The primary structure of the VLA-2/collagen receptor α2 subunit (platelet gpIa): Homology to other integrins and the presence of a possible collagen-binding domain

Y. Takada, M. E. Hemler

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238 Citations (Scopus)

Abstract

VLA-2 (also called gpIa/IIa on platelets) is a collagen receptor with a unique α subunit and a β subunit common to other adhesion receptors in the VLA/integrin family. Multiple cDNA clones for the human VLA-2 α2 subunit have been selected from a λgtll library by specific antibody screening. The 5,374-bp nucleotide sequence encoded for 1,181 amino acids, including a signal peptide of 29 amino acids followed by a long extracellular domain (1,103 amino acids), a transmembrane domain, and a short cytoplasmic segment (22 amino acids). Direct sequencing of purified α2 protein confirmed the identity of the 15 NH2-terminal amino acids. Overall, the α2 amino acid sequence was 18-25% similar to the sequences known for other integrin α subunits. In particular, the α2 sequence matched other integrin α chains in (a) the positions of 17 of its 20 cysteine residues; (b) the presence of three metal-binding domains of the general structure DXDXDGXXD; and (c) the transmembrane domain sequence. In addition, the α2 sequence has a 191-amino acid insert (called the I-domain), previously found only in leukocyte integrins of the β2 integrin family. The α2 I-domain was 23-41% similar to domains in cartilage matrix protein and von Willebrand factor, which are perhaps associated with collagen binding. The NH2-terminal sequence reported here for α2 does not match the previously reporteed α2 NH2-terminal sequence (Takada, Y., J.L. Strominger, and M.E. Hemler. 1987. Proc. Natl. Acad. Sci. USA. 84:3239-3243). Resolution of this discrepancy suggests that there may be another VLA heterodimer that resembles VLA-2 in size but has a different amino acid sequence.

Original languageEnglish
Pages (from-to)397-407
Number of pages11
JournalJournal of Cell Biology
Volume109
Issue number1
Publication statusPublished - 1989
Externally publishedYes

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Integrin alpha2beta1
Collagen Receptors
Integrins
Collagen
Blood Platelets
Amino Acids
Amino Acid Sequence
Matrilin Proteins
von Willebrand Factor
Protein Sorting Signals
Libraries
Cysteine
Leukocytes
Complementary DNA
Clone Cells
Metals
Antibodies

ASJC Scopus subject areas

  • Cell Biology

Cite this

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title = "The primary structure of the VLA-2/collagen receptor α2 subunit (platelet gpIa): Homology to other integrins and the presence of a possible collagen-binding domain",
abstract = "VLA-2 (also called gpIa/IIa on platelets) is a collagen receptor with a unique α subunit and a β subunit common to other adhesion receptors in the VLA/integrin family. Multiple cDNA clones for the human VLA-2 α2 subunit have been selected from a λgtll library by specific antibody screening. The 5,374-bp nucleotide sequence encoded for 1,181 amino acids, including a signal peptide of 29 amino acids followed by a long extracellular domain (1,103 amino acids), a transmembrane domain, and a short cytoplasmic segment (22 amino acids). Direct sequencing of purified α2 protein confirmed the identity of the 15 NH2-terminal amino acids. Overall, the α2 amino acid sequence was 18-25{\%} similar to the sequences known for other integrin α subunits. In particular, the α2 sequence matched other integrin α chains in (a) the positions of 17 of its 20 cysteine residues; (b) the presence of three metal-binding domains of the general structure DXDXDGXXD; and (c) the transmembrane domain sequence. In addition, the α2 sequence has a 191-amino acid insert (called the I-domain), previously found only in leukocyte integrins of the β2 integrin family. The α2 I-domain was 23-41{\%} similar to domains in cartilage matrix protein and von Willebrand factor, which are perhaps associated with collagen binding. The NH2-terminal sequence reported here for α2 does not match the previously reporteed α2 NH2-terminal sequence (Takada, Y., J.L. Strominger, and M.E. Hemler. 1987. Proc. Natl. Acad. Sci. USA. 84:3239-3243). Resolution of this discrepancy suggests that there may be another VLA heterodimer that resembles VLA-2 in size but has a different amino acid sequence.",
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T1 - The primary structure of the VLA-2/collagen receptor α2 subunit (platelet gpIa)

T2 - Homology to other integrins and the presence of a possible collagen-binding domain

AU - Takada, Y.

AU - Hemler, M. E.

PY - 1989

Y1 - 1989

N2 - VLA-2 (also called gpIa/IIa on platelets) is a collagen receptor with a unique α subunit and a β subunit common to other adhesion receptors in the VLA/integrin family. Multiple cDNA clones for the human VLA-2 α2 subunit have been selected from a λgtll library by specific antibody screening. The 5,374-bp nucleotide sequence encoded for 1,181 amino acids, including a signal peptide of 29 amino acids followed by a long extracellular domain (1,103 amino acids), a transmembrane domain, and a short cytoplasmic segment (22 amino acids). Direct sequencing of purified α2 protein confirmed the identity of the 15 NH2-terminal amino acids. Overall, the α2 amino acid sequence was 18-25% similar to the sequences known for other integrin α subunits. In particular, the α2 sequence matched other integrin α chains in (a) the positions of 17 of its 20 cysteine residues; (b) the presence of three metal-binding domains of the general structure DXDXDGXXD; and (c) the transmembrane domain sequence. In addition, the α2 sequence has a 191-amino acid insert (called the I-domain), previously found only in leukocyte integrins of the β2 integrin family. The α2 I-domain was 23-41% similar to domains in cartilage matrix protein and von Willebrand factor, which are perhaps associated with collagen binding. The NH2-terminal sequence reported here for α2 does not match the previously reporteed α2 NH2-terminal sequence (Takada, Y., J.L. Strominger, and M.E. Hemler. 1987. Proc. Natl. Acad. Sci. USA. 84:3239-3243). Resolution of this discrepancy suggests that there may be another VLA heterodimer that resembles VLA-2 in size but has a different amino acid sequence.

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