Document 0015
 DOCN  M9650015
 TI    Expression of HIV-1 envelope glycoprotein alters cellular calmodulin.
 DT    9605
 AU    Radding W; Pan ZQ; Hunter E; Johnston P; Williams JP; McDonald JM;
       Department of Pathology, University of Alabama at Birmingham;
       35294-0007, USA.
 SO    Biochem Biophys Res Commun. 1996 Jan 5;218(1):192-7. Unique Identifier :
       AIDSLINE MED/96136299
 AB    Removal of parts of a known calmodulin binding site at the C-terminus of
       HIV-1 envelope glycoprotein, gp160, can result in diminished
       infectivity. We investigated whether expression of full length gp160
       would result in changes in intracellular calmodulin compared to
       expression of gp160 truncated to remove both known calmodulin binding
       sites. Both Western and Northern blots demonstrated that expression of
       gp160 led to increased calmodulin when compared to expression of
       truncated gp160. The induced calmodulin was associated preferentially
       with a particulate subcellular fraction. Confocal immunomicroscopy
       confirmed the increase in calmodulin and also showed that there was
       enhanced colocalization of calmodulin with gp160. Understanding of the
       role of calmodulin in the viral life-cycle may lead to new therapeutics.
 DE    Binding Sites  Blotting, Western  Calmodulin/BIOSYNTHESIS/*METABOLISM
       Cell Line  Gene Products, env/*BIOSYNTHESIS/METABOLISM  Human
       HIV-1/METABOLISM/*PHYSIOLOGY  Microscopy, Confocal  Protein Binding
       Protein Precursors/*BIOSYNTHESIS/METABOLISM  Recombinant
       Proteins/BIOSYNTHESIS/METABOLISM  Sequence Deletion  Subcellular
       Fractions/METABOLISM  Support, U.S. Gov't, P.H.S.  Transfection  JOURNAL
       ARTICLE

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