Dimer conformation of soluble PECAM-1, an endothelial marker. (August 2016)
- Record Type:
- Journal Article
- Title:
- Dimer conformation of soluble PECAM-1, an endothelial marker. (August 2016)
- Main Title:
- Dimer conformation of soluble PECAM-1, an endothelial marker
- Authors:
- Jiang, Longguang
Lin, Lin
Li, Rui
Yuan, Cai
Xu, Mingming
Huang, Joy H.
Huang, Mingdong - Abstract:
- Graphical abstract: Highlights: PECAM-1 is commonly-used as an endothelial cell marker. The structural details of homophilic interaction of sPECAM-1 are unknown. Recombinant sPECAM-1 in large quantity by Drosophila expression system. We observed the predominant presence of sPECAM-1 as a dimer on gel filtration chromatography and dynamic light scattering. Small-angle X-ray scattering reveals sPECAM-1 is a homophilic adhesion protein. sPECAM-1 formed a symmetric homodimer of Ω-shape in solution. The sPECAM-1 dimer is mediated through the intermolecular interactions through the first N-terminal domain of sPECAM-1 (D1). Abstract: Platelet endothelial cell adhesion molecule 1 (PECAM-1) is a cell surface receptor widely distributed on endothelium and hematopoietic-derived cells, and maintain the integrity of the blood vessels. PECAM-1 is widely recognized as an endothelial cell marker. The homophilic interaction through its extracellular domain of PECAM-1 (soluble PECAM-1, or sPECAM-1) is important to its functions. However, structural details for such dimerization are not fully understood. Here we report the production of recombinant sPECAM-1 in large quantity by Drosophila expression system and the small-angle X-ray diffraction (SAXS) study. The recombinant sPECAM-1 was found to form one population of dimer, but not oligomer, and was able to bind to heparin immobilized on a chip in surface plasmon resonance imaging (SPRi) binding experiments. The results of SAXS demonstratedGraphical abstract: Highlights: PECAM-1 is commonly-used as an endothelial cell marker. The structural details of homophilic interaction of sPECAM-1 are unknown. Recombinant sPECAM-1 in large quantity by Drosophila expression system. We observed the predominant presence of sPECAM-1 as a dimer on gel filtration chromatography and dynamic light scattering. Small-angle X-ray scattering reveals sPECAM-1 is a homophilic adhesion protein. sPECAM-1 formed a symmetric homodimer of Ω-shape in solution. The sPECAM-1 dimer is mediated through the intermolecular interactions through the first N-terminal domain of sPECAM-1 (D1). Abstract: Platelet endothelial cell adhesion molecule 1 (PECAM-1) is a cell surface receptor widely distributed on endothelium and hematopoietic-derived cells, and maintain the integrity of the blood vessels. PECAM-1 is widely recognized as an endothelial cell marker. The homophilic interaction through its extracellular domain of PECAM-1 (soluble PECAM-1, or sPECAM-1) is important to its functions. However, structural details for such dimerization are not fully understood. Here we report the production of recombinant sPECAM-1 in large quantity by Drosophila expression system and the small-angle X-ray diffraction (SAXS) study. The recombinant sPECAM-1 was found to form one population of dimer, but not oligomer, and was able to bind to heparin immobilized on a chip in surface plasmon resonance imaging (SPRi) binding experiments. The results of SAXS demonstrated that sPECAM-1 formed a symmetric homodimer of Ω-shape in solution, and each protomer adopted an extended conformation. The dimer is mediated through the intermolecular interactions through the first N-terminal domain (D1) of sPECAM-1. This model provides new structural information for its homophilic interaction mechanism. … (more)
- Is Part Of:
- International journal of biochemistry & cell biology. Volume 77:Part A(2016:Aug.)
- Journal:
- International journal of biochemistry & cell biology
- Issue:
- Volume 77:Part A(2016:Aug.)
- Issue Display:
- Volume 77 (2016)
- Year:
- 2016
- Volume:
- 77
- Issue Sort Value:
- 2016-0077-0000-0000
- Page Start:
- 102
- Page End:
- 108
- Publication Date:
- 2016-08
- Subjects:
- PECAM-1 -- Immunoglobulin domains -- Dimer -- Homophilic interactions -- SAXS
Biochemistry -- Periodicals
Cytology -- Periodicals
Biochemistry -- Periodicals
Cell Biology -- Periodicals
Biochimie -- Périodiques
Cytologie -- Périodiques
Biochimie
Cytologie
Biochemistry
Cytology
Ressource Internet (Descripteur de forme)
Périodique électronique (Descripteur de forme)
Periodicals
572.05 - Journal URLs:
- http://www.sciencedirect.com/science/journal/13572725 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.biocel.2016.06.001 ↗
- Languages:
- English
- ISSNs:
- 1357-2725
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4542.135000
British Library DSC - BLDSS-3PM
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- 7921.xml