Transfer Factor
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- Published in 1988
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Record 1 from database: MEDLINE
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- Title
- Murine transfer factor. IV. Studies with genetically regulated immune
responses.
- Author
- Rozzo SJ; Merryman CF; Kirkpatrick CH
- Address
- Conrad D. Stephenson Laboratory, National Jewish Center for Immunology and
Respiratory Medicine, Denver, Colorado 80206.
- Source
- Cell Immunol, 1988 Aug, 115:1, 130-45
- Abstract
- Transfer factor-containing dialysates from mice that were either high or low
responders to GAT10, GLA5, or ovalbumin were assayed for their ability to
transfer delayed hypersensitivity to murine recipients of either high or low
responder phenotype. Dialysates from high responder strains contained transfer
factor that would transfer delayed hypersensitivity to both high and low
responder recipients. These transfers were not restricted by disparities at the
MHC or Igh loci. Identically prepared materials from low responder donors
contained little or no transfer factor activity and would not transfer delayed
hypersensitivity to either high or low responder recipients. Thus,
administration of transfer factor transfers the high responder phenotype to low
responder recipients. The data also suggest that production of transfer factor
is regulated by Ir genes but that the immunologic activities of transfer factor
are not.
- Language of Publication
- English
- Unique Identifier
- 88295138
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- MeSH Heading (Major)
- Hypersensitivity, Delayed|ET/*GE/IM; Transfer Factor|*/AD/BI/GE
- MeSH Heading
- Animal; Carrier Proteins|IM; Dialysis; Dose-Response Relationship,
Immunologic; H-2 Antigens|GE; Mice; Mice, Inbred BALB C; Mice, Inbred CBA; Mice,
Inbred C57BL; Peptides|IM; Serum Albumin, Bovine|IM; Species Specificity;
Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0008-8749
- Country of Publication
- UNITED STATES
Record 2 from database: MEDLINE
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- Title
- Transfer factor.
- Author
- Kirkpatrick CH
- Address
- Conrad D. Stephenson Laboratory, National Jewish Center for Immunology and
Respiratory Medicine, Denver, CO 80206.
- Source
- J Allergy Clin Immunol, 1988 May, 81:5 Pt 1, 803-13
- Abstract
- It has been more than 30 years since Dr. H. S. Lawrence first reported that
it was possible to transfer delayed-type hypersensitivity from sensitized donors
to unsensitized recipients with lysates of blood leukocytes. During recent
years, research from several laboratories has demonstrated that this effect is
immunologically specific. Although the molecules that possess this activity have
not been completely characterized, there is a significant body of evidence that
they are small polypeptides and that they can interact with antigen molecules in
an immunologically specific manner. Studies with immune responses that are under
genetic control have demonstrated that the ability of an animal to produce
transfer factor is genetically regulated but that transfer of delayed
hypersensitivity with transfer factor is not genetically restricted. In fact,
when mice of low-responder phenotypes are administered transfer factor from
high-responder donors, they express delayed hypersensitivity responses that are
comparable to the high responders. Clinical studies have demonstrated that
transfer factor is an efficacious method for immunotherapy of certain viral and
fungal infections.
- Language of Publication
- English
- Unique Identifier
- 88228780
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- MeSH Heading (Major)
- Transfer Factor|*/IM/TU
- MeSH Heading
- Animal; Human; Hypersensitivity, Delayed|IM; Mice; Support, Non-U.S. Gov't;
Support, U.S. Gov't, P.H.S.
- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0091-6749
- Country of Publication
- UNITED STATES
Record 3 from database: MEDLINE
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- Title
- De novo initiation of specific cell-mediated immune responsiveness in
chickens by transfer factor (specific immunity inducer) obtained from bovine
colostrum and milk.
- Author
- Wilson GB; Poindexter C; Fort JD; Ludden KD
- Address
- Amtron, Inc., Charleston, South Carolina.
- Source
- Acta Virol, 1988 Jan, 32:1, 6-18
- Abstract
- Transfer factors (TF) were prepared from colostrum and milk of bovines
previously immunized with antigens obtained from Coccidioides immitis,
infectious bovine rhinotracheitis virus, or from the viral agents responsible
for avian Newcastle disease, laryngotracheitis disease or infectious bursal
disease. The ability of bovine TF to transfer specific cell-mediated immune
responsiveness to a markedly xenogenic species was studied using specific
pathogen free (SPF) and standard commercial (SC) chickens as model recipients.
