TY - JOUR
T1 - Muscle is the major source of plasma gelsolin
AU - Kwiatkowski, D. J.
AU - Mehl, R.
AU - Izumo, S.
AU - Nadal-Ginard, B.
AU - Yin, H. L.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1988
Y1 - 1988
N2 - Gelsolin, a Ca2+- and polyphosphoinositide-regulated actin-binding protein, is unique among vertebrate proteins in being both cytoplasmic and secreted. Plasma gelsolin, present at > 200 μg/ml in human plasma, may have a protective function by promoting the clearance of actin filaments released during tissue injury. Although there is evidence that smooth muscle tissues and HepG2 cells synthesize plasma gelsolin, the predominant secretory source is hitherto unknown. We report here that skeletal, cardiac, and smooth muscles have large amounts of plasma gelsolin mRNA and devote 0.5-3% of their biosynthetic activity to plasma gelsolin, whereas liver makes relatively little. Since skeletal muscle accounts for a large fraction of body mass and total protein synthesis, it is the major source of plasma gelsolin.
AB - Gelsolin, a Ca2+- and polyphosphoinositide-regulated actin-binding protein, is unique among vertebrate proteins in being both cytoplasmic and secreted. Plasma gelsolin, present at > 200 μg/ml in human plasma, may have a protective function by promoting the clearance of actin filaments released during tissue injury. Although there is evidence that smooth muscle tissues and HepG2 cells synthesize plasma gelsolin, the predominant secretory source is hitherto unknown. We report here that skeletal, cardiac, and smooth muscles have large amounts of plasma gelsolin mRNA and devote 0.5-3% of their biosynthetic activity to plasma gelsolin, whereas liver makes relatively little. Since skeletal muscle accounts for a large fraction of body mass and total protein synthesis, it is the major source of plasma gelsolin.
UR - http://www.scopus.com/inward/record.url?scp=0023899912&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0023899912&partnerID=8YFLogxK
M3 - Article
C2 - 2836420
AN - SCOPUS:0023899912
SN - 0021-9258
VL - 263
SP - 8239
EP - 8243
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 17
ER -