Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.23.5 (cathepsin D)
 4,130 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Endo- and exopeptidase activities have been measured post-mortem human prefrontal cortex and subjacent white matter to estimate their relative capabilities for protein and peptide degradation. Cathepsin D and three dipeptidases versus leucyl-glycine, glycyl-L-leucine and glycyl-glycine) were assayed in serial, microtome prepared frozen sections (+/- 125 micrograms fresh weight) and related to histological composition (Nissl stain), dry weight, total protein, and DNA content. RNA concentrations were similarly determined, serving as approximate indices of protein synthetic potential. Cathepsin D activity and RNA concentration were, respectively, threefold and twofold greater in cortical gray than in subcortical white matter. Each dipeptidase showed somewhat higher activity in white matter than in cortex. In both tissues the order of activities were: glycyl-leucine greater than glycyl-glycine greater than leucyl-glycine dipeptidase. The results are consistent with preferential localizations of cathepsin D in cortical neurons and dipeptidases in neuroglia. None of the four enzymes showed differences in activity in comparable cortex from six patients with chronic schizophrenia.
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PMID:Protease activities in normal and schizophrenic human prefrontal cortex and white matter. 617 79

Enzymatic activity was investigated in metal-binding proteins from rat epidermal cells. Tris-HCl buffer soluble and KSCN solubilized proteins were extracted stepwise from granular and cornified cells of 2-day old rat epidermis. Each extract was separately applied to a Cu2+ or Zn2+ chelate Sepharose 6B column and the proteins were eluted with buffers of different pHs and finally with EDTA solution. Metal chelate-binding proteins were found in both soluble and solubilized proteins but there was a larger amount in the latter. Affinity of the proteins to bind with Cu2+ chelate was greater than that with Zn2+ chelate. In Tris-HCl buffer extract, histidase activity was detected in Cu2+ chelate-binding proteins, but not in Zn2+ chelate-binding proteins. Acid phosphatase, cysteine proteinase, dipeptidase, cathepsin D, beta-galactosidase, gelatin hydrolase, and superoxide dismutase did not bind to metal chelates although these enzymes, except acid phosphatase, were inhibited by Cu2+, but not by Zn2+. In contrast, KSCN solubilized metal chelate-binding proteins showed plasminogen activator, acid phosphatase, and gelatin and casein hydrolases while histone hydrolase did not bind to either chelate column. Since metal-binding proteins in rat epidermal cells have been shown previously to be histidine- and cysteine-rich proteins concentrated in keratohyalin granules, interaction of metals and the structural proteins with certain enzymes may be involved in the regulation of epidermal cell functions.
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PMID:Enzymatic activity of metal-binding proteins in epidermal cells. 653 44