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Amblyomma americanum salivary gland homolog of nSec1 is essential for saliva protein secretion.

Abstract：

:Soluble N-ethylmaleimide-sensitive factor attachment protein receptor proteins assemble in tight core complexes which promote fusion of carrier vesicles with target compartments. Members of this class of proteins are expressed in all eukaryotic cells and distributed in distinct subcellular compartments. All vesicle transport mechanisms known to date have an essential requirement for a member of the Sec1 protein family, including the nSec1 in regulated exocytosis. A homolog of nSec1 was cloned and sequenced from the salivary glands of partially fed female ticks. Double-stranded RNA was used to specifically reduce the amount of nSec1 mRNA and protein in female adult tick salivary glands. This reduction was accompanied by a decrease in anticoagulant protein release by the glands and by abnormalities in feeding by dsRNA treated ticks. We report the efficacy of double-stranded RNA-mediated interference in "knocking down" nSec1 both in vivo and in vitro in tick salivary glands and the applicability of this technique for studying the mechanism of exocytosis in tick salivary glands.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Karim S,Ramakrishnan VG,Tucker JS,Essenberg RC,Sauer JR

doi

10.1016/j.bbrc.2004.09.189

subject

Has Abstract

pub_date

2004-11-26 00:00:00

pages

1256-63

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(04)02211-9

journal_volume

324

pub_type

杂志文章

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