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D B Rylatt

Publications and source records attributed to D B Rylatt.

49 records · Page 3Linked to original sources
PubMed1982

Anti-self receptors. V. Properties of a mouse serum factor that blocks autorosetting receptors on lymphocytes.

Murine lymphocytes spontaneously bind autologous and allogeneic erythrocytes via receptors that primarily recognize self H-2L molecules on the erythrocyte surface. Normal mouse serum contains a factor, termed autorosette inhibition factor (AIF), that very effectively blocks autorosette formation. This paper describes experiments that determine the origin and nature of serum AIF. It was found that AIF lacks strain and species specificity, serum from several mammalian and non-mammalian species inhibiting the autorosetting of BALB/c thymocytes. However, mouse strains differed in the levels of AIF in their serum. Furthermore, AIF appears to directly interact with autorosetting receptors on lymphocytes as thymocytes from the BALB/c-H-2dm2 mutant strain, which lack autorosetting receptors, were unable to absorb the factor. Several lines of experimental evidence indicated that AIF is secreted by a population of short-lived, radiosensitive macrophages (or monocytes). Firstly, in vivo administration of the anti-macrophage agents carrageenan and silica profoundly depressed AIF levels in serum. Secondly, in vitro culturing of different lymphoid cells revealed that AIF is secreted by an adherent population of peritoneal cells. Thirdly, total body irradiation experiments demonstrated that AIF production is dependent upon a radiosensitive cell that is bone marrow derived. Finally, AIF was purified to homogeneity from mouse plasma and shown to be a single polypeptide chain with a molecular weight of 84,000.

Aging↗
PubMed1980

Glycogen synthase from rabbit skeletal muscle. Amino acid sequence at the sites phosphorylated by glycogen synthase kinase-3, and extension of the N-terminal sequence containing the site phosphorylated by phosphorylase kinase.

Glycogen synthase kinase-3 phosphorylates three serine residues on glycogen synthase (sites 3a, 3b and 3c) which are all located in the same nine-amino-acid segment of the polypeptide chain. The sequence in this region is: Arg-Tyr-Pro-Arg-Pro-Ala-Ser(P)-Val-Pro-Pro-Ser(P)-Pro-Ser-Leu-Ser(P)-Arg-. These serine residues are distinct from the sites phosphorylated preferentially by cyclic-AMP-dependent protein kinase (sites 1a and 1b) and phosphorylase kinase (site 2). The N-terminal sequence of glycogen synthase containing the serine residue phosphorylated by phosphorylase kinase has been extended. The sequence in this region is: Pro-Leu-Ser-Arg-Thr-Leu-Ser(P)-Val-Ser-Ser-Leu-Pro-Gly-Leu-Glu-Asp-Trp-Glu-Asp- Glu-Phe-Asp-Leu-Glu-Asn-Ser-Val-Leu-Phe-(Asx2,Glx2,Ala2,Val2,Lys)-. The similarity to the N-terminal sequence of phosphorylase is confined to the immediate vicinity of the phosphorylation site (residues 4--15). The relationship of glycogen synthase kinase-3 to glycogen synthase kinases that have been described by other laboratories is discussed.

Amino Acid Sequence↗