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    188宝金博页面版: Regulation of Proteolytic Activity of Pepsin in Mice by Rotating Electromagnetic Field

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    内容提示： 3160007-4888/05/1393?0316 ? 2005 Springer Science+Business Media, Inc.Regulation of Proteolytic Activity of Pepsinin Mice by Rotating Electromagnetic FieldT. I. Subbotina, A. A. Khadartsev,M. A. Yashin, and A. A. YashinTranslated from Byulleten’ Eksperimental’noi Biologii i Meditsiny, Vol. 139, No. 3, pp. 294-296, March, 2005Original article submitted January 22, 2004In experiments on Wistar rats we studied the effect of low-frequency electromagnetic fieldrotating in either right-handed or a left-hande...

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    3160007-4888/05/1393?0316 © 2005 Springer Science+Business Media, Inc.Regulation of Proteolytic Activity of Pepsinin Mice by Rotating Electromagnetic FieldT. I. Subbotina, A. A. Khadartsev,M. A. Yashin, and A. A. YashinTranslated from Byulleten’ Eksperimental’noi Biologii i Meditsiny, Vol. 139, No. 3, pp. 294-296, March, 2005Original article submitted January 22, 2004In experiments on Wistar rats we studied the effect of low-frequency electromagnetic fieldrotating in either right-handed or a left-handed sense on proteolytic activity of pepsin. Theright-handed rotating field increased, while left-handed rotating field decreased pepsin acti-vity. Possible mechanisms of these changes in pepsin activity are discussed.Key Words: rotating electromagnetic field; pepsin; proteolytic activity; chiralityState Unitary Company, Institute of New Medical Technologies, Tula.Address for correspondence: niinmt@mednet.com. A. A. YashinRotating magnetic field (RMF) produces an informa-tional and phenomenological effect on the whole orga-nism. The effect of electromagnetic fields (EMF) onliving organisms depends on polarization of constitu-ting biological molecules (chirality) [2]. Proteolyticactivity of pepsin was measured under the influenceof magnetic field rotating in a right-handed or a left-handed sense (D- and L-chirality). The molecularstructure of pepsin is characterized by D-spatial sym-metry (right-handed sense).Inactive proenzyme pepsinogen is synthesized inchief cells of the gastric mucosa and secreted into thestomach. Pepsinogen is also present in other biologicalfluids (blood, urine, sperm, and cerebrospinal fluid).Pepsinogen biomolecule of has a molecular weight of42,500 and is stable at pH 6-7 [1].The terminal (inactive) part of pepsinogen con-tains 6 peptides with a molecular weight of 3100. Theactive site can be unblocked only in an acid medium.An inhibitor of the active site undergoes dissociationat pH<5.4 and is digested with active pepsin at pH 3.5-4.0. Pepsinogen is characterized by autocatalytic acti-vation.Secretion of pepsinogen is stimulated by choli-nergic fibers, vagus nerve, sympathetic fibers termi-nating in β-adrenoceptors, gastrin, histamine, secretin,and cholecystokinin. The enzymes secretin and chole-cystokinin directly stimulate pepsinogen synthesis.It can be hypothesized that RMF stimulates pep-sinogen secretion by the following mechanisms: in-crease in Ca2+ transport in cells, stimulation of Na+/K+-ATPase, stimulation of intracellular transport ofzymogene granules, activation of membrane phospho-lipase, increased release of zymogene granules fromcells, and activation of cGMP and cAMP.Gastrin acts as a stimulator of parietal cells. Gas-trin-mediated stimulation is followed by the release ofconsiderable amounts of gastric juice with high aci-dity. The enzyme gastrin is produced in the gastricmucosa. This polypeptide exists in 2 forms containing34 and 17 amino acids. “Short” gastrin is most potentin stimulating parietal cells. This compound increasesthe rate of HCl secretion by 8 times. In view of bio-chemical specificity, pepsin hydrolyzes only peptidebonds and is specific to optical configuration of aminoacid residues on either side of the hydrolyzed bond:Bulletin of Experimental Biology and Medicine, Vol. 139, No. 3, 2005 BIOPHYSICS AND BIOCHEMISTRY

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