Zobrazeno 1 - 10
of 25
pro vyhledávání: '"A. C. Hanglow"'
Publikováno v:
Biochemical and Biophysical Research Communications. 205:1156-1163
The tissue inhibitors of metalloproteinases (TIMPs) represent a family of naturally occurring protein inhibitors of stromelysin and other members of the family of matrix metalloproteinases. A series of peptides based on the N-terminal sequence of nat
Publikováno v:
Journal of Biological Chemistry. 269:30227-30231
Stromelysin is secreted as an inactive zymogen that is activated in the extracellular space by cleavage of the His81-Phe82 bond with the release of the 81-amino acid propeptide domain. This segment contains a 12-amino acid sequence (MRKPRC75GVPDVG) t
Publikováno v:
Agents and Actions. 34:11-15
After 72 hrs in culture, unseparated spleen cells from rats with adjuvant-induced arthritis (AA) stimulated with high concentrations of Con A (greater than 0.63 micrograms/ml) leaked more lactate dehydrogenase (LDH) than did either unstimulated cultu
Publikováno v:
International Journal of Immunopharmacology. 12:703-712
Proliferative responses to the T-cell mitogen, Con A, were markedly suppressed in spleen cells isolated from rats 12-16 days following induction of adjuvant-induced arthritis (AA). These responses were only partially restored following removal of pla
Publikováno v:
Agents and Actions. 34:81-83
The effect of adjuvant-induced arthritis on rat peritoneal macrophage (RPM) function with respect to [14C]arachidonic acid (AA) release, leukotriene B4 (LTB4) and prostaglandin E2 (PGE2) production, and secreted phospholipase A2 (PLA2) activity was i
Publikováno v:
Inflammation research : official journal of the European Histamine Research Society ... [et al.]. 44
Publikováno v:
Inflammation research : official journal of the European Histamine Research Society ... [et al.]. 44
Publikováno v:
The Journal of biological chemistry. 269(48)
Stromelysin is secreted as an inactive zymogen that is activated in the extracellular space by cleavage of the His81-Phe82 bond with the release of the 81-amino acid propeptide domain. This segment contains a 12-amino acid sequence (MRKPRC75GVPDVG) t
Publikováno v:
Agents and actions.
Accurate kinetic characterization of stromelysin (MMP-3) inhibitors is critical in the design of potent inhibitors of this enzyme. We have successfully modified a previously described assay [1] which used an internally quenched peptide substrate (Dnp
Autor:
N. Fotouhi, Robert L. Walsky, A. Lugo, A. C. Hanglow, M. B. Finch-Arietta, L. Lusch, M. Visnick
Publikováno v:
Agents and actions.
Prostromelysin, a member of the family of matrix metalloproteinases, is secreted as a zymogen which is activated after cleavage of the His81-Phe82 bond. The 82 amino acid propeptide that is removed during activation contains 12 amino acids, MRKPRC75G