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Plasmalemma vesicle-associated protein: A crucial component of vascular homeostasis

View Article: PubMed Central - PubMed

ABSTRACT

Endothelial subcellular structures, including caveolae, fenestrae and transendothelial channels, are crucial for regulating microvascular function. Plasmalemma vesicle-associated protein (PLVAP) is an endothelial cell-specific protein that forms the stomatal and fenestral diaphragms of blood vessels and regulates basal permeability, leukocyte migration and angiogenesis. Loss of PLVAP in mice leads to premature mortality due to disrupted homeostasis. Evidence from previous studies suggested that PLVAP is involved in cancer, traumatic spinal cord injury, acute ischemic brain disease, transplant glomerulopathy, Norrie disease and diabetic retinopathy. Specifically, PLVAP expression has been demonstrated to be upregulated in these diseases, accompanied by pro-angiogenic or pro-inflammatory responses. Therefore, PLVAP is considered a novel therapeutic target, in addition to an endothelial cell marker. The present review summarizes the structure and functions of PLVAP, and its roles in pathophysiological processes.

No MeSH data available.


Protein structure of plasmalemma vesicle-associated protein.
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f1-etm-0-0-3557: Protein structure of plasmalemma vesicle-associated protein.

Mentions: PLVAP, a type II integral membrane glycoprotein with a molecular weight of ~60 kDa, forms dimers in situ and binds to heparin at physiological pH (3,5,28,29). PLVAP consists of three sections: A short (27-amino acid) intracellular tail, a transmembrane domain and a long (358-amino acid) extracellular C-terminal domain (6,30) (Fig. 1). The intracellular domain of PLVAP consists of two short identical stretches of amino acids: One is adjacent to the transmembrane region (8 amino acids) and contains a putative caveolin-1 binding domain, whereas the other is at the extreme N-terminus (7 amino acids) of the protein (6). The extracellular domain consists of four N-glycosylation sites, a proline-rich region near the C-terminus and two large coiled-coil domains (31) (Fig. 1). Every seventh amino acid of the α-helix of the coiled-coil domain is hydrophobic to facilitate the formation of an intermolecular superhelix (4).


Plasmalemma vesicle-associated protein: A crucial component of vascular homeostasis
Protein structure of plasmalemma vesicle-associated protein.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4998186&req=5

f1-etm-0-0-3557: Protein structure of plasmalemma vesicle-associated protein.
Mentions: PLVAP, a type II integral membrane glycoprotein with a molecular weight of ~60 kDa, forms dimers in situ and binds to heparin at physiological pH (3,5,28,29). PLVAP consists of three sections: A short (27-amino acid) intracellular tail, a transmembrane domain and a long (358-amino acid) extracellular C-terminal domain (6,30) (Fig. 1). The intracellular domain of PLVAP consists of two short identical stretches of amino acids: One is adjacent to the transmembrane region (8 amino acids) and contains a putative caveolin-1 binding domain, whereas the other is at the extreme N-terminus (7 amino acids) of the protein (6). The extracellular domain consists of four N-glycosylation sites, a proline-rich region near the C-terminus and two large coiled-coil domains (31) (Fig. 1). Every seventh amino acid of the α-helix of the coiled-coil domain is hydrophobic to facilitate the formation of an intermolecular superhelix (4).

View Article: PubMed Central - PubMed

ABSTRACT

Endothelial subcellular structures, including caveolae, fenestrae and transendothelial channels, are crucial for regulating microvascular function. Plasmalemma vesicle-associated protein (PLVAP) is an endothelial cell-specific protein that forms the stomatal and fenestral diaphragms of blood vessels and regulates basal permeability, leukocyte migration and angiogenesis. Loss of PLVAP in mice leads to premature mortality due to disrupted homeostasis. Evidence from previous studies suggested that PLVAP is involved in cancer, traumatic spinal cord injury, acute ischemic brain disease, transplant glomerulopathy, Norrie disease and diabetic retinopathy. Specifically, PLVAP expression has been demonstrated to be upregulated in these diseases, accompanied by pro-angiogenic or pro-inflammatory responses. Therefore, PLVAP is considered a novel therapeutic target, in addition to an endothelial cell marker. The present review summarizes the structure and functions of PLVAP, and its roles in pathophysiological processes.

No MeSH data available.