Results 221 to 230 of about 154,667 (281)

Gut microbial DL-endopeptidase alleviates Crohn’s disease via the NOD2 pathway [PDF]

Cell Host and Microbe, 2022
The pattern-recognition receptor NOD2 senses bacterial muropeptides to regulate host immunity and maintain homeostasis. Loss-of-function mutations in NOD2 are associated with Crohn's disease (CD), but how the variations in microbial factors influence ...
Zhenhe Huang
exaly   +2 more sources

Neutral Endopeptidase Expression and Distribution in Human Skin and Wounds

Journal of Investigative Dermatology, 1999
Cutaneous sensory nerves mediate inflammation and wound healing by the release of neuropeptides such as substance P. Neutral endopeptidase is a cell surface enzyme that degrades substance P and thereby terminates its biologic actions. The distribution of
John E Olerud, Marcia L Usui, John C Ansel   +2 more
exaly   +2 more sources

Molecular cloning of the α-subunit of rat endopeptidase-24.18 (endopeptidase-2) and co-localization with endopeptidase-24.11 in rat kidney by in situ hybridization

FEBS Letters, 1992
Endopeptidase-24.18 (endopeptidase-2, EC 3.4.24.18, E-24.18) is a Zn-ectoenzyme of rat renal and intestinal microvillar membranes exhibiting an oligometric structure, α2-β2.
Denis Corbeil, P Crine
exaly   +2 more sources

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Degradation of lysylbradykinin by endopeptidase 24.11 and endopeptidase 24.15

Peptides, 1995
Lysylbradykinin (LBK), a potent bioactive peptide with pleiotropic actions, is the major kinin generated in the extravascular space. To explore possible mechanisms of inactivation of this peptide in tissues, we evaluated its degradation by endopeptidase 24.11 (EP 24.11) and endopeptidase 24.15 (EP 24.15), two zinc metalloenzymes widely distributed in ...
C, Rosenbaum, C, Cardozo, M, Lesser
openaire   +2 more sources

Prolyl endopeptidase inhibitors

Il Farmaco, 2000
Selective prolyl endopeptidase inhibitors were elaborated by modification of the structure of SUAM-1221, by using a CoMFA study and protein crystallography. The most active representatives of omega-(N-hetaryl)alkanoylprolylpyrrolidines, containing 2- or 3-methylene chain links have high activity (IC50 10(-9)-10(-11)) and exhibit significant in vivo ...
I, Hermecz, K, Kánai
openaire   +2 more sources

Proline-Specific Endopeptidases

Russian Journal of Bioorganic Chemistry, 2003
Prolyl endopeptidases, or post-proline-cleaving enzymes, are the specific endopeptidases that hydrolyze peptide substrates at the carbonyl of the internal Pro residue. All the currently known prolyl endopeptidases from animals, microorganisms, fungi, and plants as well as the post-proline-cleaving enzymes that do not exhibit the strict specificity to ...
D V, Besedin, G N, Rudenskaia
openaire   +2 more sources

Prolyl endopeptidase

Life Sciences, 1983
Prolyl endopeptidase (E.C. 3.4.21.26) an enzyme previously called post proline cleaving enzyme, TRH-deamidase or kininase B, may play a role in neuropeptide metabolism. This enzyme, highly active in brain and other tissues, catabolizes proline-containing peptides such as substance P, neurotensin, luteinizing hormone-releasing hormone, thyrotropin ...
openaire   +2 more sources

Pituitary endopeptidases

Molecular and Cellular Biochemistry, 1983
This review summarizes our knowledge of pituitary endopeptidases. Emphasis has been placed on well-characterized enzymes and their potential roles in proteolytic processes of the pituitary. Because of space limitations, degradation of biologically active peptide by crude preparations has generally not been discussed.
openaire   +2 more sources

Quantitation of Endopeptidase 24.11 and Endopeptidase 24.15 in Human Blood Leukocytes

Enzyme and Protein, 2017
Endopeptidase 24.11 (EP 24.11; also called neutral endopeptidase, enkephalinase, CALLA, or CD10) and endopeptidase 24.15 (EP 24.15) are widely distributed neutral metalloendopeptidases that degrade a number of bioactive peptides including substance P, bradykinin, neurotensin, and chemotactic peptides.
L, Casale, C, Cardozo, T, Kalb, M, Lesser   +3 more
openaire   +2 more sources

Biosynthesis of lysosomal endopeptidases

Journal of Cellular Biochemistry, 1989
AbstractDespite the clear differences between the amino acid sequence and enzymatic specificity of aspartic and cysteine endopeptidases, the biosynthetic processing of lysosomal members of these two families is very similar. With in vitro translation and pulse‐chase analysis in tissue culture cells, the biosynthesis of cathepsin D, a aspartic protease,
openaire   +2 more sources