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J. Biol. Chem., Vol. 276, Issue 30, 28233-28241, July 27, 2001
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From the Serine proteases are implicated in a
variety of processes during neurogenesis, including cell migration,
axon outgrowth, and synapse elimination. Tissue-type plasminogen
activator and urokinase-type activator are expressed in the floor plate
during embryonic development. F-spondin, a gene also expressed in the
floor plate, encodes a secreted, extracellular matrix-attached protein
that promotes outgrowth of commissural axons and inhibits outgrowth of
motor axons. F-spondin is processed in vivo to yield an
amino half protein that contains regions of homology to reelin and
mindin, and a carboxyl half protein that contains either six or four
thrombospondin type I repeats (TSRs). We have tested F-spondin to see
whether it is subjected to processing by plasmin and to determine
whether the processing modulates its biological activity. Plasmin
cleaves F-spondin at its carboxyl terminus. By using nested deletion
proteins and mutating potential plasmin cleavage sites, we have
identified two cleavage sites, the first between the fifth and sixth
TSRs, and the second at the fifth TSR. Analysis of the
extracellular matrix (ECM) attachment properties of the TSRs revealed
that the fifth and sixth TSRs bind to the ECM, but repeats 1-4 do not. Structural functional experiments revealed that two basic motives are
required to elicit binding of TSR module to the ECM. We demonstrate further that plasmin releases the ECM-bound F-spondin protein.
Plasmin-mediated Release of the Guidance Molecule F-spondin from
the Extracellular Matrix*
§,,
,
Department of Anatomy and Cell Biology,
Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel, the ¶ Institut de Recerca Oncologica, Centre d'Oncologia
Molecular, L'Hospitalet de Llobregat, Barcelona 08907, Spain the
Department of Oncology, Hadassah-Hebrew University Hospital,
Jerusalem 91120, Israel, and the ** Department of Animal and Plant Cell
Biology, Faculty of Biology, University of Barcelona,
Barcelona 08028, Spain
*
This work was supported by grants from the Israel United
States of America Binational Foundation, the Israel Science Foundation, the Human Frontier Science Foundation (to A. K.), and a grant from the
Fundacio La Marató-TV3 (to P. M. C).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.
To whom correspondence should be addressed: Hebrew
University-Hadassah Medical School, P. O. Box 12272, Jerusalem 91120, Israel. Tel.: 972-2-675-7133; Fax: 972-2-675-7451; E-mail:
avihu@cc.huji.ac.il.
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