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Electrophoretic analysis of the "cross-class" interaction between novel inhibitory serpin, squamous cell carcinoma antigen-1 and cysteine proteinases.
Electrophoresis. 1997 May; 18(5):784-9.E

Abstract

We investigated the "cross-class" interaction between cysteine proteinases and a novel inhibitory serpin, recombinant squamous cell carcinoma (rSCC) antigen-1, which inhibits a serine proteinase, chymotrypsin. rSCC antigen-1 inhibited the cysteine proteinases, papain, papaya proteinase IV and cathepsin L. Interestingly, although rSCC antigen-1 formed sodium dodecyl sulfate (SDS)- and heat-stable complexes with chymotrypsin, rSCC antigen-1 gave the 40 kDa fragment and small molecular mass peptide by incubation with papain without forming an SDS- and heat-stable complex. The cleavage was observed between the Gly353-Ser354 bond, indicating that rSCC antigen-1 interacts with cysteine proteinases not at the predicted reactive site P1-P1' portion (Ser354-Ser355), but at the Gly353-Ser354 of the P2-P1 portion. These findings promote understanding of the "suicide inhibition" mechanism of SCC antigen-1 against cysteine proteinases.

Authors+Show Affiliations

Nawata S
Department of Obstetrics and Gynecology, Yamaguchi University School of Medicine, Ube, Japan.
Nakamura K
No affiliation info available
Tanaka T
No affiliation info available
Numa F
No affiliation info available
Suminami Y
No affiliation info available
Tsunaga N
No affiliation info available
Kakegawa H
No affiliation info available
Katunuma N
No affiliation info available
Kato H
No affiliation info available

MeSH

AnimalsAntigens, NeoplasmBinding SitesChymotrypsinCysteine EndopeptidasesCysteine Proteinase InhibitorsElectrophoresis, Polyacrylamide GelLysosomesPapainProtein ConformationRecombinant Fusion ProteinsSerpins

Pub Type(s)

Journal Article

Language

eng

PubMed ID

9194607

Citation

Nawata, S, et al. "Electrophoretic Analysis of the "cross-class" Interaction Between Novel Inhibitory Serpin, Squamous Cell Carcinoma Antigen-1 and Cysteine Proteinases." Electrophoresis, vol. 18, no. 5, 1997, pp. 784-9.
Nawata S, Nakamura K, Tanaka T, et al. Electrophoretic analysis of the "cross-class" interaction between novel inhibitory serpin, squamous cell carcinoma antigen-1 and cysteine proteinases. Electrophoresis. 1997;18(5):784-9.
Nawata, S., Nakamura, K., Tanaka, T., Numa, F., Suminami, Y., Tsunaga, N., Kakegawa, H., Katunuma, N., & Kato, H. (1997). Electrophoretic analysis of the "cross-class" interaction between novel inhibitory serpin, squamous cell carcinoma antigen-1 and cysteine proteinases. Electrophoresis, 18(5), 784-9.
Nawata S, et al. Electrophoretic Analysis of the "cross-class" Interaction Between Novel Inhibitory Serpin, Squamous Cell Carcinoma Antigen-1 and Cysteine Proteinases. Electrophoresis. 1997;18(5):784-9. PubMed PMID: 9194607.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Electrophoretic analysis of the "cross-class" interaction between novel inhibitory serpin, squamous cell carcinoma antigen-1 and cysteine proteinases. AU - Nawata,S, AU - Nakamura,K, AU - Tanaka,T, AU - Numa,F, AU - Suminami,Y, AU - Tsunaga,N, AU - Kakegawa,H, AU - Katunuma,N, AU - Kato,H, PY - 1997/5/1/pubmed PY - 1997/5/1/medline PY - 1997/5/1/entrez SP - 784 EP - 9 JF - Electrophoresis JO - Electrophoresis VL - 18 IS - 5 N2 - We investigated the "cross-class" interaction between cysteine proteinases and a novel inhibitory serpin, recombinant squamous cell carcinoma (rSCC) antigen-1, which inhibits a serine proteinase, chymotrypsin. rSCC antigen-1 inhibited the cysteine proteinases, papain, papaya proteinase IV and cathepsin L. Interestingly, although rSCC antigen-1 formed sodium dodecyl sulfate (SDS)- and heat-stable complexes with chymotrypsin, rSCC antigen-1 gave the 40 kDa fragment and small molecular mass peptide by incubation with papain without forming an SDS- and heat-stable complex. The cleavage was observed between the Gly353-Ser354 bond, indicating that rSCC antigen-1 interacts with cysteine proteinases not at the predicted reactive site P1-P1' portion (Ser354-Ser355), but at the Gly353-Ser354 of the P2-P1 portion. These findings promote understanding of the "suicide inhibition" mechanism of SCC antigen-1 against cysteine proteinases. SN - 0173-0835 UR - https://www.unboundmedicine.com/medline/citation/9194607/Electrophoretic_analysis_of_the_"cross_class"_interaction_between_novel_inhibitory_serpin_squamous_cell_carcinoma_antigen_1_and_cysteine_proteinases_ L2 - https://doi.org/10.1002/elps.1150180521 DB - PRIME DP - Unbound Medicine ER -