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(Received for publication, October 25, 1996, and in revised form, January 10, 1997)
From the Myeloid-related protein (MRP) 8 and MRP14, two
members of the S100 family expressed in myelomonocytic cells, have been
ascribed some extracellular functions, e.g.
antimicrobial, cytostatic, and chemotactic activities. Since S100
proteins lack structural requirements for secretion via the classical
endoplasmic reticulum/Golgi route, the process of secretion is unclear.
We now demonstrate the specific, energy-dependent release
of MRP8 and MRP14 by human monocytes after activation of protein kinase
C. This secretory process is not blocked by inhibitors of vesicular
traffic through the endoplasmic reticulum and Golgi, and comparative
studies on tumor necrosis factor-
Volume 272, Number 14,
Issue of April 4, 1997
pp. 9496-9502
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,§
,
,
,
and
Institute of Experimental Dermatology and
§ Department of Pediatrics, University of Münster,
48129 Münster, Germany and 
Department of Dermatology,
University of Würzburg, 97080 Würzburg, Germany
and interleukin-1
indicate that
MRP8 and MRP14 follow neither the classical nor the
interleukin-1-like alternative route of secretion. Inhibition
by microtubule-depolymerizing agents revealed that MRP8/MRP14 secretion
requires an intact tubulin network. Accordingly, upon initiation of
MRP8/MRP14 secretion, immunofluorescence microscopy showed a
co-localization of both proteins with tubulin filaments. Release of
MRP8 and MRP14 is associated with down-regulation of their de
novo synthesis, suggesting that extracellular signaling via
MRP8/MRP14 is restricted to distinct differentiation stages of
monocytes. Our data provide evidence that the S100 proteins MRP8 and
MRP14 are secreted after activation of protein kinase C via a novel
pathway requiring an intact microtubule network.
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