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Involvement of cathepsin B- and L-like proteinases in silk gland histolysis during metamorphosis of Bombyx mori.
Arch Biochem Biophys. 2001 Jun 01; 390(1):28-34.AB

Abstract

To identify proteinases involved in programmed cell death of the silk glands of Bombyx mori, we measured enzyme activities in silk gland homogenates. Several peptidyl-4-methylcoumaryl-7-amides (MCAs) and bovine hemoglobin were used as substrates in the presence and absence of proteinase inhibitors. The hydrolysis of t-butyloxycarbonyl-Phe-Ser-Arg-MCA (Boc-FSR-MCA), benzyloxy-carbonyl-Phe-Arg-MCA (Z-FR-MCA), and Z-Arg-Arg-MCA (Z-RR-MCA) was optimal at pH 5.5, 5.0, and 5.5, respectively. It was stimulated by the sulfhydryl compounds or EDTA and inhibited by both cysteine proteinase inhibitors and a cathepsin B-specific inhibitor, l-3-trans-(propyl-carbamoyl)oxirane-2-carbonyl)-L-isoleucyl-L-prolin (CA-074). The hemoglobin hydrolysis at the optimum pH 3.5 was inactivated by cysteine proteinase inhibitors, but stimulated slightly by pepstatin. The cleavage of Arg-MCA (R-MCA) and Leu-MCA (L-MCA) at optimum pH of 7.0 was strongly inhibited by an aminopeptidase inhibitor, puromycin, and by sulfhydryl compounds. The Boc-FSR-MCA, Z-FR-MCA, Z-RR-MCA, and hemoglobin hydrolyzing activities increased in the silk glands dramatically after cocoon formation, while the R-MCA and L-MCA cleaving activities declined. The results strongly suggest the involvement of cathepsin B- and cathepsin L-like proteinases in the histolysis of the silk gland during metamorphosis.

Authors+Show Affiliations

Shiba H
Department of Applied Biological Science, College of Bioresource Sciences, Nihon University, 1866 Kameino, Fujisawa-shi, Kanagawa, 252-8510, Japan. chang@brs.nihon-u.ac.jp
Uchida D
No affiliation info available
Kobayashi H
No affiliation info available
Natori M
No affiliation info available

MeSH

AnimalsBombyxCathepsin BCathepsin LCathepsinsCattleCysteine EndopeptidasesEndopeptidasesExocrine GlandsHemoglobinsHydrolysisIn Vitro TechniquesInsect ProteinsKineticsMetamorphosis, BiologicalProtease InhibitorsSilkSubstrate Specificity

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

11368511

Citation

Shiba, H, et al. "Involvement of Cathepsin B- and L-like Proteinases in Silk Gland Histolysis During Metamorphosis of Bombyx Mori." Archives of Biochemistry and Biophysics, vol. 390, no. 1, 2001, pp. 28-34.
Shiba H, Uchida D, Kobayashi H, et al. Involvement of cathepsin B- and L-like proteinases in silk gland histolysis during metamorphosis of Bombyx mori. Arch Biochem Biophys. 2001;390(1):28-34.
Shiba, H., Uchida, D., Kobayashi, H., & Natori, M. (2001). Involvement of cathepsin B- and L-like proteinases in silk gland histolysis during metamorphosis of Bombyx mori. Archives of Biochemistry and Biophysics, 390(1), 28-34.
Shiba H, et al. Involvement of Cathepsin B- and L-like Proteinases in Silk Gland Histolysis During Metamorphosis of Bombyx Mori. Arch Biochem Biophys. 2001 Jun 1;390(1):28-34. PubMed PMID: 11368511.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Involvement of cathepsin B- and L-like proteinases in silk gland histolysis during metamorphosis of Bombyx mori. AU - Shiba,H, AU - Uchida,D, AU - Kobayashi,H, AU - Natori,M, PY - 2001/5/23/pubmed PY - 2001/6/29/medline PY - 2001/5/23/entrez SP - 28 EP - 34 JF - Archives of biochemistry and biophysics JO - Arch Biochem Biophys VL - 390 IS - 1 N2 - To identify proteinases involved in programmed cell death of the silk glands of Bombyx mori, we measured enzyme activities in silk gland homogenates. Several peptidyl-4-methylcoumaryl-7-amides (MCAs) and bovine hemoglobin were used as substrates in the presence and absence of proteinase inhibitors. The hydrolysis of t-butyloxycarbonyl-Phe-Ser-Arg-MCA (Boc-FSR-MCA), benzyloxy-carbonyl-Phe-Arg-MCA (Z-FR-MCA), and Z-Arg-Arg-MCA (Z-RR-MCA) was optimal at pH 5.5, 5.0, and 5.5, respectively. It was stimulated by the sulfhydryl compounds or EDTA and inhibited by both cysteine proteinase inhibitors and a cathepsin B-specific inhibitor, l-3-trans-(propyl-carbamoyl)oxirane-2-carbonyl)-L-isoleucyl-L-prolin (CA-074). The hemoglobin hydrolysis at the optimum pH 3.5 was inactivated by cysteine proteinase inhibitors, but stimulated slightly by pepstatin. The cleavage of Arg-MCA (R-MCA) and Leu-MCA (L-MCA) at optimum pH of 7.0 was strongly inhibited by an aminopeptidase inhibitor, puromycin, and by sulfhydryl compounds. The Boc-FSR-MCA, Z-FR-MCA, Z-RR-MCA, and hemoglobin hydrolyzing activities increased in the silk glands dramatically after cocoon formation, while the R-MCA and L-MCA cleaving activities declined. The results strongly suggest the involvement of cathepsin B- and cathepsin L-like proteinases in the histolysis of the silk gland during metamorphosis. SN - 0003-9861 UR - https://www.unboundmedicine.com/medline/citation/11368511/Involvement_of_cathepsin_B__and_L_like_proteinases_in_silk_gland_histolysis_during_metamorphosis_of_Bombyx_mori_ DB - PRIME DP - Unbound Medicine ER -