Document Detail

Characterization of the hypertonically induced tyrosine phosphorylation of erythrocyte band 3.
MedLine Citation:
PMID:  9761728     Owner:  NLM     Status:  MEDLINE    
Human erythrocyte band 3 becomes rapidly phosphorylated on tyrosine residues after exposure of erythrocytes to hypertonic conditions. The driving force for this phosphorylation reaction seems to be a decrease in cell volume, because (1) changes in band 3 phosphotyrosine content accurately track repeated changes in erythrocyte volume through several cycles of swelling and shrinking; (2) the level of band 3 phosphorylation is independent of the osmolyte employed but strongly sensitive to the magnitude of cell shrinkage; and (3) exposure of erythrocytes to hypertonic buffers under conditions in which intracellular osmolarity increases but volume does not change (nystatin-treated cells) does not promote an increase in tyrosine phosphorylation. We hypothesize that shrinkage-induced tyrosine phosphorylation results either from an excluded-volume effect, stemming from an increase in intracellular crowding, or from changes in membrane curvature that accompany the decrease in cell volume. Although the net phosphorylation state of band 3 is shown to be due to a delicate balance between a constitutively active tyrosine phosphatase and constitutively active tyrosine kinase, the increase in phosphorylation during cell shrinkage was demonstrated to derive specifically from an activation of the latter. Further, a peculiar inhibition pattern of the volume-sensitive erythrocyte tyrosine kinase that matched that of p72syk, a tyrosine kinase already known to associate with band 3 in vivo, suggested the involvement of this kinase in the volume-dependent response.
G Minetti; C Seppi; A Ciana; C Balduini; P S Low; A Brovelli
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Biochemical journal     Volume:  335 ( Pt 2)     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1998 Oct 
Date Detail:
Created Date:  1998-12-22     Completed Date:  1998-12-22     Revised Date:  2011-11-02    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  305-11     Citation Subset:  IM    
Dipartimento di Biochimica 'A. Castellani', Università di Pavia, Via Bassi 21, I-27100 Pavia, Italy.
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MeSH Terms
Anion Exchange Protein 1, Erythrocyte / drug effects,  genetics,  metabolism*
Cell Size / drug effects
Enzyme Inhibitors / pharmacology
Enzyme Precursors / antagonists & inhibitors,  genetics,  metabolism
Erythrocytes / drug effects,  physiology*
Hypertonic Solutions / pharmacology*
Intracellular Signaling Peptides and Proteins
Osmolar Concentration
Phosphoric Monoester Hydrolases / antagonists & inhibitors,  metabolism
Phosphorylation / drug effects
Protein-Tyrosine Kinases / antagonists & inhibitors,  genetics,  metabolism
Recombinant Proteins / genetics,  metabolism
Staurosporine / pharmacology
Time Factors
Tyrosine / metabolism*
Grant Support
Reg. No./Substance:
0/Anion Exchange Protein 1, Erythrocyte; 0/Enzyme Inhibitors; 0/Enzyme Precursors; 0/Hypertonic Solutions; 0/Intracellular Signaling Peptides and Proteins; 0/Recombinant Proteins; 55520-40-6/Tyrosine; 62996-74-1/Staurosporine; EC Kinases; EC kinase; EC 3.1.3.-/Phosphoric Monoester Hydrolases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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