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Related Experiment Videos

Processing and expression of rat and human clotting factor-X-encoding cDNAs

C Stanton1, R P Ross, S Hutson

  • 1Department of Medicine, Wake Forest University Medical Center, Winston Salem, NC 27157, USA.

Gene
|March 9, 1996
PubMed
Summary

Researchers cloned rat clotting factor X (FX) cDNA, finding its propeptide cleavage site differs from human FX. This difference may explain variations in how human and rat FX are processed by proteases.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Clotting Factor X (FX) is a vitamin-K-dependent protein crucial for blood coagulation.
  • Vitamin-K-dependent proteins typically have a dibasic sequence at their propeptide cleavage site.
  • Human FX has a unique Thr-Arg sequence at this site, unlike the expected dibasic sequence.

Purpose of the Study:

  • To clone and characterize rat clotting factor X (FX) cDNA.
  • To compare the propeptide cleavage site of rat FX with that of human FX.
  • To investigate the implications of sequence differences on FX processing.

Main Methods:

  • Cloning of rat liver cDNA library to obtain FX encoding cDNA.
  • DNA sequencing to determine the nucleotide and amino acid sequences.

Related Experiment Videos

  • Expression of rat and human FX cDNAs in Cos-1 cells.
  • Analysis of secreted Factor X forms (single- and two-chain).

    • Main Results:

    • Rat FX cDNA encodes a protein with an Arg-Arg dibasic sequence at the propeptide cleavage site.
    • Human and rat FX share 76% amino acid sequence identity but differ at the cleavage site.
    • Expression studies showed both rat and human cDNAs produced single- and two-chain FX.
    • Two-chain forms, lacking the propeptide, were secreted at similar rates for both species.

    Conclusions:

    • Rat FX processing follows the typical pattern for vitamin-K-dependent proteins.
    • The unique Thr-Arg cleavage site in human FX suggests involvement of additional proteases.
    • Further investigation is needed to identify proteases processing human FX at the Thr-Arg motif.