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PMID: 2430973 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins.

The Journal of cell biology ·Vol. 103 ·No. 5 ·1986-11-00 ·Pages 1635-48

Lawler J, Hynes RO

Abstract

Thrombospondin is one of a class of adhesive glycoproteins that mediate cell-to-cell and cell-to-matrix interactions. We have used two monoclonal antibodies to isolate cDNA clones of thrombospondin from a human endothelial cell cDNA library and have determined the complete nucleotide sequence of the coding region. Three regions of known amino acid sequence of human platelet thrombospondin confirm that the clones are authentic. Three types of repeating amino acid sequence are present in thrombospondin. The first is 57 amino acids long and shows homology with circumsporozoite protein from Plasmodium falciparum. The second is 50-60 amino acids long and shows homology with epidermal growth factor precursor. The third occurs as a continuous eightfold repeat of a 38-residue sequence; structural homology with parvalbumin and calmodulin indicates that these repeats constitute the multiple calcium-binding sites of thrombospondin. The amino acid sequence arg-gly-asp-ala is included in the last type 3 repeat. This sequence is probably the site for the association of thrombospondin with cells. In addition, localized homologies with procollagen, fibronectin, and von Willebrand factor are present in one region of the thrombospondin molecule.

MeSH Terms
Amino Acid Sequence Base Sequence Calcium-Binding Proteins Cell Adhesion Cloning, Molecular DNA/genetics Epitopes Extracellular Matrix/metabolism Glycoproteins Humans Molecular Weight Peptide Fragments Protein Conformation Thrombospondins
Chemicals
Calcium-Binding Proteins Epitopes Glycoproteins Peptide Fragments Thrombospondins DNA
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Lawler J
Hynes R O
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64 references, click to expand
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
Published
1986-11-00
Pages
1635-48
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2114380
Subset
IM
Grants
NCI NIH HHS · CA-26712 · United States
NHLBI NIH HHS · HL-28749 · United States
Databases
GENBANK
X04665
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