Cell-mediated immune responsiveness was documented using one or more of the
following for each antigen (organism) studied: (a) an in vitro chicken leukocyte
(heterophil) migration inhibition assay; (b) delayed-wattle reactivity; or (c)
protection from clinical disease. Chicken TFs obtained from spleens of immune
donors were evaluated in parallel to bovine TF's in selected comparative
studies. Bovine TF also referred to as specific immunity inducer (SII), and
chicken TF were found to initiate antigen-specific cell-mediated immunity de
novo in previously non-immune SPF chickens as well as in SC chickens despite the
presence of maternally acquired humoral antibody which may serve as a "barrier"
to immunization of SC chickens when commercially available vaccines are
administered by parenteral routes. Bovine TF's specific for laryngotracheitis
virus or infectious bursal disease virus afforded protection equal to that found
for commercially available vaccines. Bovine TF's action was rapid (less than a
day) and of relatively long duration at least 35 days.
- Language of Publication
- English
- Unique Identifier
- 88238284
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- MeSH Heading (Major)
- Immunity, Cellular|*; Transfer Factor|BI/IP/*PD
- MeSH Heading
- Animal; Antigens, Viral|IM; Cattle; Chickens; Colostrum|IM; Female;
Herpesvirus 1, Gallid|IM; Immunization; Infectious Bursal Disease Virus|IM;
Male; Milk|IM; Newcastle Disease Virus|IM; Pregnancy; Species Specificity
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0001-723X
- Country of Publication
- CZECHOSLOVAKIA
Record 4 from database: MEDLINE
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- Title
- Chromatographic and enzymatic effects on transfer factor-like activity from
human leukocytes and porcine spleen dialysate.
- Author
- Karhumäki E; Marnela KM; Krohn K
- Address
- Institute of Biomedical Sciences, University of Tampere, Finland.
- Source
- Int J Biochem, 1988, 20:10, 1067-72
- Abstract
- 1. The effect of dialysable transfer factor (TFd), derived from human
leukocytes or porcine spleen cells, was measured using Listeria resistance in
mice. 2. The molecular weight range of substance(s) containing TF-like activity
is in the less than 3500 MW dialysis fraction on the basis of the capacity of
peritoneal macrophages to produce superoxide anion (O2-). This biological
activity is removed by heating at 56 degrees C. 3. After Sephadex G-10
chromatography of dialysates the significant activities are found in fractions
III and IV of human leukocyte dialysate and in fractions of II and III of
porcine spleen dialysate. 4. From enzymatic studies, most of the protective
activity of both human leukocyte and porcine spleen dialysate is based on the
action of small-molecular weight structures containing peptides and/or
polynucleotides.
- Language of Publication
- English
- Unique Identifier
- 89252383
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- MeSH Heading (Major)
- Leukocytes|*AN; Spleen|*AN; Transfer Factor|*IP/PD
- MeSH Heading
- Animal; Chromatography, Gel; Dialysis|MT; Drug Resistance, Microbial|DE;
Enzymes; Heat; Human; Listeria|DE; Listeria Infections|PC; Mice; Molecular
Weight; Support, Non-U.S. Gov't; Swine
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0020-711X
- Country of Publication
- ENGLAND
Record 5 from database: MEDLINE
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- Title
- Transfer factor in Hodgkin's disease: a randomized clinical and
immunological study.
- Author
- Hancock BW; Bruce L; Sokol RJ; Clark A
- Address
- University Department of Medicine, Royal Hallamshire Hospital, Sheffield,
U.K.
- Source
- Eur J Cancer Clin Oncol, 1988 May, 24:5, 929-33
- Abstract
- Transfer factor (TF) was prepared from buffy coats obtained from 493 units
of blood taken from healthy donors, including individuals convalescent from
various viral infections. It was administered to 22 of 47 patients with
Hodgkin's disease undergoing treatment and consenting to take part in this
randomized study to determine if TF would enhance their immunity and/or reduce
the incidence of subsequent infections. Skin test reactivity was markedly
enhanced in those patients receiving TF as opposed to placebo but other
immunological assessments showed no significant differences between the groups.
TF was not shown to be of benefit in the prevention of infections (including
varicella/zoster).
- Language of Publication
- English
- Unique Identifier
- 89005279
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- MeSH Heading (Major)
- Hodgkin Disease|*IM; Transfer Factor|*TU
- MeSH Heading
- B-Lymphocytes|IM; Blood Cell Count; Cell Migration Inhibition;
Chickenpox|PC; Clinical Trials; Double-Blind Method; Human; Immunity, Cellular;
Immunoglobulins|AN; Leukocytes|IM; Lymphocyte Transformation; Receptors, Fc|AN;
Support, Non-U.S. Gov't; T-Lymphocytes|IM
- Publication Type
- CLINICAL TRIAL; JOURNAL ARTICLE; RANDOMIZED CONTROLLED TRIAL
- ISSN
- 0277-5379
- Country of Publication
- ENGLAND
Record 6 from database: MEDLINE
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- Title
- Varicella-zoster virus IgG antibodies during primoinfection in competent and
transfer factor modulated immunocompromised host: comparison of three indirect
assays.
