scholarly journals Vascular Adhesion Protein-1 (VAP-1)/Semicarbazide-Sensitive Amine Oxidase (SSAO): A Potential Therapeutic Target for Atherosclerotic Cardiovascular Diseases

2021 ◽  
Vol 12 ◽  
Author(s):  
Hui Li ◽  
Shiyu Du ◽  
Panpan Niu ◽  
Xiaosong Gu ◽  
Jun Wang ◽  
...  
Keyword(s):  
Cardiovascular Diseases ◽  
Amine Oxidase ◽  
Vascular Inflammation ◽  
Adhesion Protein ◽  
Diagnosis And Prognosis ◽  
Atherosclerotic Lesions ◽  
Vascular Adhesion ◽  
Atherosclerotic Cardiovascular Diseases ◽  
Progression Of Atherosclerosis ◽  
Vascular Adhesion Protein 1

Vascular adhesion protein-1 (VAP-1) is a semicarbazide-sensitive amine oxidase (SSAO), whose enzymatic activity regulates the adhesion/exudation of leukocytes in/from blood vessels. Due to its abundant expressions in vascular systems and prominent roles in inflammations, increasing attentions have been paid to the roles of VAP-1/SSAO in atherosclerosis, a chronic vascular inflammation that eventually drives clinical cardiovascular events. Clinical studies have demonstrated a potential value of soluble VAP-1 (sVAP-1) for the diagnosis and prognosis of cardiovascular diseases. Recent findings revealed that VAP-1 is expressed in atherosclerotic plaques and treatment with VAP-1 inhibitors alleviates the progression of atherosclerosis. This review will focus on the roles of VAP-1/SSAO in the progression of atherosclerotic lesions and therapeutic potentials of VAP-1 inhibitors for cardiovascular diseases.

scholarly journals Zinc-α2-Glycoprotein Is An Inhibitor Of Amine Oxidase Copper-Containing 3

2019 ◽  
Author(s):  
Matthias Romauch
Keyword(s):  
Amine Oxidase ◽  
Current Knowledge ◽  
Primary Amines ◽  
Adhesion Protein ◽  
Diagnosis And Prognosis ◽  
Fat Mobilization ◽  
Clinical Biomarker ◽  
Progressive Weight Loss ◽  
Inhibitory Potential ◽  
Vascular Adhesion

AbstractZinc-alpha2-glycoprotein (ZAG) is a major plasma protein whose levels increase in chronic energy-demanding diseases and thus serves as an important clinical biomarker in the diagnosis and prognosis of the development of cachexia. Current knowledge suggests that ZAG mediates progressive weight loss through β-adrenergic signaling in adipocytes, resulting in the activation of lipolysis and fat mobilization. Here, through crosslinking experiments, amine oxidase copper-containing 3 (AOC3) is identified as a novel ZAG binding partner. AOC3 – also known as vascular adhesion protein 1 (VAP-1) and semicarbazide sensitive amine oxidase (SSAO) – deaminates primary amines, thereby generating the corresponding aldehyde, H2O2 and HN3. It is an ectoenzyme largely expressed by adipocytes and induced in endothelial cells during inflammation. Extravasation of immune cells depends on amine oxidase activity and AOC3-derived H2O2 has an insulinogenic effect. The observations described here suggest that ZAG acts as an allosteric inhibitor of AOC3 and interferes with the associated pro-inflammatory and anti-lipolytic functions. Thus, inhibition of the deamination of lipolytic hormone octopamine by AOC3 represents a novel mechanism by which ZAG might stimulate lipolysis. Furthermore, experiments involving overexpression of recombinant ZAG reveal that its glycosylation is co-regulated by oxygen availability and that the pattern of glycosylation affects its inhibitory potential. The newly identified protein interaction between AOC3 and ZAG highlights a previously unknown functional relationship, which may be relevant to inflammation, energy metabolism and the development of cachexia.

scholarly journals Zinc-α2-glycoprotein as an inhibitor of amine oxidase copper-containing 3

Open Biology ◽  
2020 ◽  
Vol 10 (4) ◽  
pp. 190035 ◽  
Author(s):  
Matthias Romauch
Keyword(s):  
Amine Oxidase ◽  
Current Knowledge ◽  
Primary Amines ◽  
Adhesion Protein ◽  
Diagnosis And Prognosis ◽  
Fat Mobilization ◽  
Clinical Biomarker ◽  
Progressive Weight Loss ◽  
Inhibitory Potential ◽  
Vascular Adhesion

Zinc-α2-glycoprotein (ZAG) is a major plasma protein whose levels increase in chronic energy-demanding diseases and thus serves as an important clinical biomarker in the diagnosis and prognosis of the development of cachexia. Current knowledge suggests that ZAG mediates progressive weight loss through β-adrenergic signalling in adipocytes, resulting in the activation of lipolysis and fat mobilization. Here, through cross-linking experiments, amine oxidase copper-containing 3 (AOC3) is identified as a novel ZAG binding partner. AOC3—also known as vascular adhesion protein 1 (VAP-1) and semicarbazide sensitive amine oxidase (SSAO)—deaminates primary amines, thereby generating the corresponding aldehyde, H 2 O 2 and NH 3 . It is an ectoenzyme largely expressed by adipocytes and induced in endothelial cells during inflammation. Extravasation of immune cells depends on amine oxidase activity and AOC3-derived H 2 O 2 has an insulinogenic effect. The observations described here suggest that ZAG acts as an allosteric inhibitor of AOC3 and interferes with the associated pro-inflammatory and anti-lipolytic functions. Thus, inhibition of the deamination of lipolytic hormone octopamine by AOC3 represents a novel mechanism by which ZAG might stimulate lipolysis. Furthermore, experiments involving overexpression of recombinant ZAG reveal that its glycosylation is co-regulated by oxygen availability and that the pattern of glycosylation affects its inhibitory potential. The newly identified protein interaction between AOC3 and ZAG highlights a previously unknown functional relationship, which may be relevant to inflammation, energy metabolism and the development of cachexia.

