Structural Differences Between Rabbit Cathepsin E and Cathepsin D

Lapresle, C; Puizdar,; Porchon-Bertolotto, C; Joukoff, Elisabeth; Turk,

doi:10.1515/bchm3.1986.367.1.523

Cited by 17 publications

(3 citation statements)

References 2 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The two domains comprise the active site. The DTG sequence occurs in cathepsin E molecules in humans and all animal species except rabbit cathepsin E [28].…”

Section: Biosynthesismentioning

confidence: 99%

Cathepsin E (EC 3.4.23.34) — a review

Chlabicz¹,

Gacko²,

Worowska³

et al. 2012

Folia Histochem Cytobiol.

View full text Add to dashboard Cite

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.

show abstract

“…The two domains comprise the active site. The DTG sequence occurs in cathepsin E molecules in humans and all animal species except rabbit cathepsin E [28].…”

Section: Biosynthesismentioning

confidence: 99%

Cathepsin E (EC 3.4.23.34) — a review

Chlabicz¹,

Gacko²,

Worowska³

et al. 2012

Folia Histochem Cytobiol.

View full text Add to dashboard Cite

show abstract

“…For instance, Cathepsin A and G are serine proteases; cathepsin B, C, F, H, K, L1, L2, O, S, W, and Z are cysteine proteases; while cathepsin D and E are aspartyl proteases. Cathepsin D is a 40 kDa protein with an isoelectric point of 6.95, whereas cathepsin E is a dimeric peptide each having a molecular mass of 40 kDa with an isoelectric point of 4.6 and 4.65 [4]. With the exception of cathepsin K, which works extracellularly after secretion by osteoclasts during bone resorption, most cathepsin proteases are within the lysosomes.…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization and expression analysis of the channel catfish cathepsin D genes

Feng

Zhang

Liu

et al. 2011

Fish & Shellfish Immunology

View full text Add to dashboard Cite

“…It is a glycoprotein with an (intact) Mr of 42000, but consists of one (rat) or two chains (human) depending on the species of origin. By contrast, relatively little information is available on cathepsin E. Until recently, it has been localized in polymorphonuclear leucocytes and macrophages [2] and had been isolated only from rabbit bone marrow [3] and rat spleen [4]. By contrast, spleen of bovine or human origin appears to contain little if any of this enzyme, and indeed there has been considerable uncertainty as to whether this proteinase is a genuine enzyme in its own right or is derived from dimerization of cathepsin D [5].…”

Section: Introductionmentioning

confidence: 99%

Identification of the aspartic proteinases from human erythrocyte membranes and gastric mucosa (slow-moving proteinase) as catalytically equivalent to cathepsin E

Jupp¹,

Richards²,

Kay³

et al. 1988

Biochemical Journal

View full text Add to dashboard Cite

Three aspartic proteinases with similar Mr values (approx. 80,000) but from distinct sources (human gastric mucosa, human erythrocyte membranes and rat spleen) were shown to have immunological cross-reactivity and comparable mobilities when subjected to polyacrylamide-gel electrophoresis under non-denaturing conditions. Kinetic parameters (kcat, Km and Ki) were determined for the interactions of the three enzymes with two synthetic chromogenic substrates and five inhibitors (naturally occurring and synthetic). On this basis it would appear that all of the enzymes should be considered equivalent to cathepsin E. pH-activity measurements indicated that the aspartic proteinase that originated from the erythrocyte membranes retained activity at a higher pH value than either of its readily soluble counterparts.

show abstract

Structural Differences Between Rabbit Cathepsin E and Cathepsin D

Cited by 17 publications

References 2 publications

Cathepsin E (EC 3.4.23.34) — a review

Cathepsin E (EC 3.4.23.34) — a review

Molecular characterization and expression analysis of the channel catfish cathepsin D genes

Identification of the aspartic proteinases from human erythrocyte membranes and gastric mucosa (slow-moving proteinase) as catalytically equivalent to cathepsin E

Contact Info

Product

Resources

About