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• W1556547170 abstract "To the Editor: A recent JID paper byHerouy et al., 1998Herouy Y. May A.E. Pornschlegel G. et al.Lipodermatosclerosis is characterized by elevated expression and activation of matrix metalloproteinases: implications for venous ulcer formation.J Invest Dermatol. 1998; 111: 822-827Abstract Full Text Full Text PDF PubMed Scopus (113) Google Scholar presented some interesting new data on lipodermatoschlerosis. Their interpretations of the data, however, are based upon a single paper in the MMP literature (Aimes and Quigley, 1995Aimes R.T. Quigley J.P. Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4 and 1/4 length fragments.J Biol Chem. 1995; 270: 5872-5876Crossref PubMed Scopus (798) Google Scholar), which claims that MMP2 (gelatinase A) is an interstitial collagenase, a claim that we have not been able to confirm. We were the first laboratory to purify, characterize, and clone human MMP2 (Seltzer et al., 1981Seltzer J.L. Adams S.A. Grant G.A. Eisen A.Z. Purification and properties of a gelatin-specific neutral protease from human skin.J Biol Chem. 1981; 256: 4662-4668Abstract Full Text PDF PubMed Google Scholar;Collier et al., 1988Collier I.E. Wilhelm S.M. Eisen A.Z. et al.H-ras oncogene-transformed human bronchial-eptiehlial cells (TBE-1) secrete a single metalloproteinase capable of degrading basement membrane collagen.J Biol Chem. 1988; 263: 6579-6587Abstract Full Text PDF PubMed Google Scholar). We found that this proteinase had absolutely no activity against helical collagen. Native helical collagen is defined by its resistance to trypsin cleavage and characteristic viscosity in solution. Subsequent work from our laboratory has shown that MMP2 is an extremely opportunistic proteinase against any collagenous sequence in which the helicity is not perfect. For example, MMP2 cleaves helical type VII collagen within the helical portion of the molecule, but in an area that has relaxed helicity (Seltzer et al., 1989Seltzer J.L. Eisen A.Z. Bauer E.A. Burgeson R.E. Cleavage of type VII collagen by interstitial collagenase and type IV collagenase (gelatinase) derived from human skin.J Biol Chem. 1989; 264: 3822-3826Abstract Full Text PDF PubMed Google Scholar). When the Aimes and Quigley paper was published we confirmed our original observations using pure TIMP-free MMP2 and helical collagen shown to be trypsin resistant. Interstitial type I collagen in which the helix was relaxed enough to render it susceptible to trypsin digestion was indeed susceptible to digestion by MMP2. Intact helical collagen was not.Ohuchi et al., 1997Ohuchi E. Kazushi I. Fuji Y. Sata H. Seiki H. Okada Y. Membrane type I matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules.J Biol Chem. 1997; 272: 2446-2451Crossref PubMed Scopus (804) Google Scholar have recently reconfirmed our original findings. Cleavage of interstitial collagen by MMP1 yields two characteristic fragments, which lose their helicity at 37°C and become soluble. Therefore, solubilization of type I collagen is not indicative of MMP2 activity, but is of MMP1 activity. Herouy et al. clearly show active MMP1 in their western immunoblots, indicating that cleavage of labeled type I collagen by their extracts can definitely occur. It is important to point out that TIMP-MMP complexes have been previously described, but are separated when subjected to SDS-PAGE electrophoresis (Goldberg et al., 1989Goldberg G.I. Marmer B.L. Grant G.A. Eisen A.Z. Wilhelm S. He C. Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2.Proc Natl Acad Sci USA. 1989; 86: 8207-8211Crossref PubMed Scopus (533) Google Scholar;Wilhelm et al., 1989Wilhelm S.M. Collier I.E. Marmer B.L. Eisen A.Z. Grant G.A. Goldberg G.I. SV40-transformed human lung fibroblasts secrete a 92 kDa type IV collagenase which is identical to that secreted by normal human macrophages.J Biol Chem. 1989; 264: 17213-17221Abstract Full Text PDF PubMed Google Scholar). The high molecular weight band shown in the immunoblots (Fig 2) byHerouy et al., 1998Herouy Y. May A.E. Pornschlegel G. et al.Lipodermatosclerosis is characterized by elevated expression and activation of matrix metalloproteinases: implications for venous ulcer formation.J Invest Dermatol. 1998; 111: 822-827Abstract Full Text Full Text PDF PubMed Scopus (113) Google Scholar either are a new type of complex, or represent an artifact of antipeptide antibodies." @default.
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• W1556547170 date "1999-06-01" @default.
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• W1556547170 title "Native Type I Collagen is Not a Substrate for MMP2 (Gelatinase A)" @default.
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• W1556547170 doi "https://doi.org/10.1046/j.1523-1747.1999.00616.x" @default.
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