• Publications
  • Influence
Matrix metalloproteinases and their inhibitors in connective tissue remodeling
  • J. Woessner
  • Biology, Medicine
  • FASEB journal : official publication of the…
  • 1 May 1991
TLDR
Latency is overcome by physical, chemical, and enzymatic treatments that separate the cysteine residue from the zinc Expression of the metalloproteinases is switched on by a variety of agents acting through regulatory elements of the gene, particularly the AP‐1 binding site. Expand
Handbook of proteolytic enzymes
(Abbreviated Contents Including Section Headings:) Serine Peptidases. Serine Peptidases and Their Clans. Family S1 of Trypsin (Clan SA). Tissue Kallikrein and Its Relatives. Other Families of ClanExpand
Matrix metalloproteinases and TIMPs
ABBREVIATIONS INTRODUCTION MMP SEQUENCES TIMP SEQUENCES THREE DIMENSIONAL STRUCTURES OF THE MMPS AND TIMPS ACTIVATION OF THE ZYMOGEN FORMS OF MMPS PROTEIN SUBSTRATES OF THE MMPS SPECIFICITYExpand
CD44 anchors the assembly of matrilysin/MMP-7 with heparin-binding epidermal growth factor precursor and ErbB4 and regulates female reproductive organ remodeling.
TLDR
It is demonstrated that CD44 heparan sulfate proteoglycan recruits proteolytically active matrix metalloproteinase 7 (matrilysin, MMP-7) and heparin-binding epidermal growth factor precursor (pro-HB-EGF) to form a complex on the surface of tumor cell lines, postpartum uterine and lactating mammary gland epithelium, and uterine smooth muscle. Expand
TIMP-3 Binds to Sulfated Glycosaminoglycans of the Extracellular Matrix*
TLDR
The present results show that glycosaminoglycans such as heparin, heparan sulfate, chondroitin sulfates A, B, and C, and sulfated compounds such as suramin and pentosan efficiently extract TIMP-3 from the postpartum rat uterus. Expand
The family of matrix metalloproteinases.
  • J. Woessner
  • Medicine
  • Annals of the New York Academy of Sciences
  • 1994
Evidence for metalloproteinase and metalloproteinase inhibitor imbalance in human osteoarthritic cartilage.
TLDR
Titration of TIMP against the two metalloproteinases indicates that there is a small excess of inhibitor over enzymes in normal cartilage; in OA, TIMP does not increase to the same extent as the proteinases; the resultant excess of proteinases over TIMP may contribute to cartilage breakdown. Expand
Heparan Sulfate Proteoglycans as Extracellular Docking Molecules for Matrilysin (Matrix Metalloproteinase 7)*
TLDR
Dislodging MMPs by treatment with compounds such as heparin might be beneficial in attenuating excessive tissue breakdown such as occurs in cancer metastasis, arthritis, and angiogenesis. Expand
Matrix Metalloproteinase Inhibition: From The Jurassic To The Third Millennium
  • J. Woessner
  • Chemistry, Medicine
  • Annals of the New York Academy of Sciences
  • 1 June 1999
TLDR
An overview of the inhibition of these proteases by natural inhibitors such as α2 macroglobulin and the TIMPs and by synthetic inhibitors, which are largely chelating agents. Expand
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