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

Stress stimuli-induced lymphocyte activation.

H M Lander1, D M Levine, A Novogrodsky

  • 1Rogosin Institute, Cornell University Medical College, New York, New York 10021.

Cellular Immunology
|November 1, 1992
PubMed
Summary

Stress stimuli like heavy metals and heat shock affect protein tyrosine phosphorylation (PTyr-P) and protein tyrosine phosphatase (PTPase) activity in human cells. These stress responses involve complex regulation of PTyr-P and PTPase, impacting cell signaling pathways.

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

Multivariate Analysis Of The Visual Information Processing Of Numbers.

Multivariate behavioral research·2016
Same author

Influence of multi-lumen extensions on fluid flow through intravenous cannulae.

Anaesthesia·2013
Same author

Butyrate-induced differentiation in leukemic myeloid cells - in-vitro and in-vivo studies.

International journal of oncology·2011
Same author

Physician-patient communication in the urban clinical setting.

Bulletin of the New York Academy of Medicine·2009
Same author

Rapid infusion of a phospholipid emulsion attenuates the effects of endotoxaemia in horses.

Equine veterinary journal·2007
Same author

Tyrphostins reduce chemotherapy-induced intestinal injury in mice: assessment by a biochemical assay.

British journal of cancer·2005

Area of Science:

  • Cellular biology
  • Biochemistry
  • Immunology

Background:

  • Stress stimuli, including oxidants, heavy metals, and heat shock, are known to induce stress proteins and enhance glucose uptake.
  • Protein tyrosine phosphorylation (PTyr-P) and protein tyrosine phosphatase (PTPase) activity are critical regulators of cellular signaling pathways.
  • The src family protein tyrosine kinase (PTK), p56lck, plays a role in immune cell activation and signaling.

Purpose of the Study:

  • To investigate the effects of stress stimuli on PTyr-P, PTPase activity, p56lck activation, and glucose uptake in human peripheral blood mononuclear cells.
  • To elucidate the relationship between stress-induced modulation of PTPase activity and PTyr-P.
  • To explore the correlation between PTPase activity, p56lck activation, and glucose uptake under various stress conditions.

Related Experiment Videos

Main Methods:

  • Human peripheral blood mononuclear cells were treated with various stress stimuli (Hg2+, heat shock, phenylarsine oxide - PAO).
  • Protein tyrosine phosphorylation (PTyr-P) was assessed using Western blotting techniques.
  • Protein tyrosine phosphatase (PTPase) activity and p56lck activation were measured.
  • Glucose uptake was quantified in response to stress stimuli.

Main Results:

  • Stress stimuli modulated PTPase activity and activated p56lck in a dose-dependent manner.
  • Hg2+ and heat shock stimulated PTPase activity, while PAO showed marginal stimulation.
  • PTyr-P was observed at stress-inducing doses that inhibited PTPase activity, not those that stimulated it.
  • A correlation was found between PTPase activity increase and p56lck activation with heat shock and Hg2+.
  • PAO activated PTPase at lower concentrations than those required for p56lck activation.
  • No clear correlation was established between PTyr-P induction and glucose uptake.

Conclusions:

  • The relationship between PTPase activity, p56lck activation, PTyr-P, and biological responses is complex and not linear.
  • Both stimulation and inhibition of PTPase may regulate PTyr-P by influencing src family PTKs or dephosphorylation of target proteins.
  • The findings may provide a biochemical basis for the mitogenic effects of Hg2+ on lymphocytes.