- Author
- Zachar V; Mayer V; Schmidtmayerová H
- Address
- Institute of Virology, Slovak Academy of Sciences, Bratislaya,
Czechoslovakia.
- Source
- Acta Virol, 1988 May, 32:3, 243-51
- Abstract
- Ten patients with acute leukaemia and next three with Hodgkin's or
non-Hodgkin's lymphoma, suffering from varicella-zoster-virus (VZV)
primoinfection, were given 1 to 2 doses of ultrafiltrate of the human leukocytes
lysate (LLU) containing transfer factor (TF) activity (1 dose being equivalent
to the product of 10(8) leukocytes). Only LLU administered to patients with
acute lymphocytic leukaemia (ALL) at early phases of the illness (days 1 and 2)
displayed a notable benefit on the clinical course of varicella. No influence
upon the infection, on the other hand, was observed following LLU administration
to subjects with lymphoma. The convalescent levels of IgG antibodies to VZV, as
detected by indirect immunoperoxidase assay to membrane antigen (IPAMA),
demonstrated no significant difference between infected competent and
immunocompromised untreated and LLU treated individuals. The performance
characteristics of IPAMA are compared with indirect immunofluorescence method
(IFA) and non-competitive enzyme-linked immunosorbent assay (ELISA) on the same
panel of specimens.
- Language of Publication
- English
- Unique Identifier
- 89022589
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- MeSH Heading (Major)
- Antibodies, Viral|*AN; Chickenpox|ET/*IM/TH; Herpesvirus 3, Human|*IM
- MeSH Heading
- Comparative Study; Enzyme-Linked Immunosorbent Assay; Fluorescent Antibody
Technique; Human; IgG|AN; Immunoenzyme Techniques; Leukemia|CO; Lymphoma|CO;
Transfer Factor|TU
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0001-723X
- Country of Publication
- CZECHOSLOVAKIA
Record 7 from database: MEDLINE
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- Title
- A randomized, double-blind, placebo-controlled trial of transfer factor as
adjuvant therapy for malignant melanoma.
- Author
- Miller LL; Spitler LE; Allen RE; Minor DR
- Address
- Paul M. Aggelar Memorial Laboratory, Children's Hospital of San Francisco,
California.
- Source
- Cancer, 1988 Apr, 61:8, 1543-9
- Abstract
- One hundred and sixty-eight evaluable patients participated in a randomized,
double-blind study of transfer factor (TF) versus placebo as surgical adjuvant
therapy of Stage I and Stage II malignant melanoma. Eighty-five patients
received TF prepared from the leukocytes of healthy volunteer donors;
eighty-three participants received placebo. Therapy was initiated within 90 days
of resection of all evident tumor and continued until 2 years of disease-free
survival or the occurrence of unresectable dissemination of melanoma. Known
prognostic variables were similarly distributed in the treatment and control
groups, documenting the randomization efficacy. Three endpoints were analyzed:
disease-free interval, time to Stage III metastasis, and survival. After a
median follow-up period of 24.75 months, there was a trend in favor of the
placebo group with regard to all three endpoints and this was significant (P
less than or equal to 0.05) for time to Stage III metastasis. These findings
indicate that TF is not effective as surgical adjuvant therapy of malignant
melanoma.
- Language of Publication
- English
- Unique Identifier
- 88164707
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- MeSH Heading (Major)
- Melanoma|SU/*TH; Transfer Factor|*TU
- MeSH Heading
- Clinical Trials; Combined Modality Therapy; Double-Blind Method; Human;
Random Allocation; Support, Non-U.S. Gov't
- Publication Type
- CLINICAL TRIAL; JOURNAL ARTICLE; RANDOMIZED CONTROLLED TRIAL
- ISSN
- 0008-543X
- Country of Publication
- UNITED STATES
Record 8 from database: MEDLINE
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- Title
- Evidence for protein-catalyzed transfer of platelet activating factor by
macrophage cytosol.
- Author
- Banks JB; Wykle RL; OFlaherty JT; Lumb RH
- Address
- Biochemistry Group, Western Carolina University, Cullowhee, NC 28723.
