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Article

A deletion mutant of vitronectin lacking the somatomedin B domain exhibits residual plasminogen activator inhibitor-1-binding activity.

The Journal of biological chemistry - 18 Apr 2008

Schar Christine R, Blouse Grant E, Minor Kenneth H, Peterson Cynthia B

Abstract excerpt

Vitronectin and plasminogen activator inhibitor-1 (PAI-1) are important physiological binding partners that work in concert to regulate cellular adhesion, migration, and fibrinolysis. The high affinity binding site for PAI-1 is located within the N-terminal somatomedin B domain of vitronectin; ho...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 18174166
DOI: 10.1074/jbc.M708017200
PMCID: PMC2447658

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18174166-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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A deletion mutant of vitronectin lacking the somatomedin B domain exhibits residual plasminogen activator inhibitor-1-binding activity.PMID 18174166Read ↗

Characterization of a site on PAI-1 that binds to vitronectin outside of the somatomedin B domain.Semantic proximity Read ↗

Construction of a plasminogen activator inhibitor-1 variant without measurable affinity to vitronectin but otherwise normal.Semantic proximity Read ↗

Structural and functional analysis of the plasminogen activator inhibitor-1 binding motif in the somatomedin B domain of vitronectin.Semantic proximity Read ↗

Vitronectin governs the interaction between plasminogen activator inhibitor 1 and tissue-type plasminogen activator.Semantic proximity Read ↗

The cell attachment and spreading activity of vitronectin is dependent on the Arg-Gly-Asp sequence. Analysis by construction of RGD and domain deletion mutants.Semantic proximity Read ↗

Mapping of binding sites for heparin, plasminogen activator inhibitor-1, and plasminogen to vitronectin's heparin-binding region reveals a novel vitronectin-dependent feedback mechanism for the control of plasmin formation.Semantic proximity Read ↗

Historical analysis of PAI-1 from its discovery to its potential role in cell motility and diseaseSemantic proximity Read ↗

Structure-function relationships of plasminogen activator inhibitor-1 and its potential as a therapeutic agent.Semantic proximity Read ↗

Disulfide bonding arrangements in active forms of the somatomedin B domain of human vitronectin.Semantic proximity Read ↗

The Molecular Basis for Anti-Proteolytic and Non-Proteolytic Functions of Plasminogen Activator Inhibitor Type-1: Roles of the Reactive Centre Loop, the Shutter Region, the Flexible Joint Region and the Small Serpin FragmentSemantic proximity Read ↗

Intra- and extracellular plasminogen activator inhibitor-1 regulate effect of vitronectin against radiation-induced endothelial cell death.Semantic proximity Read ↗

The serpin PAI-1 inhibits cell migration by blocking integrin alpha V beta 3 binding to vitronectin.Semantic proximity Read ↗

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