Allergen-sensitization increases mast-cell expression of the exocytotic proteins SNAP-23 and syntaxin 4, which are involved in histamine secretion.

نویسندگان

  • E Salinas
  • A Quintanar-Stephano
  • L E Córdova
  • J L Ouintanar
چکیده

BACKGROUND Activation of mast cells (MCs) via aggregation of immunoglobulin E (IgE) bound to its high affinity receptor (FcepsilonRI) results in release of inflammatory mediators from secretory granules. Histamine is one of the critical biological mediators released in the allergic response. Synaptosomal-associated protein of 23 kDa (SNAP-23) and syntaxin 4 are plasma membrane proteins that have been associated with exocytosis in MCs. Studies with monoclonal IgEs indicate that binding of IgE to FcepsilonRI induces molecular and biological changes in OBJECTIVES The aim of this study was to investigate changes in the expression of SNAP-23 and syntaxin 4 by MCs following rat sensitization with ovalbumin (OVA). In addition, we assessed whether these proteins were involved in histamine secretion. METHODS SNAP-23 and syntaxin 4 expression was analyzed by Western blot using MCs from control and sensitized animals. Successful sensitization was confirmed based on the passive cutaneous anaphylaxis reaction. To test the role of these exocytotic proteins in histamine secretion, permeabilized MCs were incubated with SNAP-23 and syntaxin 4 antibodies. RESULTS Expression of SNAP-23 and syntaxin 4 was significantly higher in MCs from OVA-sensitized rats than in cells from control animals. In addition, incubation of permabilized cells with antibodies to SNAP-23 and syntaxin 4 led to a marked reduction of histamine secretion in stimulated cells. CONCLUSIONS Sensitization with OVA increases the expression of SNAP-23 and syntaxin 4 in MCs. Furthermore, our data suggest that these exocytotic proteins participate in histamine secretion.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Effect of Resveratrol Supplementation on the SNARE Proteins Expression in Adipose Tissue of Stroptozotocin-Nicotinamide Induced Type 2 Diabetic Rats

Background: Glucose uptake by muscles and fat cells is carried out by the GLUT4 system. Isoforms of the SNAP23, syntaxin-4 and VAMP-2 play an important role in regulating GLUT-4 trafficking and fusion in adipocytes. The changes of SNARE proteins levels and thus impaired GLUT-4 displacement can be one of the etiological causes of type 2 diabetes.Due to changes in the expression of these proteins...

متن کامل

Involvement of SNAP-23 and syntaxin 6 in human neutrophil exocytosis.

To understand the molecular basis of exocytosis in human neutrophils, the role of syntaxin 6 and SNAP-23 in neutrophil degranulation was examined. Human syntaxin 6 was cloned and identified as a 255-amino acid protein with a carboxy-terminal transmembrane region and two coiled-coil domains. Syntaxin 6 was localized mainly in the plasma membrane of human resting neutrophils, whereas SNAP-23 was ...

متن کامل

Effect of resveratrol on SNARE proteins expression and insulin resistance in skeletal muscle of diabetic rats

Objective(s): Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex proteins are involved in membrane trafficking. The expression of isoforms of SNAP-23, syntaxin-4, and VAMP-2 is significantly done in skeletal muscles; they control GLUT4 trafficking. It is believed that type 2 diabetes could be caused by the modifications in the express...

متن کامل

Identification of soluble N-ethylmaleimide-sensitive factor attachment protein receptor exocytotic machinery in human plasma cells: SNAP-23 is essential for antibody secretion.

Plasma cells (PC) are B-lymphocytes terminally differentiated in a postmitotic state, with the unique purpose of manufacturing and exporting Igs. Despite the importance of this process in the survival of vertebrates, no studies have been made to understand the molecular events that regulate Ig exocytosis by PC. The present study explores the possible presence of the soluble N-ethylmaleimide-sen...

متن کامل

Regulation of Ca2+ channels by SNAP-25 via recruitment of syntaxin-1 from plasma membrane clusters

SNAP-25 regulates Ca2+ channels, with potentially important consequences for diseases involving an aberrant SNAP-25 expression level. How this regulation is executed mechanistically remains unknown. We investigated this question in mouse adrenal chromaffin cells and found that SNAP-25 inhibits Ca2+ currents, with the B-isoform being more potent than the A-isoform, but not when syntaxin-1 is cle...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Journal of investigational allergology & clinical immunology

دوره 18 5  شماره 

صفحات  -

تاریخ انتشار 2008