could Salix alba slow fly aging?

X-Message-Number: 24576
Date: Wed, 1 Sep 2004 05:23:21 -0700 (PDT)
From: Doug Skrecky <>
Subject: could Salix alba slow fly aging?

[Only one real way to find out...]

Ann N Y Acad Sci. 2004 Jun;1019:223-7.
Heat shock protein 47 expression in aged normal human fibroblasts:
modulation by Salix alba extract.
  Heat shock protein (HSP) 47 is a specific chaperone of procollagen. This
heat shock protein is responsible for the correct three-dimensional
organization of procollagen and its control-quality prior secretion. The
aim of the study is to evaluate the level of HSP 47 in aged, photoaged,
and senescent fibroblasts and its modulation by a plant extract (Salix
alba). The level of HSP 47 and/or procollagen expression in fibroblasts
was measured by real-time RT-PCR (mRNA transcripts) and by flow cytometry
(immunochemistry technique for measurement of arbitrary fluorescence
intensity). Immunochemistry techniques and confocal microscopy were used
to visualize the cellular localization of HSP 47 and procollagen. These
parameters were compared with different age donors, nonsenescent, and
senescent fibroblasts. Fibroblasts were irradiated by a noncytotoxic dose
of UVA (6 J/cm(2)), and HSP 47 level was evaluated. S. alba extract was
tested for its capacity to modulate HSP 47 expression. Colocalization of
HSP 47 and procollagen was shown by confocal microscopy, indicating that
HSP 47 could play a role of procollagen molecular chaperone in the
cellular model. It was also shown that the HSP 47 level is decreased in
old-donor cells, senescent, and irradiated cells. This decrease can be
modulated by a S. alba extract (polyphenols rich) in a dose-dependent
manner. The evaluation of HSP 47 expression in the experimental
conditions can lead to a new approach of aging and photoaging, pointing
out the implication of this chaperone in these pathophysiologic
phenomena. Modulation of HSP 47 expression by this family of molecules
could be of cosmetic and/or dermatologic interest

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