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J. Biol. Chem., Vol. 277, Issue 50, 48066-48075, December 13, 2002
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From the Human adipose tissue expresses all components
necessary for the local production of angiotensin II, which has
multiple functions in adipose tissue, ranging from regulation of local
blood flow to complex influences on tissue homeostasis. Still the
mechanisms controlling human adipose tissue angiotensin II
concentrations are not yet known. We investigated whether angiotensin
II is degraded by human primary cultured preadipocytes and adipocytes
and which enzymes are responsible for its metabolism. Distinct but
transient angiotensin II production was limited by degradation due to
consecutive proteolytic cleavage by endopeptidase and
aminopeptidase activities. The endopeptidase could be identified
as neprilysin expressed on the surface of both preadipocytes and
adipocytes. Degradation of angiotensin II was preceded by a lag phase
that was considerably longer in preadipocytes. This time span could not
be explained by an induction of neprilysin nor by an increase in its
surface localization. Following the lag phase, adipocytes showed a
higher degradation activity than preadipocytes as mirrored by increased neprilysin levels and activity measured in their membrane fractions. Our findings demonstrate that human preadipocytes and adipocytes differentially express functional neprilysin and aminopeptidase activity involved in the regulation of angiotensin II concentrations in
human adipose tissue.
Human Adipose Tissue Cells Keep Tight Control on the
Angiotensin II Levels in Their Vicinity*
§¶ and
Institute for Clinical Chemistry and
Laboratory Medicine, University of Regensburg,
Franz-Josef-Strauß-Allee 11, 93053 Regensburg and
Biochemie-Zentrum (BZH), University of Heidelberg, Im
Neuenheimer Feld 328, 69120 Heidelberg, Germany
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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