Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death

Naus S, Richter M, Wildeboer D, Moss M, Schachner M, Bartsch JW (2004)
JOURNAL OF BIOLOGICAL CHEMISTRY 279(16): 16083-16090.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
The neural cell adhesion molecule "close homologue of L1," termed CHL1, has functional importance in the nervous system. CHL1 is expressed as a transmembrane protein of 185 kDa, and ectodomain shedding releases soluble fragments relevant for its physiological function. Here we describe that ADAM8, a member of the family of metalloprotease disintegrins cleaves a CHL1-Fc fusion protein in vitro at two sites corresponding to release of the extracellular domain of CHL1 in fibronectin (FN) domains II ( 125 kDa) and V ( 165 kDa), inhibited by batimastat (BB-94). Cleavage of CHL1-Fc in the 125-kDa fragment was not detectable under nonreducing conditions arguing that cleavage resulting in the 165-kDa fragment is more relevant in releasing soluble CHL1 in vivo. In cells transfected with full-length ADAM8, membrane proximal cleavage of CHL1 was similar and not stimulated by phorbol ester 12-O-tetradecanoylphorbol-13-acetate and pervanadate. No cleavage of CHL1 was observed in cells expressing either inactive ADAM8 with a Glu(330) to Gln exchange (EQ-A8), or active ADAM10 and ADAM17. Consequently, processing of CHL1 was hardly detectable in brain extracts of ADAM8-deficient mice but enhanced in a neurodegenerative mouse mutant. CHL1 processed by ADAM8 in supernatants of COS-7 cells and in co-culture with cerebellar granule neurons was very potent in stimulating neurite outgrowth and suppressing neuronal cell death, not observed in cells co-transfected with CHL1/EQ-A8, CHL1/ ADAM10, or CHL1/ ADAM17. Taken together, we propose that ADAM8 plays an important role in physiological and pathological cell interactions by a specific release of functional CHL1 from the cell surface.
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Zeitschriftentitel
JOURNAL OF BIOLOGICAL CHEMISTRY
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279
Zeitschriftennummer
16
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16083-16090
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Naus S, Richter M, Wildeboer D, Moss M, Schachner M, Bartsch JW. Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death. JOURNAL OF BIOLOGICAL CHEMISTRY. 2004;279(16):16083-16090.
Naus, S., Richter, M., Wildeboer, D., Moss, M., Schachner, M., & Bartsch, J. W. (2004). Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death. JOURNAL OF BIOLOGICAL CHEMISTRY, 279(16), 16083-16090. doi:10.1074/jbc.M400560200
Naus, S., Richter, M., Wildeboer, D., Moss, M., Schachner, M., and Bartsch, J. W. (2004). Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death. JOURNAL OF BIOLOGICAL CHEMISTRY 279, 16083-16090.
Naus, S., et al., 2004. Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death. JOURNAL OF BIOLOGICAL CHEMISTRY, 279(16), p 16083-16090.
S. Naus, et al., “Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death”, JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 279, 2004, pp. 16083-16090.
Naus, S., Richter, M., Wildeboer, D., Moss, M., Schachner, M., Bartsch, J.W.: Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death. JOURNAL OF BIOLOGICAL CHEMISTRY. 279, 16083-16090 (2004).
Naus, S, Richter, M, Wildeboer, D, Moss, M, Schachner, M, and Bartsch, JW. “Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death”. JOURNAL OF BIOLOGICAL CHEMISTRY 279.16 (2004): 16083-16090.

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