Cathepsin H from human placenta.

G Sawicki; M Warwas

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PubMed · 2486008

Cathepsin H from human placenta.

G Sawicki·M Warwas

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Abstract

Cathepsin H was isolated from human placenta by autolysis, acetone fractionation, and chromatography on DEAE-cellulose, Sephadex G-75, hydroxyapatite and concanavalin A-Sepharose. The enzyme gave on SDS-polyacrylamide gel electrophoresis two bands of Mr 25,500 and 28,500. Two active forms of the enzyme, with pI of 6.0 and 6.45, were obtained by isoelectric focusing. The enzyme is stable over the pH range 5-7.5, whereas it becomes inactive on heating to 50 degrees C. Cathepsin H of human placenta, like the enzyme from other sources, hydrolyses protein and naphthylamide substrates, showing within the latter group the strongest preference towards arginine-beta-naphthylamide (pH optimum 6.8). The enzyme is inhibited by the known inhibitors of cysteine proteases and by placental cystatins.

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Cathepsin H Cathepsins Cysteine Endopeptidases Female Humans Placenta Pregnancy Journal Article Research Support, Non-U.S. Gov't

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G Sawicki, M Warwas. 1989. Cathepsin H from human placenta.. https://pubmed.ncbi.nlm.nih.gov/2486008/

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Enzymatically modified LDL induces cathepsin H in human monocytes: potential relevance in early atherogenesis.

OBJECTIVE: Modification with proteases and cholesterylesterase transforms LDL to a moiety that resembles lipoproteins isolated from atherosclerotic lesions and possesses atherogenic properties. To identify changes in monocyte-derived foam cells laden with enzymatically modified LDL (E-LDL), we compared patterns of the most abundant transcripts in these cells after incubation with LDL or E-LDL. METHODS AND RESULTS: Serial analyses of gene expression (SAGE) libraries were constructed from human monocytes after treatment with LDL or E-LDL. Several tags were differentially expressed in LDL-treated versus E-LDL-treated cells, whereby marked selective induction by E-LDL of cathepsin H was conspicuous. We show that cathepsin H is expressed in atherosclerotic lesions in colocalization with E-LDL. Furthermore, we demonstrate that LDL modified with cathepsin H and cholesterylesterase can confer onto LDL the capacity to induce macrophage foam cell formation and to induce cathepsin H. CONCLUSIONS: Cathepsin H could contribute to the transformation of LDL to an atherogenic moiety; the process might involve a self-sustaining amplifying circle.

Cathepsin H↗

PubMed1989

Cystatins of human placenta.

Two low-molecular protein fractions inhibiting cysteine proteases were isolated from human placenta by alkalization to pH 11, acetone fractionation, affinity chromatography on CM-papain-Sepharose 4B, and Sephadex G-75 gel filtration. The results of polyacrylamide gel electrophoresis, isoelectric focusing indicate that one of there fractions in a dimer of cystatins B, and another is a mixture of cystatins A and B.

Cathepsin H↗