Linked Life Data

8431436

Source:http://linkedlifedata.com/resource/pubmed/id/8431436

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1993-3-15
pubmed:abstractText
Initial studies on the specificity of the multicatalytic proteinase complex (MPC; EC 3.4.99.46) led to the identification of three distinct proteolytic components designated as trypsin-like, chymotrypsin-like, and peptidylglutamyl-peptide hydrolyzing, all sensitive to inactivation by 3,4-dichloroisocoumarin (DCI), a general serine proteinase inhibitor. The three components cleave the peptidyl-arylamide bonds in the model synthetic substrates, Z-(D)-Ala-Leu-Arg-2-naphthylamide, Z-Gly-Gly-Leu-p-nitroanilide, and Z-Leu-Leu-Glu-2-naphthylamide, respectively. We report here evidence for the presence in the MPC of two additional distinct components, neither of them capable of cleaving the three model substrates. One of these components cleaves the Leu-Gly and the Leu-Ala bonds in the substrates Cbz-Gly-Pro-Ala-Leu-Gly-p-aminobenzoate and Cbz-Gly-Pro-Ala-Leu-Ala-p-aminobenzoate, respectively, and is activated by treatment of the MPC with DCI, N-ethylmaleimide, Mg2+, Ca2+, and low concentrations of sodium dodecyl sulfate and fatty acids. This component is apparently identical with the previously identified DCI-resistant component of the MPC that cleaves preferentially bonds on the carboxyl side of branched chain amino acids in natural peptides including neurotensin and proinsulin [Cardozo, C., Vinitsky, A., Hidalgo, M. C., Michaud, C., & Orlowski, M. (1992) Biochemistry 31, 7373-7380]. It is probably also identical with the component proposed to be the main factor responsible for the caseinolytic activity [Pereira, M. E., Nguyen, T., Wagner, B. J., Margolis, J. W., Yu, B., & Wilk, S. (1992a) J. Biol. Chem. 267, 7949-7955]. The designation "branched chain amino acid preferring" (BrAAP) is proposed for this component. The second component cleaves peptide bonds between the small neutral amino acids Ala-Gly and Gly-Gly in the substrates Cbz-Gly-Pro-Ala-Ala-Gly-p-aminobenzoate and Cbz-Gly-Pro-Ala-Gly-Gly-p-aminobenzoate, respectively. This component is sensitive to inactivation by DCI, N-ethylmaleimide, and organic mercurials, but unlike the BrAAP it is significantly activated neither by Mg2+ or Ca2+ nor by fatty acids or sodium dodecyl sulfate. The designation "small neutral amino acid preferring" (SNAAP) is proposed for this component. Both components are sensitive to inhibition by the peptidyl-aldehydes N-acetyl-Leu-Leu-norleucinal (Ac-LLnL-CHO; calpain inhibitor I) and N-acetyl-Leu-Leu-methioninal (Ac-LLM-CHO; calpain inhibitor II) but are resistant to inhibition by Z-LLF-CHO, a potent inhibitor of the chymotrypsin-like activity.(ABSTRACT TRUNCATED AT 400 WORDS)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/3,4-dichloroisocoumarin, http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/Chymotrypsin, http://linkedlifedata.com/resource/pubmed/chemical/Coumarins, http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Lauric Acids, http://linkedlifedata.com/resource/pubmed/chemical/Magnesium, http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides, http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex, http://linkedlifedata.com/resource/pubmed/chemical/Serine Proteinase Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Sodium Dodecyl Sulfate, http://linkedlifedata.com/resource/pubmed/chemical/Trypsin, http://linkedlifedata.com/resource/pubmed/chemical/lauric acid
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1563-72
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8431436-Amino Acid Sequence, pubmed-meshheading:8431436-Animals, pubmed-meshheading:8431436-Calcium, pubmed-meshheading:8431436-Cattle, pubmed-meshheading:8431436-Chymotrypsin, pubmed-meshheading:8431436-Coumarins, pubmed-meshheading:8431436-Cysteine Endopeptidases, pubmed-meshheading:8431436-Kinetics, pubmed-meshheading:8431436-Lauric Acids, pubmed-meshheading:8431436-Magnesium, pubmed-meshheading:8431436-Molecular Sequence Data, pubmed-meshheading:8431436-Multienzyme Complexes, pubmed-meshheading:8431436-Oligopeptides, pubmed-meshheading:8431436-Pituitary Gland, pubmed-meshheading:8431436-Protease Inhibitors, pubmed-meshheading:8431436-Proteasome Endopeptidase Complex, pubmed-meshheading:8431436-Serine Proteinase Inhibitors, pubmed-meshheading:8431436-Sodium Dodecyl Sulfate, pubmed-meshheading:8431436-Substrate Specificity, pubmed-meshheading:8431436-Trypsin
pubmed:year
1993
pubmed:articleTitle
Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids.
pubmed:affiliation
Department of Pharmacology, Mount Sinai School of Medicine, City University of New York, New York 10029.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.