Human Platelet Vesicles Exhibit Distinct Size and Proteome.
J Proteome Res
; 16(7): 2333-2338, 2017 07 07.
Article
in En
| MEDLINE
| ID: mdl-28587468
ABSTRACT
In the past 50 years, isolated blood platelets have had restricted use in wound healing, cancer therapy, and organ and tissue transplant, to name a few. The major obstacle for its unrestricted use has been, among others, the presence of ultrahigh concentrations of growth factors and the presence of both pro-angiogenic and anti-angiogenic proteins. To overcome this problem requires the isolation and separation of the membrane bound secretory vesicles containing the different factors. In the current study, high-resolution imaging of isolated secretory vesicles from human platelets using atomic force microscopy (AFM) and mass spectrometry enabled characterization of the remaining vesicles size and composition following their immunoseparation. The remaining vesicles obtained following osmotic lysis, when subjected to immunoseparation employing antibody to different vesicle-associated membrane proteins (VAMPs), demonstrate for the first time that VAMP-3-, VAMP-7-, and VAMP-8-specific vesicles each possesses distinct size range and composition. These results provide a window into our understanding of the heterogeneous population of vesicles in human platelets and their stability following both physical manipulation using AFM and osmotic lysis of the platelet. This study further provides a platform for isolation and the detailed characterization of platelet granules, with promise for their future use in therapy. Additionally, results from the study demonstrate that secretory vesicles of different size found in cells reflect their unique and specialized composition and function.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Blood Platelets
/
Proteome
/
Secretory Vesicles
/
R-SNARE Proteins
/
Vesicle-Associated Membrane Protein 3
Limits:
Humans
Language:
En
Journal:
J Proteome Res
Journal subject:
BIOQUIMICA
Year:
2017
Document type:
Article
Affiliation country:
Estados Unidos