Distribution of arachidonic acid among phospholipid subclasses of lone star tick salivary glands

1994 ◽  
Vol 24 (7) ◽  
pp. 663-670 ◽  
Author(s):  
Michael M. Shipley ◽  
Jack W. Dillwith ◽  
Alan S. Bowman ◽  
Richard C. Essenberg ◽  
John R. Sauer
1995 ◽  
Vol 25 (2) ◽  
pp. 225-233 ◽  
Author(s):  
Alan S. Bowman ◽  
John R. Sauer ◽  
Paul A. Neese ◽  
Jack W. Dillwith

1995 ◽  
Vol 25 (4) ◽  
pp. 441-447 ◽  
Author(s):  
Alan S. Bowman ◽  
Jack W. Dillwith ◽  
Robin D. Madden ◽  
John R. Sauer

2001 ◽  
Vol 184 (8) ◽  
pp. 1056-1064 ◽  
Author(s):  
Subrata Das ◽  
Gautam Banerjee ◽  
Kathleen DePonte ◽  
Nancy Marcantonio ◽  
Fred S. Kantor ◽  
...  

1994 ◽  
Vol 24 (4) ◽  
pp. 563-567 ◽  
Author(s):  
William J. Lamoreaux ◽  
Glen R. Needham ◽  
Lewis B. Coons

1982 ◽  
Vol 243 (5) ◽  
pp. C222-C226 ◽  
Author(s):  
I. Litosch ◽  
Y. Saito ◽  
J. N. Fain

In blowfly salivary glands, breakdown of phosphatidylinositol has been linked to the activation of hormone-sensitive Ca2+ channels. Addition of 5-hydroxytryptamine to blowfly salivary glands stimulated the breakdown of phosphatidylinositol prelabeled with 32P or [3H]arachidonic acid. This was associated with a transient accumulation of [3H]arachidonic-labeled diglyceride. There was no appreciable effect of 5-hydroxytryptamine on breakdown of phosphatidylethanolamine or phosphatidylcholine labeled with 32P or [3H]arachidonic acid, indicating that phosphatidylinositol was the immediate source of diglyceride. Extracellular Ca2+ was necessary for [3H]arachidonic acid but not 32P loss from phosphatidylinositol. Addition of arachidonic acid to salivary glands did not stimulate salivary gland secretion or 45Ca flux. In contrast, 5-hydroxytryptamine stimulated both salivary gland secretion and 45Ca flux. These results indicate that, although [3H]arachidonic acid is incorporated into phosphatidylinositol and its release from this phospholipid is increased by 5-hydroxytryptamine, the liberated arachidonic acid does not stimulate salivary gland secretion or 45Ca flux.


2001 ◽  
Vol 69 (5) ◽  
pp. 3057-3066 ◽  
Author(s):  
A. F. Barbet ◽  
Jooyoung Yi ◽  
Anna Lundgren ◽  
B. R. McEwen ◽  
E. F. Blouin ◽  
...  

ABSTRACT The rickettsial pathogen Anaplasma marginale expresses a variable immunodominant outer membrane protein, major surface protein 2 (MSP2), involved in antigenic variation and long-term persistence of the organism in carrier animals. MSP2 contains a central hypervariable region of about 100 amino acids that encodes immunogenic B-cell epitopes that induce variant-specific antibodies during infection. Previously, we have shown that MSP2 is encoded on a polycistronic mRNA transcript in erythrocyte stages of A. marginale and defined the structure of the genomic expression site for this transcript. In this study, we show that the same expression site is utilized in stages of A. marginale infecting tick salivary glands. We also analyzed the variability of this genomic expression site in Oklahoma strain A. marginale transmitted from in vitro cultures to cattle and between cattle and ticks. The structure of the expression site and flanking regions was conserved except for sequence that encoded the MSP2 hypervariable region. At least three different MSP2 variants were encoded in each A. marginalepopulation. The major sequence variants did not change on passage ofA. marginale between culture, acute erythrocyte stage infections, and tick salivary glands but did change during persistent infections of cattle. The variant types found in tick salivary glands most closely resembled those present in bovine blood at the time of acquisition of infection, whether infection was acquired from an acute or from a persistent rickettsemia. These variations in structure of an expression site for a major, immunoprotective outer membrane protein have important implications for vaccine development and for obtaining an improved understanding of the mechanisms of persistence of ehrlichial infections in humans, domestic animals, and reservoir hosts.


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