The proteolytic activity and cleavage specificity of fibronectin-gelatinase and fibronectin-lamininase

Unger J, Tschesche H (1999)
JOURNAL OF PROTEIN CHEMISTRY 18(4): 403-411.

Journal Article | Published | English

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Human plasma fibronectin contains two latent aspartic proteinases, FN-gelatinase and FN-lamininase. Both enzymes can be generated and activated in the presence of Ca2+ from the purified cathepsin D-produced 190-kDa fibronectin fragment. We investigated the proteolytic activity and cleavage specificity of both enzymes in a range of pH from 3.5 to 9.0 using the B chain of oxidized bovine insulin and chromogenic peptides as substrates. The inhibition of the enzymes by several natural inhibitors from human plasma was also tested. The specificities of FN-gelatinase and FN-lamininase are similar to other major acidic proteinases, including pepsin, renin, cathepsin D, and HIV-proteinases. Both enzymes mainly hydrolyze three peptide bonds in the oxidized insulin B chain, namely Glu-Ala (residues 13-14), Tyr-Leu (residues 16-17), and Phe-Phe (residues 24-25). For the peptide substrates H-Pro-Thr-Glu-Phe-p-nitro-Phe-Arg-Leu-OH and H-Phe-Gly-His-p-nitro-Phe-Phe-Val-Leu-OMe that were cleaved the respective values of k(cat)/K-M were 105.1 and 11.8 mM(-1) sec(-1) for cleavage by FN-gelatinase, and 123.2 and 15.5 mM(-1) sec(-1) for cleavage by FN-lamininase. The maximal activities of both enzymes were observed in a range between pH 5.6 and 6.3 and they became inactivated at a pH value above 8.4. Both FN-gelatinase and FN-lamininase were efficiently inhibited by alpha(2)-macroglobulin.
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Unger J, Tschesche H. The proteolytic activity and cleavage specificity of fibronectin-gelatinase and fibronectin-lamininase. JOURNAL OF PROTEIN CHEMISTRY. 1999;18(4):403-411.
Unger, J., & Tschesche, H. (1999). The proteolytic activity and cleavage specificity of fibronectin-gelatinase and fibronectin-lamininase. JOURNAL OF PROTEIN CHEMISTRY, 18(4), 403-411.
Unger, J., and Tschesche, H. (1999). The proteolytic activity and cleavage specificity of fibronectin-gelatinase and fibronectin-lamininase. JOURNAL OF PROTEIN CHEMISTRY 18, 403-411.
Unger, J., & Tschesche, H., 1999. The proteolytic activity and cleavage specificity of fibronectin-gelatinase and fibronectin-lamininase. JOURNAL OF PROTEIN CHEMISTRY, 18(4), p 403-411.
J. Unger and H. Tschesche, “The proteolytic activity and cleavage specificity of fibronectin-gelatinase and fibronectin-lamininase”, JOURNAL OF PROTEIN CHEMISTRY, vol. 18, 1999, pp. 403-411.
Unger, J., Tschesche, H.: The proteolytic activity and cleavage specificity of fibronectin-gelatinase and fibronectin-lamininase. JOURNAL OF PROTEIN CHEMISTRY. 18, 403-411 (1999).
Unger, J, and Tschesche, Harald. “The proteolytic activity and cleavage specificity of fibronectin-gelatinase and fibronectin-lamininase”. JOURNAL OF PROTEIN CHEMISTRY 18.4 (1999): 403-411.
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PMID: 10449038
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