An essential role for ectodomain shedding in mammalian development

Science

Volumn 282, Issue 5392, 1998, Pages 1281-1284

  Peschon, Jacques J ^a   Slack, Jennifer L ^a   Reddy, Pranitha ^a   Stocking, Kim L ^a   Sunnarborg, Susan W ^b   Lee, David C ^b   Russell, William E ^c   Castner, Beverly J ^a   Johnson, Richard S ^a   Fitzner, Jeffrey N ^a   Boyce, Rogely W ^d   Nelson, Nicole ^a   Kozlosky, Carl J ^a   Wolfson, Martin F ^a   Rauch, Charles T ^a   Cerretti, Douglas Pat ^a   Paxton, Raymond J ^a   March, Carl J ^a   Black, Roy A ^a  

^a AMGEN INC   (United States)

^b UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^c VANDERBILT UNIVERSITY   (United States)

^d CHARLES RIVER LABORATORIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE PROTEIN; DIPEPTIDYL CARBOXYPEPTIDASE; DISINTEGRIN; METALLOPROTEIN; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR;

ANIMAL TISSUE; ARTICLE; GENE MUTATION; LETHALITY; MOUSE; NONHUMAN; PHYSICAL DEVELOPMENT; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN SECRETION;

EID: 0032515018     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.282.5392.1281     Document Type: Article

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51. Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
52. Peptides were either synthesized at Immunex (TNF, L-selectin) or obtained commercially (TGFα; Syn-Pep). The enzyme used for the digests was a catalytic domain-polyHis construct expressed in Chinese hamster ovary cells and purified with Ni-nitrilotriacetic acid (Qiagen) and gel filtration columns (27). About 7 μM and 1.4 μM TACE was used for the L-selectin and TGFα peptides, respectively. All the incubations were with 0.5 mM peptide in 20 μl and were done for 0.5, 1, 2, and 4 hours at 37°C in 10mM tris (pH 7.5). Digestion was a linear function of time in all cases, and the comparative data are based on the rates of the reactions. High-performance liquid chromatography (HPLC) analysis of products was done as described [R. A. Black et al., Biochem. Biophys. Res. Commun. 225, 400 (1996]. The composition of the digests was determined by liquid chromatography/mass spectrometry (LC/MS), on a 1-mm ID Vydac C18 column with a flow rate of 50 μl/min and a linear gradient of 2% acetonitrile/min in 0.1% trifluoroacetate. LC/MS data were obtained by directing 10% of the HPLC effluent to the electrospray source of a Finnigan TSQ700 triple quadrupole mass spectrometer (San Jose, CA).
53. We thank the Immunex Animal Facility, the Flow Cytometry and Histology groups, K. Brasel, C. Willis, M. Glaccum, D. Barone, R. Blanton, K. Mohler, J. Schuh, and J. Doedens for their contributions to this work; H. Nagase of the University of Kansas Medical Center for providing MMP-3; M. Hall and G. Carlton for graphic assistance; and A. Aumell for help with manuscript preparation. Supported in part by NIH grants CA43793 (D.C.L.) and DK53804 (W.E.R.), and NSF grant MCB9729645 (W.E.R.).