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Cloning and expression of human mitogen-activated protein kinase kinase 7gamma1

Laura Michael1, Jennifer Swantek, Megan J Robinson

  • 1Pfizer Global Research & Development, Michigan Laboratories, Department of Inflammation Biology, Ann Arbor, USA. Laura.Michael@Pfizer.com

Biochemical and Biophysical Research Communications
|January 31, 2006
PubMed

Insights

Researchers cloned human MKK7gamma1, a key activator of c-Jun N-terminal kinase (JNK). This MKK7 isoform is expressed in various human tissues, tumors, and synoviocytes, suggesting a role in cellular signaling and disease.

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Biochemistry

Background:

  • Mitogen-activated protein kinase kinase 7 (MKK7) is a critical activator of c-Jun N-terminal kinase (JNK).
  • MKK7 activates JNK through phosphorylation of specific residues within kinase subdomain VIII.
  • While six murine MKK7 isoforms are known, only three human isoforms have been reported.

Purpose of the Study:

  • To report the cloning of hMKK7gamma1, the human homolog of murine MKK7gamma1.
  • To investigate the expression patterns of hMKK7gamma1 in various human tissues and disease states.
  • To assess the activation potential of recombinant hMKK7gamma1.

Main Methods:

  • Cloning of the human MKK7gamma1 gene.
  • Messenger RNA (mRNA) expression analysis using PCR in various tissues, tumors, and synoviocytes.
  • In vitro phosphorylation and activation assays using recombinant hMKK7gamma1 and MEKK1.

Main Results:

  • The human MKK7gamma1 gene was successfully cloned.
  • hMKK7gamma1 mRNA transcripts were detected in placenta, fetal liver, and skeletal muscle.
  • Expression was also observed in diverse normal tissues, tumors, and synoviocytes from patients with rheumatoid and osteoarthritis.

Conclusions:

  • hMKK7gamma1 is a newly identified human MKK7 isoform.
  • Its expression in various tissues and disease-associated cells suggests a significant role in human physiology and pathology.
  • Recombinant hMKK7gamma1 can be activated by MEKK1, providing a basis for further functional studies.

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