lung fibroblasts secrete both 72-kDa type IV collagenase and a closely related 92-kDa type IV collagenase that was not detected in the parental cell line. The 92-kDa type IV procollagenase purified from these cells exists in a noncovalent complex with the tissue inhibitor of metalloproteases, TIMP. Here we report that the 72-kDa type IV procollagenase purified from HRAS-transformed human bronchial epithelial cells, SV40-transformed lung fibroblasts, and normal skin fibroblasts exists in a stable but noncovalent stoichiometric complex with a 24-kDa inhibitor referred to here as "TIMP-2." TIMP-2 is closely related to TIMP, as demonstrated by comparison of the partial amino acid sequence of this protein to that of TIMP, although it does not cross-react with TIMP-specific antibody. The TIMP-2 inhibitor interacts with the 72-kDa type IV collagenase in preference to the 92-kDa type IV collagenase that forms a complex exclusively with TIMP. The 72-kDa type IV collagenase-TIMP-2 complex can be activated with organomercurials to yield a catalytically competent enzyme. Activation occurs concomitantly with autoproteolytic cleavage of the amino terminus of the protein and does not require dissociation of the complex. Both activity and activation of the complex can be completely inhibited by further addition of stoichiometric quantities of purified TIMP-2 or recombinant TIMP.
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Cites
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Tissue cooperation in a proteolytic cascade activating human interstitial collagenase.
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Self-citationChin, J. R., Murphy, G., & Werb, Z. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39034-8 · Cited by 495
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Antisense RNA-Induced Reduction in Murine TIMP Levels Confers Oncogenicity on Swiss 3T3 Cells
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The Activation of Human Type IV Collagenase Proenzyme
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Cited by
Yager, D. R., Zhang, L.-Y., Liang, H.-X., Diegelmann, R. F., & Cohen, I. K. (1996) · Journal of Investigative Dermatology · doi:10.1111/1523-1747.ep12365637 · Cited by 389
Matrix metalloproteinases in brain development and remodeling: Synaptic functions and targets
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Dog mastocytoma cells secrete a 92-kD gelatinase activated extracellularly by mast cell chymase.
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Shiryaev, S. A., Remacle, A. G., Golubkov, V. S., Ingvarsen, S., Porse, A., Behrendt, N., Cieplak, P., & Strongin, A. Y. (2013) · Oncogenesis · doi:10.1038/oncsis.2013.44 · Cited by 42
Metadata
- Authors
- Goldberg, G. I., Marmer, B. L., Grant, G. A., Eisen, A. Z., Wilhelm, S., & He, C. S.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1989-11
- Volume
- 86
- Issue
- 21
- Pages
- 8207-8211
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2004101410
- Cited by
- 586
- References
- 22
- FWCI
- 13.40
- Type
- journal article
- Language
- en
- Open access
- green
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- Goldberg, G. I., Marmer, B. L., Grant, G. A., Eisen, A. Z., Wilhelm, S., & He, C. S. (1989). Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.86.21.8207
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