Amino acid sequence of the factor XIII<sub>a</sub> acceptor site in bovine plasma fibronectin

McDonagh, R. P.; McDonagh, Jan; Petersen, Torben E.; Thøgersen, Hans C.; Skorstengaard, Karna; Sottrup‐Jensen, Lars; Magnusson, Staffan

doi:10.1016/0014-5793(81)80198-6

Cited by 125 publications

(59 citation statements)

References 34 publications

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“…Whereas the ␤-chain of fibrinogen was cleaved slowly, SspB rapidly removed the C terminus of the ␣-chain. During coagulation, the N terminus of fibronectin is crosslinked to the C terminus of the fibrinogen ␣-chain by coagulation factor XIII (36,37), and fibrin matrices that contain fibronectin are much better substrates for fibroblast adhesion and spreading than those lacking fibronectin (38). Therefore, by removing both the N-terminal fibronectin fragment and C-terminal ␣-chain fragment of fibrinogen, SspB has the capacity to affect the function and integrity of fibrin clots.…”

Section: Discussionmentioning

confidence: 99%

Identification of a Novel Maturation Mechanism and Restricted Substrate Specificity for the SspB Cysteine Protease ofStaphylococcus aureus

Massimi¹,

Park²,

Rice³

et al. 2002

Journal of Biological Chemistry

106

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The SspB cysteine protease of Staphylococcus aureus is expressed in an operon, flanked by the sspA serine protease, and sspC, encoding a 12.9-kDa protein of unknown function. SspB was expressed as a 40-kDa prepropeptide pSspB, which did not undergo autocatalytic maturation. Activity of pSspB was reduced compared with 22-kDa mature SspB, but it was equivalent to mature SspB after incubation with SspA, which specifically removed the pSspB N-terminal propeptide. SspC abrogated the activity of pSspB when incubated in a 1:1 complex but had no effect on SspA or papain. Activity of the pSspB⅐SspC complex was restored when incubated with SspA, and SspC was cleaved by SspA but not pSspB. Thus, SspC maintains pSspB as an inert zymogen, and SspA is required for removal of the propeptide and inactivation of SspC. Like the papain protease family, SspB cleaved substrates with a hydrophobic amino acid at P2 but had a strong preference for arginine at P1. It did not cleave casein, serum albumin, IgG, or IgA, but it promoted detachment of cultured keratinocytes and cleaved fibronectin and fibrinogen at sites recognized by urokinase plasminogen activator and plasmin, respectively. It also processed high molecular weight kininogen in a manner resembling plasma kallikrein. Thus, SspB exhibits a novel maturation mechanism and mimics the specificity of plasma serine proteases.

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Section: Discussionmentioning

confidence: 99%

Identification of a Novel Maturation Mechanism and Restricted Substrate Specificity for the SspB Cysteine Protease ofStaphylococcus aureus

Massimi¹,

Park²,

Rice³

et al. 2002

Journal of Biological Chemistry

106

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“…The sequence GQQ is likely to be a target site on the fibronectin molecule for the action of the transamidase or the transglutaminidase factor XIIla mediating covalent crosslinking of fibronectin molecules via Gln-Lys [15,22]. Presently we do not know whether or not the described in vitro cleavage will affect one or both domains because it is unknown whether such a cleavage occurs in vivo.…”

Section: Resultsmentioning

confidence: 99%

Fibronectin is a non‐viral substrate for the HIV proteinase

Oswald¹,

Helm²

1991

FEBS Letters

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The retrovirus encoded proteinase (PR) is required for the proper maturation of viral particles into infectious virus. The PR had been considered highly substrate specific, cleaving exclusively the viral gag and gag‐pol protein precursor. It has recently been reported, however, that cytoskeleton and other cellular filament proteins can be cleaved by the HIV‐1 PR. Here we have evidence that a cell‐associated protein, the fibronectin (A‐chain) is also cleaved in vitro specifically by this PR. The possibility of a cytotoxic role of the PR is conceivable.

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“…There is no obvious con- sensus feature among them. Although the specific Gln residues within several proteins, including fibronectin [24], fibrinogen [25-271, nidogen [28] which serve as substrates for FXIIIa had been identified, no consensus sequences around the Gln residues have been discovered. It is likely that the influence of the higher (tertiary and quaternary) order structure of the protein is critical i n determining which Gln residue might act as an amine acceptor in the enzyme-mediated reaction.…”

Section: Resultsmentioning

confidence: 99%

Identification of Factor‐XIIIa‐Reactive Glutaminyl Residues in the Propolypeptide of Bovine von Willebrand Factor

Takagi

Aoyama

Ueki

et al. 1995

European Journal of Biochemistry

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von Willebrand factor is a large multimeric plasma protein which plays important roles in platelet aggregation, blood coagulation and probably also in the adhesion of endothelial cells. A 100‐kDa propeptide, called the propolypeptide of von Willebrand factor (pp‐vWF), is generated during biosynthesis. We found that pp‐vWF served as a substrate for transglutaminases including human factor XIIIa and guinea pig liver transglutaminase [Usui, T., Takagi, J. & Saito, Y. (1993) J. Biol. Chem. 268, 12311–123161. As such, it could form cross‐linked copolymers with the extracellular matrix protein, laminin, making it all the more likely that pp‐vWF plays a role in cell adhesion phenomena [Takagi, J., Sudo, Y., Saito, T. & Saito, Y. (1994) Eur. J. Biochem. 222, 861–867]. In this work, we identified the Gln residues in pp‐vWF specifically reacting with blood coagulation factor XIIIa as amine acceptors. The fluorescent amine, dansylcadaverine, was employed for labeling the enzyme‐reactive sites of the protein. Following partial proteolysis, fragments containing the labeled Gln residues were isolated by passage through an anti‐dansyl affinity chromatographic column. Amino acid sequence analyses of the fragments revealed that, out of about 40 Gln residues in pp‐vWF, only four could be modified in the factor‐XIIIa‐catalyzed reaction.

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Amino acid sequence of the factor XIII_a acceptor site in bovine plasma fibronectin

Cited by 125 publications

References 34 publications

Identification of a Novel Maturation Mechanism and Restricted Substrate Specificity for the SspB Cysteine Protease ofStaphylococcus aureus

Identification of a Novel Maturation Mechanism and Restricted Substrate Specificity for the SspB Cysteine Protease ofStaphylococcus aureus

Fibronectin is a non‐viral substrate for the HIV proteinase

Identification of Factor‐XIIIa‐Reactive Glutaminyl Residues in the Propolypeptide of Bovine von Willebrand Factor

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Amino acid sequence of the factor XIIIa acceptor site in bovine plasma fibronectin

Cited by 125 publications

References 34 publications

Identification of a Novel Maturation Mechanism and Restricted Substrate Specificity for the SspB Cysteine Protease ofStaphylococcus aureus

Identification of a Novel Maturation Mechanism and Restricted Substrate Specificity for the SspB Cysteine Protease ofStaphylococcus aureus

Fibronectin is a non&#x2010;viral substrate for the HIV proteinase

Identification of Factor‐XIIIa‐Reactive Glutaminyl Residues in the Propolypeptide of Bovine von Willebrand Factor

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Product

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Amino acid sequence of the factor XIII_a acceptor site in bovine plasma fibronectin

Fibronectin is a non‐viral substrate for the HIV proteinase