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B16 mouse melanoma cells adhere to and spread on laminin. We
have previously shown that cell spreading is uncoupled from adhesion
when unglycosylated laminin is used as a substratum; spreading was
restored by a Pronase digest of laminin which became inactive when it
was specifically depleted of its mannoside peptides; spreading was also
specifically restored by mannosides such as mannan, Man9, and Man6, but
not Man3. The effector mannosides bind to a cell surface receptor,
previously shown by direct and indirect methods. We have now identified
the receptor as cell surface calreticulin by isolating it via mannan
affinity chromatography and showing its sequence identity with mouse
calreticulin. Anti-calreticulin antibodies confirm this identity,
decorate the B16 cell surface, and block cell spreading. Purified B16
cell calreticulin from whole cell lysates successfully competes with
cell surface calreticulin and prevents cell spreading. The composite
data implicate cell surface calreticulin as a putative lectin that must
be occupied to initiate spreading of laminin-adherent B16 cells.
Volume 270,
Number 27,
Issue of July 07, pp. 15926-15929, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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