scholarly journals Semicarbazide-Sensitive Amine Oxidase/Vascular Adhesion Protein-1 Activity Exerts an Antidiabetic Action in Goto-Kakizaki Rats

Diabetes ◽  
2003 ◽  
Vol 52 (4) ◽  
pp. 1004-1013 ◽  
Author(s):  
A. Abella ◽  
L. Marti ◽  
M. Camps ◽  
M. Claret ◽  
J. Fernandez-Alvarez ◽  
...  
Keyword(s):  
Amine Oxidase ◽  
Adhesion Protein ◽  
Vascular Adhesion ◽  
Vascular Adhesion Protein 1

scholarly journals Semicarbazide-Sensitive Amine Oxidase/Vascular Adhesion Protein-1 Deficiency Reduces Leukocyte Infiltration into Adipose Tissue and Favors Fat Deposition

2009 ◽  
Vol 174 (3) ◽  
pp. 1075-1083 ◽  
Author(s):  
Sandy Bour ◽  
Sylvie Caspar-Bauguil ◽  
Zsuzsa Iffiú-Soltész ◽  
Maryse Nibbelink ◽  
Béatrice Cousin ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Amine Oxidase ◽  
Fat Deposition ◽  
Leukocyte Infiltration ◽  
Adhesion Protein ◽  
Vascular Adhesion ◽  
Vascular Adhesion Protein 1

scholarly journals Vascular Adhesion Protein-1 Determines the Cellular Properties of Endometrial Pericytes

2021 ◽  
Vol 8 ◽  
Author(s):  
Seley Gharanei ◽  
Katherine Fishwick ◽  
Ruban Peter Durairaj ◽  
Tianrong Jin ◽  
Eleftherios Siamantouras ◽  
...  
Keyword(s):  
Functional Properties ◽  
Immune Cell ◽  
Amine Oxidase ◽  
Killer Cell ◽  
Human Endometrium ◽  
Cell Trafficking ◽  
Adhesion Protein ◽  
Potential Biomarker ◽  
Vascular Adhesion ◽  
Vascular Adhesion Protein 1

Vascular adhesion protein-1 (VAP-1) is an inflammation-inducible adhesion molecule and a primary amine oxidase involved in immune cell trafficking. Leukocyte extravasation into tissues is mediated by adhesion molecules expressed on endothelial cells and pericytes. Pericytes play a major role in the angiogenesis and vascularization of cycling endometrium. However, the functional properties of pericytes in the human endometrium are not known. Here we show that pericytes surrounding the spiral arterioles in midluteal human endometrium constitutively express VAP-1. We first characterize these pericytes and demonstrate that knockdown of VAP-1 perturbed their biophysical properties and compromised their contractile, migratory, adhesive and clonogenic capacities. Furthermore, we show that loss of VAP-1 disrupts pericyte-uterine natural killer cell interactions in vitro. Taken together, the data not only reveal that endometrial pericytes represent a cell population with distinct biophysical and functional properties but also suggest a pivotal role for VAP-1 in regulating the recruitment of innate immune cells in human endometrium. We posit that VAP-1 could serve as a potential biomarker for pregnancy pathologies caused by a compromised perivascular environment prior to conception.

scholarly journals Vascular Adhesion Protein 1 in the Eye

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Wenting Luo ◽  
Fang Xie ◽  
Zhongyu Zhang ◽  
Dawei Sun
Keyword(s):  
Therapeutic Target ◽  
Amine Oxidase ◽  
Inflammatory Diseases ◽  
Age Related Macular Degeneration ◽  
Soluble Form ◽  
Dual Function ◽  
Ocular Diseases ◽  
Adhesion Protein ◽  
Vascular Adhesion ◽  
Vascular Adhesion Protein 1

Semicarbazide-sensitive amine oxidase/vascular adhesion protein-1 (SSAO/VAP-1), a dual-function molecule with adhesive and enzymatic properties, is expressed on the surface of vascular endothelial cells of mammals. It also exists as a soluble form (sVAP-1), which is implicated in oxidative stress via its enzymatic activity and can be a prognostic biomarker. Recent evidence suggests that VAP-1 is an important therapeutic target for several inflammation-related ocular diseases, such as uveitis, age-related macular degeneration (AMD), and diabetic retinopathy (DR), by involving in the recruitment of leukocytes at sites of inflammation. Furthermore, VAP-1 plays an important role in the pathogenesis of conjunctival inflammatory diseases such as pyogenic granulomas and the progression of conjunctival lymphoma. VAP-1 may be an alternative therapeutic target in ocular diseases. The in vivo imaging of inflammation using VAP-1 as a target molecule is a novel approach with a potential for early detection and characterization of inflammatory diseases. This paper reviews the critical roles of VAP-1 in ophthalmological diseases which may provide a novel research direction or a potent therapeutic strategy.

scholarly journals Inhibition of semicarbazide-sensitive amine oxidase/vascular adhesion protein-1 reduces lipopolysaccharide-induced neuroinflammation

2017 ◽  
Vol 174 (14) ◽  
pp. 2302-2317 ◽  
Author(s):  
Serena Becchi ◽  
Alberto Buson ◽  
Jonathan Foot ◽  
Wolfgang Jarolimek ◽  
Bernard W Balleine
Keyword(s):  
Amine Oxidase ◽  
Adhesion Protein ◽  
Vascular Adhesion ◽  
Vascular Adhesion Protein 1
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