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Related Experiment Videos

cDNA sequence of the human integrin beta 5 subunit.

J W McLean1, D J Vestal, D A Cheresh

  • 1Department of Cardiovascular Research, Genentech Inc., South San Francisco, California 94080.

The Journal of Biological Chemistry
|October 5, 1990
PubMed
Summary
This summary is machine-generated.

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Researchers identified a new integrin receptor, beta 5, crucial for cell adhesion. This novel receptor, sharing an alpha subunit with alpha v beta 3, may be widely distributed across various cell types.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • A novel integrin receptor mediating cell adhesion to vitronectin was identified in human lung epithelial cells.
  • This receptor comprises an alpha subunit similar to that of the vitronectin receptor alpha v beta 3 and a distinct beta 5 subunit.

Purpose of the Study:

  • To isolate cDNA clones for the beta 5 subunit.
  • To determine the mRNA and amino acid sequence of the beta 5 subunit.
  • To investigate the distribution of the alpha v and beta 5 integrin subunits.

Main Methods:

  • cDNA cloning and sequencing to determine the beta 5 subunit's sequence.
  • Analysis of mRNA and amino acid sequences.
  • Polymerase chain reaction (PCR) for mRNA abundance analysis across cell lines.

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Main Results:

  • Isolated cDNA clones coding for the beta 5 subunit, revealing a 3.3-kilobase mRNA encoding a 775-amino acid protein.
  • The beta 5 and beta 3 protein sequences exhibit 56% identity, marking them as the most closely related integrin beta subunits.
  • PCR analysis indicated that alpha v and beta 5 mRNAs are present in seven diverse cell lines, whereas beta 3 mRNA was found in only three.

Conclusions:

  • The beta 5 integrin subunit has been sequenced, revealing its close relationship to beta 3.
  • The widespread presence of alpha v and beta 5 mRNAs suggests this novel integrin receptor plays a significant role in cell adhesion across various tissues.