Search results for VTN

Showing 16 results out of 19

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Protein (1 results from a total of 1)

VTN

Identifier: R-HSA-215971
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: VTN: P04004

Reaction (7 results from a total of 9)

Identifier: R-HSA-2396370
Species: Homo sapiens
Compartment: extracellular region
Vitronectin (VTN) is a major plasma glycoprotein of 75 kDa, circulating at approximately 0.2 mg/ml in humans. It interacts with collagen types I, II, III, IV, V, and VI (Gebb et al. 1986). Deglycosylation enhances VTN binding to collagen and is associated with VTN multimerization (Uchibori-Iwaki et al. 2000, Sano et al. 2007).
Identifier: R-HSA-2731122
Species: Homo sapiens
Compartment: plasma membrane, extracellular region
Syndecans have attached heparan sulfate (HS) and to a lesser extent chondroitin sulfate (CS) chains. These allow interactions with a large number of proteins, including vitronectin (VTN) (Wilkins-Port & McKeown-Longo 1996, Wilkins-Port et al. 2003). It is thought that syndecans often act in concert with other receptors, e.g. integrins alphavbeta3 and alphavbeta5 cooperate with syndecan-1 during adhesion to vitronectin (Beauvais et al. 2004, McQuade et al. 2006) while alpha2beta1 and alpha6beta4 integrins cooperate with syndecans during adhesion to laminin (laminin alpha-1 Hozumi et al. 2006, laminin gamma-2, Ogawa et al. 2007). This relationship between syndecans and co-receptors is not well understood (Alexopoulou et al. 2007). Syndecan-null mice have subtle phenotypes when compared with mice deficient in HS chain synthesis or modification (Echtermeyer et al. 2001, Ishiquro et al. 2001, Götte et al. 2002). GPI-anchored glypicans and matrix HSPGs such as perlecan may compensate for the absence of syndecans.
Identifier: R-HSA-2396079
Species: Homo sapiens
Compartment: extracellular region
The somatomedin B domain of vitronectin (VTN) binds to and stabilizes plasminogen activator inhibitor-1 (PAI1) (Declerck et al. 1988). PAI1 is the principal physiological inhibitor of both tissue (tPA) and urokinase (uPA) plasminogen activators and a key regulator of the fibrinolytic system; the stabilization of PAI1 by VTN thereby regulates proteolysis of fibrin (Zhou et al. 2003). Elevated PAI1 activity is associated with coronary thrombosis (Hamsten et al. 1987) and poor prognosis in many cancers.
Identifier: R-NUL-2465871
Species: Homo sapiens, Rattus norvegicus
Compartment: extracellular region
Vitronectin (VTN) is a major plasma glycoprotein of 75 kDa, circulating at approximately 0.2 mg/ml in humans. VTN interacts with collagen types I, II, III, IV, V, and VI (Gebb et al. 1986). Deglycosylation enhances VTN binding to collagen and is associated with VTN multimerisation (Uchibori-Iwaki et al. 2000, Sano et al. 2007).
Identifier: R-HSA-2465883
Species: Homo sapiens
Compartment: extracellular region
Vitronectin (VTN) is a major plasma glycoprotein of 75 kDa, circulating at approximately 0.2 mg/ml in humans. It interacts with collagen types I, II, III, IV, V, and VI (Gebb et al. 1986). Deglycosylation enhances VTN binding to collagen and is associated with VTN multimerization (Uchibori-Iwaki et al. 2000, Sano et al. 2007).
Identifier: R-HSA-2426471
Species: Homo sapiens
Compartment: plasma membrane, extracellular region
Integrin alphaVbeta3 is sometimes referred to as the 'vitronectin receptor'. Vitronectin interacts with integrins alphaVbeta1 (Marshall et al. 1995), alphaVbeta3 (Pytela et al. 1985, Boettiger et al. 2001), alphaVbeta5 (Panetti & McKeown-Longo 1993) and alpha2b beta3 (Pytela et al. 1986) through Arg-Gly-Asp (RGD) cell binding sequences.

Endothelial cells lining the microvascular wall form a semi-permeable barrier to the movement of blood components. The attachment of endothelial cells to the extracellular matrix (ECM) is largely mediated by transmembrane integrins which recognize short sequence motifs such as Arg-Gly-Asp (RGD) in many ECM proteins.

Integrin alpha5beta1 and alphaVbeta3 bind to the ECM proteins fibronectin and vitronectin respectively. Both are critical for the establishment and stabilization of endothelial monolayers (Cheng & Kramer 1989). Synthetic peptides that compete with ECM proteins for the integrins or antibodies directed against alpha5beta1 and alphaVbeta3 cause endothelial cell detachment (Hayman et al. 1985, Pierschbacher & Ruoslahti 1987).
Identifier: R-HSA-216076
Species: Homo sapiens
Compartment: extracellular region, plasma membrane
Integrin alphaVbeta3 is highly expressed on osteoclasts, bone resorbing cells and is upregulated during vascular damage, angiogenesis and certain type of malignancies. It binds to vitronectin by recognizing the conserved RGD sequence within the N-terminal region. Integrin alphaVbeta3 plays an important role in signal transduction and regulation of osteoclast function. The integrin alphaVbeta5 receptor also interacts with vitronectin, promoting cell spreading. Integrin alphaVbeta8 can bind vitronectin as well as fibrin.

Complex (7 results from a total of 8)

Identifier: R-HSA-2731126
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-2530437
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-2530442
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-NUL-2465855
Species: Rattus norvegicus, Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-216017
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-2465898
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-2465830
Species: Homo sapiens
Compartment: extracellular region

Set (1 results from a total of 1)

Identifier: R-HSA-2466235
Species: Homo sapiens
Compartment: plasma membrane
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