Identification of SNARE and cell trafficking regulatory proteins in the salivary glands of the lone star tick, Amblyomma americanum (L.)

S. Karim, R. C. Essenberg, J. W. Dillwith, J. S. Tucker, Alan Stuart Bowman, J. R. Sauer

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

Prostaglandin E-2 (PGE(2)) stimulates secretion of tick salivary gland proteins via a phosphoinositide signaling pathway and mobilization of intracellular Ca2+ (Qian et al., 1998; Yuan et al., 2000). Highly conserved intracellular SNARE (soluble NSF attachment protein receptors) complex proteins are associated with the mechanism of protein secretion in vertebrate and invertebrate neuronal and non-neuronal cells. Proteins in the salivary glands of partially fed female lone star ticks cross-react individually with antibodies to synaptobrevin-2 (vesicle (v)-SNARE), syntaxin-1A, syntaxin-2 and SNAP-25 (target (t)-SNAREs), cytosolic alpha/beta SNAP and NSF (N-ethylmaleimide-sensitive fusion protein), Ca2+ sensitive synaptotagmin, vesicle associated synaptophysin, and regulatory cell trafficking GTPases Rab3A and nSec1. V-SNARE and t-SNARE proteins form an SDS-resistant, boiling sensitive core complex in the salivary glands. Antibodies to SNARE complex proteins inhibit PGE(2)-stimulated secretion of anticoagulant protein in permeabilized tick salivary glands. We conclude that SNARE and cell trafficking regulatory proteins are present and functioning in the process of PGE(2)-stimulated Ca2+ regulated protein secretion in tick salivary glands. (C) 2002 Elsevier Science Ltd. All rights reserved.

Original languageEnglish
Pages (from-to)1711-1721
Number of pages10
JournalInsect Biochemistry and Molecular Biology
Volume32
Issue number12
DOIs
Publication statusPublished - 2002

Keywords

  • salivary glands
  • SNARE
  • exocytosis
  • ticks
  • DIGITONIN-PERMEABILIZED CELLS
  • SYNAPTIC VESICLE DOCKING
  • CLOSTRIDIAL NEUROTOXINS
  • PROSTAGLANDIN E-2
  • CHROMAFFIN CELLS
  • FEMALE TICK
  • KINASE-C
  • EXOCYTOSIS
  • SECRETION
  • CALCIUM

Cite this

Identification of SNARE and cell trafficking regulatory proteins in the salivary glands of the lone star tick, Amblyomma americanum (L.). / Karim, S.; Essenberg, R. C.; Dillwith, J. W.; Tucker, J. S.; Bowman, Alan Stuart; Sauer, J. R.

In: Insect Biochemistry and Molecular Biology, Vol. 32, No. 12, 2002, p. 1711-1721.

Research output: Contribution to journalArticle

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abstract = "Prostaglandin E-2 (PGE(2)) stimulates secretion of tick salivary gland proteins via a phosphoinositide signaling pathway and mobilization of intracellular Ca2+ (Qian et al., 1998; Yuan et al., 2000). Highly conserved intracellular SNARE (soluble NSF attachment protein receptors) complex proteins are associated with the mechanism of protein secretion in vertebrate and invertebrate neuronal and non-neuronal cells. Proteins in the salivary glands of partially fed female lone star ticks cross-react individually with antibodies to synaptobrevin-2 (vesicle (v)-SNARE), syntaxin-1A, syntaxin-2 and SNAP-25 (target (t)-SNAREs), cytosolic alpha/beta SNAP and NSF (N-ethylmaleimide-sensitive fusion protein), Ca2+ sensitive synaptotagmin, vesicle associated synaptophysin, and regulatory cell trafficking GTPases Rab3A and nSec1. V-SNARE and t-SNARE proteins form an SDS-resistant, boiling sensitive core complex in the salivary glands. Antibodies to SNARE complex proteins inhibit PGE(2)-stimulated secretion of anticoagulant protein in permeabilized tick salivary glands. We conclude that SNARE and cell trafficking regulatory proteins are present and functioning in the process of PGE(2)-stimulated Ca2+ regulated protein secretion in tick salivary glands. (C) 2002 Elsevier Science Ltd. All rights reserved.",
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AB - Prostaglandin E-2 (PGE(2)) stimulates secretion of tick salivary gland proteins via a phosphoinositide signaling pathway and mobilization of intracellular Ca2+ (Qian et al., 1998; Yuan et al., 2000). Highly conserved intracellular SNARE (soluble NSF attachment protein receptors) complex proteins are associated with the mechanism of protein secretion in vertebrate and invertebrate neuronal and non-neuronal cells. Proteins in the salivary glands of partially fed female lone star ticks cross-react individually with antibodies to synaptobrevin-2 (vesicle (v)-SNARE), syntaxin-1A, syntaxin-2 and SNAP-25 (target (t)-SNAREs), cytosolic alpha/beta SNAP and NSF (N-ethylmaleimide-sensitive fusion protein), Ca2+ sensitive synaptotagmin, vesicle associated synaptophysin, and regulatory cell trafficking GTPases Rab3A and nSec1. V-SNARE and t-SNARE proteins form an SDS-resistant, boiling sensitive core complex in the salivary glands. Antibodies to SNARE complex proteins inhibit PGE(2)-stimulated secretion of anticoagulant protein in permeabilized tick salivary glands. We conclude that SNARE and cell trafficking regulatory proteins are present and functioning in the process of PGE(2)-stimulated Ca2+ regulated protein secretion in tick salivary glands. (C) 2002 Elsevier Science Ltd. All rights reserved.

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