Amylase released from the parotid gland by pilocarpine elevates the enzyme activity in the submandibular and sublingual glands of rats

Stimulation by pilocarpine led to a marked increase in amylase activity in the submandibular and sublingual glands and serum, and resulted in a considerable depletion of the enzyme in the parotid gland and pancreas of rats. Parotidectomy reduced these pilocarpine effects. It is concluded that amylase released by pilocarpine from the parotid gland but not from the pancreas elevated the enzyme activity in the submandibular and sublingual glands.     

Inhibition of brain enolases by acrylamide and its related compounds in vitro, and the structure-activity relationship

Acrylamide and its related compounds inhibited brain enolases in vitro independently of their neurotoxicity. The inhibitory potency was a function of the binding constants of the compounds for phenylalanine. The binding constant for tryptophan was higher in neurotoxic compounds than in non-neurotoxic ones.     

A small chimerically bifunctional monomeric protein: <Emphasis Type="Italic">Tapes japonica</Emphasis> lysozyme

The lysozyme of the marine bilave Tapes japonica (13.8 kDa) is a novel protein. The protein has 46% homology with the destabilase from medicinal leech that has isopeptidase activity. Based on these data, we confirmed hydrolysis activity of T. japonica lysozyme against three substrates: L--Glu-pNA, D--Glu-pNA, and -(-Glu)-L-Lys. The optimal pH of chitinase and isopeptidase activity was 5.0 and 7.0, respectively. The isopeptidase activity was inhibited with serine protease inhibitor, but the lytic and chitinase activities were not. Moreover, only isopeptidase activity is decreased by lyophilization, but lytic and chitinase activities were not. We conclude that T. japonica lysozyme expresses isopeptidase and chitinase activity at different active sites.Received 25 February 2003; received after revision 29 May 2003; accepted 12 June 2003     

Irreversible inhibition of Ca2+ release in saponin-treated macrophages by the photoaffinity derivative of inositol-1, 4, 5-trisphosphate

D-myo-inositol-1,4,5-trisphosphate (InsP3) is a putative intracellular second messenger for the mobilization of Ca2+ from intracellular stores, in particular, the endoplasmic reticulum. Specific binding sites on the endoplasmic reticulum may participate in the InsP3-induced release of Ca2+ from the Ca2+ pool. To examine the specific binding sites on the endoplasmic reticulum, we synthesized an arylazide derivative of InsP3 for photoaffinity labelling; InsP3 coupled to p-azidobenzoic acid (InsP3-pAB) using N,N'-carbonyldiimidazole (CDI) was obtained at a 9-11% yield. Here, we report that InsP3-pAB, but not an arylazide derivative of inositol-1,4-bisphophate (Ins(1,4)P2), causes the irreversible inhibition of InsP3-induced release of Ca2+ in saponin-permeabilized photo-irradiated macrophages. The irreversible inhibition by InsP3-pAB after photo-irradiation was prevented by a 10-fold excess of unmodified InsP3.     

An alkaline protease in the delayed hypersensitivity skin lesions in the guinea-pigs.

An alkaline hemoglobinolytic protease was extracted from the delayed hypersensitivity skin lesions induced by bovine gamma-globulin as an antigen in the guinea-pig. The enzyme was heat-labile and inhibited by thiol-blocking reagents. The mol.wt. was more than 100,000 and optimal pH around 9.     

(+)-Curcuphenol and dehydrocurcuphenol, novel sesquiterpenes which inhibit H,K-ATPase, from a marine sponge Epipolasis sp

Two H,K-ATPase inhibitors and an inactive related compound have been isolated from a marine sponge Epipolasis sp. They are aromatic sesquiterpene alpha-curcumenes.     

Synsthesis and RES-stimulating activity of bacterial cell-wall peptidoglycan peptides related to FK-156

Summary The bacterial cell-wall peptidoglycan peptides and related compounds coupled with some fatty acids were synthesized, and their immunostimulating property was examined by carbon clearance assay. All the new compounds (2–6) proved to possess significant potencies superior to that of FK-156 (1).Acknowledgment. We are grateful to Dr J. Mori and his coworkers for the biological assays.