TMC-52A to D, novel cysteine proteinase inhibitors, produced by Gliocladium sp.

  title={TMC-52A to D, novel cysteine proteinase inhibitors, produced by Gliocladium sp.},
  author={Kengo Isshiki and Maki Nishio and Naoki Sakurai and Tomofumi Uchida and T{\^o}ru Okuda and Saburo Komatsubara},
  journal={The Journal of antibiotics},
  volume={51 7},
New cysteine proteinase inhibitors, TMC-52A, B, C, and D, were isolated from the fungal fermentation broth. On the basis of a taxonomical study, the producing strain, F-2665, was characterized as Gliocladium sp. Spectroscopic analyses and chemical degradation have shown TMC-52A to D to be epoxysuccinyl peptides. TMC-52A to D strongly inhibited cysteine proteinases, in particular, cathepsin L with IC50 values of 13 nM, 10nM, 10nM, and 6nM, respectively. 
TMC-171A,B,C and TMC-154, novel polyketide antibiotics produced by Gliocladium sp. TC 1304 and TC 1282.
Four new antibiotics have been isolated from the fermentation of fungal strains Gliocladium sp.
WF14861, a new cathepsins B and L inhibitor produced by Colletotrichum sp. II. Biological properties.
The compound ameliorated the tissue damage and the bone destruction models of low-calcium-diet-fed mouse and adjuvant arthritis rat model and showed inhibitory activities against bone derived crude protease and other cysteine proteases in vitro.
Aurantiamide Acetate, a Selective Cathepsin Inhibitor, Produced by Aspergillus penicilloides
Aurantiamide acetate was isolated from the fermentation broth of Aspergillus penicilloides for the first time and in the adjuvant-arthritic rat model, subcutaneously administered 10 mg/kg body weight of this compound suppressed hind paw swelling.
(2S,3S)-Oxirane-2,3-dicarboxylic acid: a privileged platform for probing human cysteine cathepsins.
To investigate these particular fraction of proteolytical activity of the human degradome even in a complex cellular environment, chemical probes that covalently label the corresponding proteases proved to be versatile tools.
Biological Activities of Fungal Metabolites
The amazing range of chemical structures observed for fungal metabolites is derived from a relatively small number of basic metabolic pathways, plus combinations of these, which have become extremely diversified during the course of evolution.
International Journal of Current Research in
This review is a comprehensive survey of unique, unusual, and rare fatty acids incorporated into natural marine and terrestrial peptides obtained from fungi, fungal endophytes, lichenized
6. Cathepsin K inhibitors: their potential as anti-osteoporosis agents.
Early human data supports a promising future for this therapeutic class of osteoporosis drugs, and multiple cycles of design, synthesis, structure elucidation, and drug property profiling have proved fruitful.


Isolation and characterization of new thiol protease inhibitors estatins A and B.
New thiol protease inhibitors, estatins A and B, were isolated from the culture filtrate of Myceliophthora thermophila M4323 and suppressed IgE antibody production in mice, but not IgG.
Cathestatins, new cysteine protease inhibitors produced by Penicillium citrinum.
New cysteine protease inhibitors, named cathestatin A and B, have been discovered as metabolites of Penicillium citrinum, which suppressed parathyroid hormone (PTH)-stimulated 45Ca release in organ cultures of chick embryonic calvaria.
Engineering the S2 subsite specificity of human cathepsin S to a cathepsin L- and cathepsin B-like specificity.
The primary specificity of papain-like proteinases is largely determined by S2-P2 site interactions, and the activities of the Phe-205-->Glu single and the Gly-133-->Ala/Phen-205 -->Glu double mutants of cathepsin S toward the dibasic substrate is modulated by an additional ionizable group.
Studies on the optimum pH for the action of pepsin on "native" and denatured bovine serum albumin and bovine hemoglobin.
It is suggested that native as well aa denatured proteins can serve as protease substrates, a view also held by Chernikov and Green and Neurath.
Participation of cathepsin L on bone resorption
It is suggested that cathepsin L is the main proteinase responsible for bone collagen degradation in osteo‐resorption and Serum calcium in rats placed on a low calcium diet was decreased by treatment of E‐64 or cystatin A, but not by CA‐074.
A Dictionary of the Fungi
A Dictionary of the FungiBy Dr. G. C. Ainsworth Dr. G. R. Bisby. Pp. viii + 360. (Kew: Imperial Mycological Institute, 1943.) 20s.
MIIKE (Meiji Seika Kaisha, LTD.): Production of PF1126A and B
  • JPK
  • 1995
PEGLER: Dictionary of the fungi
  • Eighth edition.,
  • 1995
KIRSCHKE: Cathepsin B, cathepsin H, and cathepsin L. Methods Enzymol
  • 1985
Cathepsin B, Cathepsin H, and cathepsin L.