Vitronectin

Background

Creative Biolabs provides a wide range of high-quality antibodies, assay kits, and vitronectin proteins to help researchers improve their experiments and research. Our dedication to quality ensures reliable results, improving the quality and efficiency of your study.

Introduction

Vitronectin (also named VTN) is an abundant glycoprotein member of the hemopexin family. It can be found in serum and extracellular matrix with a concentration of 200-400 μg/ml, synthesized and excreted by the liver. Vitronectin is essential in a broad spectrum of cell activities, such as cell migration, cell invasion, cell proliferation, and tissue remodeling. It binds to specific cell surface receptors such as integrins αVβ3 and αVβ5 mediated by the Arg-Gly-Asp (RGD) sequence.

Fig.1 PAI-1 in complex with the SMB domain of vitronectin.Distributed under public domain, from Wiki, without modification.

Role of Vitronectin in the Regulation of PAI-1

PAI-1 refers to plasminogen activator inhibitor-1, which functions to inhibit plasminogen activation. This inhibition leads to a decrease in fibrinolytic activity, which promotes the accumulation of thrombus formation, further exacerbating thromboembolic disease and fibrosis of tissues and organs. When vitronectin binds with PAI-1 by the somatomedin B domain, PAI-1 becomes more stable. Therefore, vitronectin can modulate proteolysis, which is initiated by plasminogen activation. Due to the proximity of the binding sites, PAI-1 competes with integrins and u-PAR for binding to vitronectin on the surface of cancer cells. This leads to the separation of tumor cells from the extracellular matrix, which results in enhanced metastasis of the cancer cells. Vitronectin also participates in immune defense by interacting with the complement terminal complex. In the process of hemostasis, vitronectin works by attaching to heparin and counteracting the inhibitory impact of antithrombin III on thrombin and factor Xa.

Vitronectin and Atherosclerotic Disease

Atherosclerosis is a cardiovascular disease, a hardening of the arterial wall and inflammatory lesions of the blood vessels caused by lipid deposits. It is associated with genetic factors, low activity levels, and poor diet. Intima-media thickening is a characteristic feature of atherosclerosis. Studies have shown the significant role played by extracellular matrix proteins, especially glycoproteins, in this pathologic process. Vitronectin is a glycoprotein that accumulates in atherosclerotic plaques. It may come from several origins. Vitronectin can originate from the diffusion from plasma. In the damaged endothelium, the activated platelets release vitronectin. What's more, the cells participating in atherosclerotic plaques can synthesize vitronectin.

Creative Biolabs provides various kinds of vitronectin products, including antibodies, assay kits, proteins, peptides, and lysates. These antibodies are recombinantly expressed and can be employed in various applications including Elisa, FC, etc. We make every effort to fulfill your diverse experimental requirements.

Vitronectin Functional Service

Creative Biolabs offers an extensive range of vitronectin-related products, including anti-vitronectin antibodies, ELISA kits for vitronectin detection, recombinant human vitronectin protein, and vitronectin protein lysates. These reagents proficiently facilitate the detection and monitoring of interactions between various factors and the human vitronectin protein, thereby establishing themselves as vital resources in research efforts focused on developing therapeutic approaches for disease management.

Fig.2 Assessment of vitronectin's binding interaction with SE36.¹

The malaria parasite Plasmodium falciparum thrives in the bloodstream, necessitating sophisticated immune evasion strategies. Researchers have identified Serine repeat antigen 5 (SERA5) as a key antigen expressed during the late trophozoite and schizont stages, with its P47 N-terminal domain forming the foundation of the SE36 vaccine candidate. Investigating the P47 domain's function, researchers utilized ELISA to reveal that vitronectin binds directly to a 20-residue segment in the SE36's C-terminal region. Co-localization of vitronectin with the P47 domain during schizont and merozoite stages, alongside phagocytosis assays, illustrates that vitronectin binding impedes SE36-bead engulfment, suggesting host proteins camouflage merozoites through vitronectin interactions against immune responses.

Creative Biolabs offers expert services concentrated on the functional analysis of vitronectin, which include the study of interaction dynamics and detailed functional evaluations. These services, customized to the unique needs of esteemed clients, are crucial for propelling both clinical and scientific research initiatives forward.

Reference

1. Tougan, Takahiro, et al. "Molecular camouflage of Plasmodium falciparum merozoites by binding of host vitronectin to P47 fragment of SERA5." Scientific reports 8.1 (2018): 5052. Distributed under Open Access license CC BY 4.0, without modification.