Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

MAP kinases from bovine brain: purification and characterization

T J Childs1, A S Mak

  • 1Department of Biochemistry, Queen's University, Kingston, ON, Canada.

Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire
|November 1, 1993
PubMed
Summary

Researchers purified two novel mitogen-activated protein (MAP) kinase isoforms from bovine brain. The 42-kDa isoform resembles tau kinase, while the 44-kDa isoform is a previously unreported brain MAP kinase.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Effect of Standard Radiotherapy With Cisplatin vs Accelerated Radiotherapy With Panitumumab in Locoregionally Advanced Squamous Cell Head and Neck Carcinoma: A Randomized Clinical Trial.

JAMA oncology·2016
Same author

MAPK and PKC activity are not required for H(2)O(2)-induced arterial muscle contraction.

American journal of physiology. Heart and circulatory physiology·2000
Same author

Phosphorylation of caldesmon by p21-activated kinase. Implications for the Ca(2+) sensitivity of smooth muscle contraction.

The Journal of biological chemistry·2000
Same author

Different molecular mechanisms for Rho family GTPase-dependent, Ca2+-independent contraction of smooth muscle.

The Journal of biological chemistry·1998
Same author

Autoradiographic localization of 2[125I]iodomelatonin binding sites in the gastrointestinal tract of mammals including humans and birds.

Journal of pineal research·1997
Same author

NMR studies of caldesmon-calmodulin interactions.

Biochemistry·1997

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Mitogen-activated protein (MAP) kinases are crucial signaling enzymes.
  • Understanding brain-specific MAP kinase isoforms is essential for neuroscience research.

Purpose of the Study:

  • To purify and characterize novel mitogen-activated protein (MAP) kinase isoforms from bovine brain.
  • To investigate the substrate specificity and activation properties of these newly identified kinases.

Main Methods:

  • Purification of 42- and 44-kilodalton (kDa) MAP kinase isoforms using multiple chromatography techniques (phenyl-Sepharose, polylysine-agarose, hydroxylapatite, Mono-Q).
  • Assay of kinase activity using myelin basic protein and detection with anti-sea star p44mpk antibody.
  • Investigation of substrate specificity with myelin basic protein, smooth muscle caldesmon, and histone H1.

Related Experiment Videos

Main Results:

  • Successfully purified 42- and 44-kDa MAP kinase isoforms from bovine brain.
  • Identified myelin basic protein and smooth muscle caldesmon as substrates, but not histone H1.
  • The 42-kDa isoform is likely similar to brain tau kinase; the 44-kDa isoform represents a novel brain MAP kinase.
  • Neither purified brain kinase was significantly stimulated by tyrosine kinases p56lck, p56lyn, or p59fyn.
  • Both isoforms undergo autophosphorylation on tyrosine residues, with the 44-kDa isoform showing significant coincident activation.

Conclusions:

  • Bovine brain contains distinct 42-kDa and 44-kDa MAP kinase isoforms with unique properties.
  • The 44-kDa isoform is a novel brain-specific MAP kinase.
  • These findings expand the understanding of MAP kinase signaling in the brain and their potential roles in neuronal function.