FITC characterization of a cathepsin B‐responsive nanoprobe for report of differentiation of HL60 cells into macrophages

2021 ◽  
Author(s):  
Chengxing Zhang ◽  
Jingjing Meng ◽  
Yanhui Zhang ◽  
Dehua Huang ◽  
Peiyang Yan ◽  
...  
Keyword(s):  
Cathepsin B ◽  
Hl60 Cells

scholarly journals Characterization of cathepsins in cartilage

1967 ◽  
Vol 105 (2) ◽  
pp. 549-557 ◽  
Author(s):  
S. Y. Ali ◽  
L. Evans ◽  
E. Stainthorpe ◽  
C. H. Lack
Keyword(s):  
Cathepsin B ◽  
Cartilage Matrix ◽  
Heat Inactivation ◽  
Ph Values ◽  
Fixed Weight ◽  
Exogenous Substrate ◽  
Nitrophenyl Phosphate ◽  
Rabbit Ear ◽  
Ear Cartilage

The presence of a cathepsin B-like enzyme in rabbit ear cartilage was established by the use of the synthetic substrates benzoyl-l-arginine amide and benzoyl-dl-arginine 2-naphthylamide. This was facilitated by using a technique that permits the incubation of a fixed weight of thin (18μ) cartilage sections with an appropriate exogenous substrate. The enzymic properties of cathepsin B in cartilage have been compared with an endogenous enzyme that liberates chondromucopeptide by degrading the cartilage matrix autocatalytically at pH5. Besides being maximally active at pH4·7, these cartilage enzymes are enhanced in activity by cysteine and inhibited by arginine analogues, iodoacetamide, chloroquine and mercuric chloride. They are not inhibited by EDTA, di-isopropyl phosphorofluoridate and diethyl p-nitrophenyl phosphate. When inhibiting the release of chondromucopeptide from cartilage at pH5, the arginine-containing synthetic substrates are hydrolysed simultaneously. These enzymes also share the same heat-inactivation characteristics at various pH values, being stable at acid pH and unstable at neutral and alkaline pH. The experimental evidence indicates that a cathepsin B-like enzyme may be partly responsible for the autolytic degradation of cartilage matrix at pH5.

Characterization of the cathepsin B-like proteinases of Trichomonas tenax ATCC 30207

2000 ◽  
Vol 15 (6) ◽  
pp. 360-364 ◽  
Author(s):  
A. Yamamoto ◽  
E. Asaga ◽  
E. Nagao ◽  
T. Igarashi ◽  
N. Goto
Keyword(s):  
Cathepsin B

Isolation and characterization of cathepsin B from bovine brain

1986 ◽  
Vol 11 (6) ◽  
pp. 851-867 ◽  
Author(s):  
John D. Bradley ◽  
John N. Whitaker
Keyword(s):  
Cathepsin B ◽  
Bovine Brain ◽  
Isolation And Characterization

Rat epidermal cathepsin B: Purification and characterization of proteolytic properties toward filaggrin and synthetic substrates

1995 ◽  
Vol 27 (2) ◽  
pp. 175-183 ◽  
Author(s):  
Akira Kawada ◽  
Kenji Hara ◽  
Koukichi Morimoto ◽  
Masataro Hiruma ◽  
Akira Ishibashi
Keyword(s):  
Cathepsin B ◽  
Purification And Characterization

Cloning and characterization of a novel cathepsin B-like cysteine proteinase from Angiostrongylus cantonensis

2012 ◽  
Vol 110 (6) ◽  
pp. 2413-2422 ◽  
Author(s):  
Mei Cheng ◽  
Xiao Yang ◽  
Zhuoya Li ◽  
Hualiang He ◽  
Zhenyu Qu ◽  
...  
Keyword(s):  
Cathepsin B ◽  
Cysteine Proteinase ◽  
Angiostrongylus Cantonensis
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