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PMID: 2430295 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

cDNA and amino acid sequences of the cell adhesion protein receptor recognizing vitronectin reveal a transmembrane domain and homologies with other adhesion protein receptors.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 83 ·No. 22 ·1986-11-00 ·Pages 8614-8

Suzuki S, Argraves WS, Pytela R, Arai H, Krusius T, Pierschbacher MD, Ruoslahti E

Abstract

Cells adhere to vitronectin substrates through a cell surface receptor that recognizes an Arg-Gly-Asp sequence in vitronectin. The receptor is a glycoprotein composed of a 150-kDa alpha and a 115-kDa beta subunit. The alpha subunit consists of two disulfide-bonded chains of 125 kDa and 25 kDa. cDNA clones were isolated for the alpha subunit of the vitronectin receptor from a phage lambda gt11 expression library made with RNA from a human fibroblast cell line, IMR-90. The identity of the clones that had been selected from the library based on immunological criteria was verified by comparison of DNA and protein sequences. NH2-terminal sequences were obtained for each of the alpha-subunit chains. The sequence of the 25-kDa chain of the alpha subunit was found in a cDNA clone, and the amino acid sequence deduced from the cDNA establishes the complete amino acid sequence of the 25-kDa chain. This chain contains a membrane-spanning domain as well as a putative intracytoplasmic region that is 32 amino acids long and consists mostly of polar amino acids. Comparison of the cDNA and protein sequences shows that the 25-kDa chain is generated by proteolytic cleavage of an alpha-subunit precursor, the partial sequence of which is contained in the cDNA clones. These clones contain 1910 base pairs of open reading frame and a 3' untranslated sequence. RNA blot hybridization detected one transcript of about 7 kilobases in RNA from fibroblastic and epithelial cells. Together, the cDNA clones cover 4442 bases of this RNA. The alpha-subunit sequence showed strong homology with the sequence of the alpha subunit of fibronectin receptor. Moreover, the NH2-terminal protein sequence of the 125-kDa chain was homologous with the NH2-terminal sequences of two other cell surface proteins, lymphocyte function-associated antigen 1 (LFA-1) and macrophage antigen 1 (Mac-1), which have been implicated as receptors for adhesion proteins of leukocytes. These results establish several of the structural features in the vitronectin receptor and suggest the existence of a superfamily of receptors for cell adhesion proteins.

MeSH Terms
Amino Acid Sequence Antigens, Surface/analysis,metabolism Base Sequence Cell Adhesion Molecules DNA/analysis Lymphocyte Function-Associated Antigen-1 Macrophage-1 Antigen Platelet Membrane Glycoproteins/analysis RNA, Messenger/analysis Receptors, Fibronectin Receptors, Immunologic/analysis,genetics Receptors, Vitronectin
Chemicals
Antigens, Surface Cell Adhesion Molecules Lymphocyte Function-Associated Antigen-1 Macrophage-1 Antigen Platelet Membrane Glycoproteins RNA, Messenger Receptors, Fibronectin Receptors, Immunologic Receptors, Vitronectin DNA
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Suzuki S
Argraves W S
Pytela R
Arai H
Krusius T
Pierschbacher M D
Ruoslahti E
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.83.22.8614
Published
1986-11-00
Pages
8614-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC386981
Subset
IM
Grants
NCI NIH HHS · CA 28896 · United States
NCI NIH HHS · CA 30199 · United States
NCI NIH HHS · CA 38352 · United States
Databases
GENBANK
J02826, M14648, M18365
External Links
PubMed source DOI: 10.1073/pnas.83.22.8614 PMC Full Text View journal details
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