Literature DB >> 2424786

GTP gamma S-induced solubilization of actin and myosin from rabbit peritoneal neutrophil membrane.

C K Huang, J F Devanney.   

Abstract

Addition of guanosine 5'-(3-O-thio)triphosphate (GTP gamma S) to the membrane fraction isolated from rabbit peritoneal neutrophils results in the solubilization of several proteins from the membrane. The major proteins are of 180 kDa (myosin) and 43 kDa (actin). The effect is observed with a half-maximum GTP gamma S concentration of 70 microM. The potencies of various nucleotides are compared: GTP gamma S greater than GTP greater than ATP greater than GDP, GMP, cGMP, cAMP. The effect does not require calcium and is not inhibited by using membranes prepared from cells that have been pretreated with pertussis toxin.

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Year:  1986        PMID: 2424786     DOI: 10.1016/0014-5793(86)80645-7

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Octyl glucoside extracts GTP-binding regulatory proteins from rat brain "synaptoneurosomes" as large, polydisperse structures devoid of beta gamma complexes and sensitive to disaggregation by guanine nucleotides.

Authors:  S Nakamura; M Rodbell
Journal:  Proc Natl Acad Sci U S A       Date:  1990-08       Impact factor: 11.205

2.  Guanine nucleotides inhibit poly-L-arginine-induced membrane damage in polymorphonuclear leukocytes.

Authors:  J G Elferink
Journal:  Experientia       Date:  1988-12-01

3.  Guanine nucleotide-induced polymerization of actin in electropermeabilized human neutrophils.

Authors:  S Therrien; P H Naccache
Journal:  J Cell Biol       Date:  1989-09       Impact factor: 10.539

  3 in total

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