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Structural characterization of recombinant domain II of the basement membrane proteoglycan perlecan
Author(s) -
Costell Mercedes,
Sasaki Takako,
Mann Karlheinz,
Yamada Yoshihiko,
Timpl Rupert
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)01082-4
Subject(s) - perlecan , proteoglycan , chemistry , glycosylation , proteolysis , basement membrane , tandem repeat , epitope , transfection , microbiology and biotechnology , biochemistry , biology , antibody , genetics , gene , extracellular matrix , genome , enzyme
Mouse perlecan domain II (325 residues), consisting of four cysteine‐rich LA modules, one IG module and a link region, was obtained in purified form from a stably transfected mammalian cell clone. Rotary shadowing electron microscopy demonstrated a globular domain connected to a short rod‐like segment of variable length. This suggested that tandem arrays of LA modules form rod‐like elements. Folding into a native structure was indicated by the sharing of immunological epitopes with tissue perlecan, a CD spectrum demonstrating 37% β structure and a limited susceptibility to proteolysis. The domain also showed N ‐glycosylation of a single acceptor site and 7–8 O ‐linked oligosaccharides. The latter were located mainly in the link region within proline‐rich sequences.