The purification and properties of a proteolytic enzyme, rabbit cathepsin E, and further studies on rabbit cathepsin D

Lapresle, C; Webb, Tom R.

doi:10.1042/bj0840455

Cited by 126 publications

(34 citation statements)

References 6 publications

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“…1, using hemoglobin as substrate and under the experimental conditions described above, cathepsin D from rabbit spleen shows activity optimum at pH 3.5, whereas the optimum pH for the activity of cathepsin E lies at pH 2.5-2.8. These results are in good agreement with the data obtained before using serum albumin as substrate [4]. Neither cathepsin D nor cathepsin E are inhibited by diisopropylphosphofluoridate or sulfhydryl reagents.…”

Section: Resultssupporting

confidence: 91%

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Inhibition of cathepsin E by diazoacetyl‐norleucine methyl ester

Keilová

Lapresle

1970

FEBS Letters

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Section: Resultssupporting

confidence: 91%

“…Bone marrow is the original source of cathepsin E. It has been shown that this proteinase occurs in large amounts in polymorphonuclear cells, in smaller quantities in macrophages, and only in trace amounts in lymphocytes, in contrast to cathepsin D, whose presence in all of these three cell types has been demonstrated [4].…”

Section: Resultsmentioning

confidence: 99%

Inhibition of cathepsin E by diazoacetyl‐norleucine methyl ester

Keilová

Lapresle

1970

FEBS Letters

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“…Cathepsin E was first described in 1962 by Lapresle and Webb [1]. It belongs to the third class of enzymes -hydrolases, a subclass of peptide bond hydrolases and a sub-subclass of endopeptidases with aspartic catalytic sites.…”

Section: Introductionmentioning

confidence: 99%

Cathepsin E (EC 3.4.23.34) — a review

Chlabicz¹,

Gacko²,

Worowska³

et al. 2012

Folia Histochem Cytobiol.

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Cathepsin E belongs to the third class of enzymes -hydrolases, a subclass of peptide bond hydrolases and a sub-subclass of endopeptidases with aspartic catalytic sites. Cathepsin E is an endopeptidase with substrate specificity similar to that of cathepsin D. In a human organism, cathepsin E occurs in: erythrocytes, thymus, dendritic cells, epithelial M cells, microglia cells, Langerhans cells, lymphocytes, epithelium of gastrointestinal tract, urinary bladder, lungs, osteoclasts, spleen and lymphatic nodes. In human cells, loci of the gene of pre-procathepsin E are located on chromosome 1 in the region 1231-32. The catalytic site of cathepsin E is two residues of aspartic acid -Asp96 and Asn281, occurring in amino acid triads with sequences DTG96-98 and DTG281-283. To date, no particular role of cathepsin E in the metabolism of proteins in normal tissues has been found. However, it is known that there are many documented pathological conditions in which overexpression of cathepsin E occurs.

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“…This range of pH optimal activity has been observed with some cathepsins previously studied (23). How-ever, most of the cathepsin group of enzymes appears to have maximal activity in the acid pH ranges (24,25,26). Cathepsins have been defined as intracellular proteinases which are distinct from the well-known protein splitting enzymes such as pepsin and trypsin which are secreted into the mammalian gastrointestinal tract (23).…”

Section: Resultsmentioning

confidence: 99%

Studies on human platelet protease activity

Nachman¹,

Ferris²

1968

J. Clin. Invest.

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A B S T R A C T Solubilized protein derived from human platelets was fractionated by DEAE cellulose column chromatography and analyzed for protease activity using three substrates: denatured bovine hemoglobin, alpha casein, and purified plasminogen-free human fibrinogen. A protein fraction was found with proteolytic activity which was heat labile and not attributable to plasmin. The activity was not potentiated by cysteine or inhibited by iodoacetamide. Studies of pH optima indicated a broad range of enzyme activity with peaks in both the acid and alkaline region. Cathepsin A activity was detected in the platelet protease fraction by hydrolysis of the synthetic substrate N-carbobenzoxy-a-L-glutamyl-L-tyrosine. Similar proteolytic activity was found when the proteins derived from isolated platelet granules were examined. The results indicate that human platelets possess potent intracellular proteolytic enzymes. The relationship of this proteolytic activity to the hemostatic process is discussed.

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The purification and properties of a proteolytic enzyme, rabbit cathepsin E, and further studies on rabbit cathepsin D

Cited by 126 publications

References 6 publications

Inhibition of cathepsin E by diazoacetyl‐norleucine methyl ester

Inhibition of cathepsin E by diazoacetyl‐norleucine methyl ester

Cathepsin E (EC 3.4.23.34) — a review

Studies on human platelet protease activity

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