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J. Biol. Chem., Vol. 277, Issue 14, 12182-12189, April 5, 2002
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From the Punctin (ADAMTSL-1) is a secreted
molecule resembling members of the ADAMTS family of proteases. Punctin
lacks the pro-metalloprotease and the disintegrin-like domain typical
of this family but contains other ADAMTS domains in precise order
including four thrombospondin type I repeats. Punctin is the product of
a distinct gene on human chromosome 9p21-22 and mouse chromosome 4 that
is expressed in adult skeletal muscle. His-tagged punctin expressed in
stably transfected High-FiveTM insect cells was
purified to apparent homogeneity by Ni-chromatography of conditioned
medium. The NH2 terminus is not blocked and has the
sequence EEDRD and so forth as determined by Edman degradation, demonstrating signal peptidase processing. Recombinant epitope-tagged punctin has a calculated mass of 59,991 Da but exhibits major molecular
species of 61970 ± 6 Da and 62131 ± 5 Da as measured by
liquid chromatography electrospray mass spectrometry. Punctin is
a glycoprotein based on carbohydrate staining and liquid chromatography electrospray mass spectrometry glycopeptide analysis. Glycosylation occurs at a single N-linked site as demonstrated by altered
electrophoretic migration of punctin expressed in the presence of
tunicamycin A. Punctin contains disulfide bonds based on antibody
accessibility and electrophoretic migration under reducing
versus nonreducing conditions. Rotary shadowing
demonstrates that punctin is hatchet-shaped having a globular region
attached to a short stem. In transfected COS-1 cells, punctin is
deposited in the cell substratum in a punctate fashion and is excluded
from focal contacts. Punctin is the first member of a novel family of
ADAMTS-like proteins that may have important functions in the
extracellular matrix.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF176313.
Punctin, a Novel ADAMTS-like Molecule, ADAMTSL-1, in
Extracellular Matrix*
§,§,
,§§
Department of Biomedical Engineering, Lerner
Research Institute, the Department of
Orthopaedic Surgery, Cleveland Clinic Foundation, the ¶ Department
of Ophthalmic Research, Cole Eye Institute, Cleveland Clinic
Foundation, Cleveland, Ohio 44195, the Rowe Program in Genetics,
Departments of Biological Chemistry and Medicine, University of
California at Davis, Davis, California 956161, and the
** Shriner's Hospital for Children, Portland, Oregon
97201
*
This work was supported in part by the Cleveland Clinic
Foundation (to S. S. A.), a Yamanouchi USA Foundation Award (to
S. S. A.), and National Institutes of Health Grants EY06603 (to
J. W. C.) and HGO0734 (to M. F. S.).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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