Popovic, et al. (1), find that cathepsin L is capable of truncating cystatin C which they state has a much lower affinity for cysteine proteinases than the intact inhibitor. Might this occur in the Cer mutant and could that then result in increased cathepsin S which Munger and associates (2) report may generate Abeta from amyloidogenic fragments of beta APP? It would seem of interest that cathepsin S activity is upregulated by IFNgamma (3). I wonder whether the study by Hucke et al (2) finding that NO may reduce the protein content of indoleamine 2,3-dioxygenase and hence bacteriostasis, may explain the positive reports with the use of antibiotics? Is anyone trialling minocycline therapy in AD? Furthermore, may the fact that interferon gamma induces iNOS expression be reason to expect that Meiogen's anti-interferon may be useful?
References:
Popovic T, Cimerman N, Dolenc I, Ritonja A, Brzin J.
Cathepsin L is capable of truncating cystatin C of 11 N-terminal amino acids.
FEBS Lett. 1999 Jul 16;455(1-2):92-6.
PubMed.
Munger JS, Haass C, Lemere CA, Shi GP, Wong WS, Teplow DB, Selkoe DJ, Chapman HA.
Lysosomal processing of amyloid precursor protein to A beta peptides: a distinct role for cathepsin S.
Biochem J. 1995 Oct 1;311 ( Pt 1):299-305.
PubMed.
Storm van's Gravesande K, Layne MD, Ye Q, Le L, Baron RM, Perrella MA, Santambrogio L, Silverman ES, Riese RJ.
IFN regulatory factor-1 regulates IFN-gamma-dependent cathepsin S expression.
J Immunol. 2002 May 1;168(9):4488-94.
PubMed.
Hucke C, Mackenzie CR, Adjogble KD, Takikawa O, Däubener W.
Nitric oxide-mediated regulation of gamma interferon-induced bacteriostasis: inhibition and degradation of human indoleamine 2,3-dioxygenase.
Infect Immun. 2004 May;72(5):2723-30.
PubMed.
Comments
Popovic, et al. (1), find that cathepsin L is capable of truncating cystatin C which they state has a much lower affinity for cysteine proteinases than the intact inhibitor. Might this occur in the Cer mutant and could that then result in increased cathepsin S which Munger and associates (2) report may generate Abeta from amyloidogenic fragments of beta APP? It would seem of interest that cathepsin S activity is upregulated by IFNgamma (3). I wonder whether the study by Hucke et al (2) finding that NO may reduce the protein content of indoleamine 2,3-dioxygenase and hence bacteriostasis, may explain the positive reports with the use of antibiotics? Is anyone trialling minocycline therapy in AD? Furthermore, may the fact that interferon gamma induces iNOS expression be reason to expect that Meiogen's anti-interferon may be useful?
References:
Popovic T, Cimerman N, Dolenc I, Ritonja A, Brzin J. Cathepsin L is capable of truncating cystatin C of 11 N-terminal amino acids. FEBS Lett. 1999 Jul 16;455(1-2):92-6. PubMed.
Munger JS, Haass C, Lemere CA, Shi GP, Wong WS, Teplow DB, Selkoe DJ, Chapman HA. Lysosomal processing of amyloid precursor protein to A beta peptides: a distinct role for cathepsin S. Biochem J. 1995 Oct 1;311 ( Pt 1):299-305. PubMed.
Storm van's Gravesande K, Layne MD, Ye Q, Le L, Baron RM, Perrella MA, Santambrogio L, Silverman ES, Riese RJ. IFN regulatory factor-1 regulates IFN-gamma-dependent cathepsin S expression. J Immunol. 2002 May 1;168(9):4488-94. PubMed.
Hucke C, Mackenzie CR, Adjogble KD, Takikawa O, Däubener W. Nitric oxide-mediated regulation of gamma interferon-induced bacteriostasis: inhibition and degradation of human indoleamine 2,3-dioxygenase. Infect Immun. 2004 May;72(5):2723-30. PubMed.
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