The subcellular distribution of FK506 binding proteins in rat brain

1994 ◽  
Vol 22 (4) ◽  
pp. 412S-412S ◽  
Author(s):  
ABIGAIL R. CHARTERS ◽  
MASAKAZU KOBAYASHI ◽  
STEVE P. BUTCHER
Keyword(s):  
Rat Brain ◽  
Subcellular Distribution ◽  
Binding Proteins ◽  
Fk506 Binding Proteins

DEVELOPMENTAL EXPRESSION OF FK506 BINDING PROTEINS AND CALCINEURIN IN RAT BRAIN

1995 ◽  
Vol 23 (3) ◽  
pp. 422S-422S ◽  
Author(s):  
ABIGAIL R. CHARTERS ◽  
MASAKAZU KOBAYASHI ◽  
STEVE P. BUTCHER
Keyword(s):  
Rat Brain ◽  
Binding Proteins ◽  
Developmental Expression ◽  
Fk506 Binding Proteins

Immunochemical analysis of FK506 binding proteins in neuronal cell lines and rat brain

1994 ◽  
Vol 22 (4) ◽  
pp. 411S-411S ◽  
Author(s):  
ABIGAIL R. CHARTERS ◽  
MASAKAZU KOBAYASHI ◽  
STEVE P. BUTCHER
Keyword(s):  
Rat Brain ◽  
Cell Lines ◽  
Binding Proteins ◽  
Neuronal Cell ◽  
Immunochemical Analysis ◽  
Neuronal Cell Lines ◽  
Fk506 Binding Proteins

scholarly journals Characterization of GTP-binding proteins in Golgi-associated membrane vesicles from rat adipocytes

1992 ◽  
Vol 283 (3) ◽  
pp. 795-801 ◽  
Author(s):  
A Schürmann ◽  
W Rosenthal ◽  
G Schultz ◽  
H G Joost
Keyword(s):  
G Proteins ◽  
Glucose Transport ◽  
Subcellular Distribution ◽  
Sucrose Gradient ◽  
Binding Proteins ◽  
Glucose Transporters ◽  
Beta Subunits ◽  
Transport Activity ◽  
Gtp Binding Proteins ◽  
Gtp Binding

We have previously reported that guanine nucleotides inhibit glucose transport activity reconstituted from adipocyte membrane fractions. In order to further investigate the hypothetical involvement of guanine-nucleotide-binding proteins (GTP-binding proteins) in the regulation of insulin-sensitive glucose transport activity, we studied their subcellular distribution in adipocytes treated or not with insulin. Adipocytes were homogenized and fractionated to yield plasma membranes (PM) and a Golgi-enriched fraction of intracellular membranes (low-density microsomes, LDM). In these membrane fractions, total guanosine 5′-[gamma-[35S]thio]triphosphate ([35S]GTP[S]) binding, alpha- and beta-subunits of heterotrimeric G-proteins, proto-oncogenes Ha-ras and K-ras, and 23-28 kDa GTP-binding proteins were assayed. The levels of alpha s and alpha i (the alpha-subunits of Gs and Gi) were approx. 8-fold lower in LDM than in PM; beta-subunits, Ha-ras and K-ras were not detectable in LDM. Total GTP[S]-binding sites and 23-28 kDa GTP-binding proteins were present in LDM in approximately the same concentrations as in PM. Insulin gave rise to the characteristic translocation of glucose transporters, but failed to alter the subcellular distribution of any of the GTP-binding proteins. Fractionation of the LDM on a discontinuous sucrose gradient revealed that alpha s and alpha i, as detected with antiserum against a common peptide sequence (alpha common), and the bulk of the 23-28 kDa G-proteins sedimented at different sucrose densities. None of the GTP-binding proteins co-sedimented with glucose transporters. Furthermore, the inhibitory effect of GTP[S] on the reconstituted transport activity was lost in the peak fractions of glucose transporters partially purified on the sucrose gradient. These data indicate that LDM from adipocytes contain several GTP-binding proteins in discrete vesicle populations. However, the intracellular GTP-binding proteins are not tightly associated with the vesicles containing the glucose transporter.

scholarly journals Inhibition of FK506 Binding Proteins Reduces  -Synuclein Aggregation and Parkinson's Disease-Like Pathology

2010 ◽  
Vol 30 (7) ◽  
pp. 2454-2463 ◽  
Author(s):  
M. Gerard ◽  
A. Deleersnijder ◽  
V. Daniels ◽  
S. Schreurs ◽  
S. Munck ◽  
...  
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Binding Proteins ◽  
Fk506 Binding Proteins

scholarly journals Recombinant Protein Truncation Strategy for Inducing Bactericidal Antibodies to the Macrophage Infectivity Potentiator Protein of Neisseria meningitidis and Circumventing Potential Cross-Reactivity with Human FK506-Binding Proteins

2014 ◽  
Vol 83 (2) ◽  
pp. 730-742 ◽  
Author(s):  
Magdalena K. Bielecka ◽  
Nathalie Devos ◽  
Mélanie Gilbert ◽  
Miao-Chiu Hung ◽  
Vincent Weynants ◽  
...  
Keyword(s):  
Neisseria Meningitidis ◽  
Bactericidal Activity ◽  
Binding Proteins ◽  
Leader Peptide ◽  
Type I ◽  
Globular Domain ◽  
His Tag ◽  
Macrophage Infectivity Potentiator ◽  
Fk506 Binding Proteins ◽  
Macrophage Infectivity

A recombinant macrophage infectivity potentiator (rMIP) protein ofNeisseria meningitidisinduces significant serum bactericidal antibody production in mice and is a candidate meningococcal vaccine antigen. However, bioinformatics analysis of MIP showed some amino acid sequence similarity to human FK506-binding proteins (FKBPs) in residues 166 to 252 located in the globular domain of the protein. To circumvent the potential concern over generating antibodies that could recognize human proteins, we immunized mice with recombinant truncated type I rMIP proteins that lacked the globular domain and the signal leader peptide (LP) signal sequence (amino acids 1 to 22) and contained the His purification tag at either the N or C terminus (C-term). The immunogenicity of truncated rMIP proteins was compared to that of full (i.e., full-length) rMIP proteins (containing the globular domain) with either an N- or C-terminal His tag and with or without the LP sequence. By comparing the functional murine antibody responses to these various constructs, we determined that C-term His truncated rMIP (−LP) delivered in liposomes induced high levels of antibodies that bound to the surface of wild-type but not Δmipmutant meningococci and showed bactericidal activity against homologous type I MIP (median titers of 128 to 256) and heterologous type II and III (median titers of 256 to 512) strains, thereby providing at least 82% serogroup B strain coverage. In contrast, in constructs lacking the LP, placement of the His tag at the N terminus appeared to abrogate bactericidal activity. The strategy used in this study would obviate any potential concerns regarding the use of MIP antigens for inclusion in bacterial vaccines.

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