Detail of "4289-98-9"

Reference

Chemiluminescence of phagocytic cells caused by N-formylmethionyl peptides

Chemiluminescence of phagocytic cells caused by N-formylmethionyl peptides. Hatch, Gary E.; Gardner, Donald E.; Menzel, Daniel B. (Dep. Pharmacol. Med., Duke Univ., Durham, N. C., USA). J. Exp. Med., 147(1), 182-95 (English) 1978. CODEN: JEMEAV. ISSN: 0022-1007. DOCUMENT TYPE: Journal CA Section: 3 (Biochemical Interactions) Section cross-reference(s): 15 N-formylmethionyl (F-Met) peptides, when added alone to macrophages or polymorphonuclear leukocytes (PMN), induced a chemiluminescent response of shorter duration than that produced by the commonly employed particulate stimulant, zymosan. The cellular nature of F-Met peptide-induced chemiluminescence was indicated by its dependence on cell concn., and by its inhibition by cell disruption, heat inactivation, or previous maximal stimulation by the peptides. Comparison of PMN and macrophages from different species showed that the maximal chemiluminescent response seen in the dose-response curve of F-Met-Phe [22008-60-2] was different in different cell types. Chemiluminescence reached highest values in human PMN, it was intermediate in guinea pig macrophages and PMN, and in rabbit PMN; but it was nonexistent in rabbit alveolar macrophages and very low in rabbit peritoneal macrophages. A definite relation was obsd. between peptide structure and chemiluminescent activity. Met-Phe [14492-14-9], F-Met [4289-98-9] and phenylalanine [63-91-2] were inactive even at millimolar concns., whereas F-Met-Phe caused chemiluminescence at micromolar concns. Four active peptides were tested in guinea pig, rabbit, and human PMN, and in guinea pig alveolar and peritoneal macrophages. The relative activity of these peptides was the same in all cells studied, e.g. F-Met-Leu-Phe [59880-97-6] ? F-Met-Phe > F-Met-Val [29790-45-2] > F-Met-Ala [15183-28-5]. Low concns. of superoxide dismutase (10 mg/mL) completely inhibited chemiluminescence caused by the F-Met peptides, suggesting the involvement of O2- or O2--derived compds. in this response. NaN3, an inhibitor of peroxidase reactions, had either no effect or a slight inhibitory effect on chemiluminescence. However, when the extracellular release of lysosomal enzymes was induced by cytochalasin B, an azide-inhibitable enhancement of chemiluminescence was seen in PMN, but not in macrophages. Apparently the F-Met-peptides stimulate O2- prodn. in addn. to stimulating lysosomal enzyme release and chemotaxis. The similar structure-activity relation which appears to exist for these processes may indicate that they are all initiated by a single receptor mechanism. Since F-Met peptides are formed in bacteria it is likely that their actions represent an important physiologic response.

Biosynthesis of reovirus-specified polypeptides

Biosynthesis of reovirus-specified polypeptides. Initiation of reovirus messenger RNA translation in vitro and identification of methionyl-X initiation peptides. Samuel, Charles E.; Joklik, Wolfgang K. (Dep. Biol. Sci., Univ.Chemical with cas number 4289-98-9 also plays role. California, Santa Barbara, Calif., USA). Virology, 74(2), 403-13 (English) 1976. CODEN: VIRLAX. DOCUMENT TYPE: Journal CA Section: 6 (General Biochemistry) The initiation of reovirus mRNA-directed protein synthesis in vitro was investigated in a cell-free protein-synthesizing system prepd. from Krebs ascites tumor cells. The principal translation products of the mixt. of 10 reovirus mRNA species transcribed in vitro by reovirus cores were polypeptides .mu.0, .mu.1, .sigma.2a, and .sigma.3. Translation was initiated with formylmethionine transferred from rat liver methionyl-tRNA formylated by Escherichia coli formyltransferase with 10-formyltetrahydrofolate as the formyl donor. Formylmethionine incorporation was complete within 10-15 min and was inhibited by aurin tricarboxylic acid and pactamycin; by contrast, incorporation of methionine and leucine continued for 30-60 min. The following N-terminal amino acids of the polypeptides synthesized in vitro were elucidated: .mu.0, (N-formyl)methionyl-valyl-(proline); .mu.1, (N-formyl)methionyl-leucyl-valine; .sigma.2a, (N-formyl)methionyl-threonyl-valine; and .sigma.3, (N-formyl)methionyl-valyl-tyrosyl-(proline). No evidence was obtained for N-terminal acetylation or formylation of reovirus-specific protein synthesized in vitro in the absence of exogenously added formylmethionyl-tRNA. .