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Characterization of zinc‐α 2 ‐glycoprotein as a cell adhesion molecule that inhibits the proliferation of an oral tumor cell line
Author(s) -
Lei Gang,
Brysk Henry,
Arany Istvan,
Tyring Stephen K.,
Srinivasan Ganesan,
Brysk Miriam M.
Publication year - 1999
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(19991001)75:1<160::aid-jcb16>3.0.co;2-b
Subject(s) - fibronectin , laminin , vitronectin , microbiology and biotechnology , integrin , cell culture , extracellular matrix , chemistry , cell adhesion , biology , cell growth , cell , biochemistry , genetics
Zn‐α 2 ‐glycoprotein (Znα 2 gp) is a soluble protein widely distributed in body fluids and glandular epithelia. We have found it to be expressed in stratified epithelia as well. Znα 2 gp is clinically correlated with differentiation in various epithelial tumors, including oral and epidermal tumors. We have cloned epidermal Znα 2 gp and report the preparation of the recombinant protein in a Baculovirus expression system. Like the native molecule, recombinant Znα 2 gp has RNase activity. Znα 2 gp functions as a matrix protein for the Tu‐138 oral squamous cell carcinoma cell line. Cell attachment to Znα 2 gp is comparable to that for fibronectin and is inhibited by the synthetic RGD peptides RGD, RGDV, and RGDS. Attachment is also inhibited by the antibody to integrin α 5 β 1 (the fibronectin receptor), but not by antibodies to integrins α v β 3 , α 3 β 1 , and α 2 β 1 . We find that the proliferation of Tu‐138 cells is inhibited on a Znα 2 gp matrix, as compared with other matrix proteins (fibronectin, vitronectin, laminin, and collagens I and IV) on which growth resembles that on the BSA control. We believe that the role of Znα 2 gp in differentiation and its RNase activity are two likely suspects as agents of the inhibition of proliferation. J. Cell. Biochem. 75:160–169, 1999. © 1999 Wiley‐Liss, Inc.