- Source
- Biochim Biophys Acta, 1988 Jul, 961:1, 48-52
- Abstract
- Platelet activating factor (PAF) is a potent, proinflammatory lipid. PAF is
synthesized in response to stimuli and is rapidly destroyed by specific
acetylhydrolases. In order to express its biological activity, PAF and its
metabolites are transported among subcellular membranes by as yet unexplained
mechanisms. We report here an assay system using methylcarbamyl-PAF (CPAF,
1-O-hexadecyl-2-O-(N-methylcarbamyl)-sn-glycero-3-phosphocholine) and a
vesicle-extrusion technique for examining protein-catalyzed intermembrane
transfer of CPAF, and demonstrate the presence of proteins catalyzing the
separate transfer of CPAF and diacyl phosphatidylcholine in macrophage cytosol.
The CPAF transfer activity is heat- and trypsin-sensitive and elutes from
gel-filtration columns well separated from proteins catalyzing the transfer of
phosphatidylcholine.
- Language of Publication
- English
- Unique Identifier
- 88252202
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- MeSH Heading (Major)
- Macrophages|*ME; Phospholipid Ethers|*ME; Platelet Activating Factor|*ME;
Proteins|*ME
- MeSH Heading
- Animal; Biological Transport; Cattle; Cytosol|ME; Intracellular
Membranes|ME; Kinetics; Organ Specificity; Rabbits; Support, U.S. Gov't, P.H.S.
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0006-3002
- Country of Publication
- NETHERLANDS
Record 9 from database: MEDLINE
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- Title
- Affinity labeling at the A-site of Escherichia coli ribosomes by a
non-hydrolyzable gamma-amide analog of GTP.
- Author
- Babkina GT; Jonák J; Karpova GG; Knorre DG; Rychlík I; Vladimirov SN
- Address
- Institute of Bioorganic Chemistry, Siberian Division of the Academy of
Sciences, Novosibirsk, U.S.S.R.
- Source
- Biochimie, 1988 May, 70:5, 597-603
- Abstract
- gamma-Amides of GTP and affinity and photoaffinity derivatives of
gamma-amides of GTP: gamma-anilide of GTP, gamma-(4-azido)anilide of GTP,
gamma-[N-(4-azidobenzyl)-N-methyl]amide of GTP,
gamma[4-N-(2-chloroethyl)-N-methylaminobenzyl]amide of GTP and
gamma-[4-N-(2-oxoethyl)-N-methylaminobenzyl]amide of GTP substituted efficiently
for GTP in the EF-Tu-dependent transfer of aminoacyl-tRNA to the ribosome but,
in contrast to GTP, they were not hydrolyzed in this process. They represent a
new class of non-hydrolyzable GTP analogs with preserved gamma-phosphodiester
bond. The radioactive analog of GTP:
gamma-[4-N-(2-chloroethyl)-N-methylamino[14C]benzyl]amide of GTP was used as an
affinity labeling probe for the identification of components of the GTPase
center formed in the EF-Tu-dependent transfer reaction of aminoacyl-tRNA to the
ribosomal A-site. Within a six-component complex of poly(U)-programmed E. coli
ribosomes with elongation factor Tu, Phe-tRNA(Phe) (at the A-site), tRNA(Phe)
(at the P-site) and the [14C]GTP analog, mainly the ribosomal 23S RNA and to a
lesser extent the ribosomal proteins L17, L21, S16, S21 and the ribosomal 16S
RNA were labeled by the reagent. No significant modification of EF-Tu was
detected.
- Language of Publication
- English
- Unique Identifier
- 89000961
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- MeSH Heading (Major)
- Affinity Labels|*ME; Escherichia coli|*ME; Guanosine Triphosphate|*AA/ME;
Ribosomes|*ME
- MeSH Heading
- Amides|ME; Binding Sites; GTP Phosphohydrolase|ME; Hydrolysis; Peptide
Elongation Factor Tu|PH; Peptides|BI; Photochemistry; RNA, Transfer, Amino
Acyl|ME
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0300-9084
- Country of Publication
- FRANCE
Record 10 from database: MEDLINE
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- Title
- Fluorescent modification of the cysteine 202 residue of Escherichia coli
transcription termination factor rho.
- Author
- Seifried SE; Wang Y; von Hippel PH
- Address
- Institute of Molecular Biology, University of Oregon, Eugene 97403.
- Source
- J Biol Chem, 1988 Sep, 263:27, 13511-4
- Abstract
- The lone cysteine residue (Cys-202) of transcription termination factor rho
has been modified with the sulfhydryl-specific dyes 5-iodoacetamidofluorescein
and 5-(2-[iodoacetyl)amino)ethyl)aminonaphthalene-1-sulfonic acid. Labeling with
both dyes is specific for the Cys-202 residue and is at least 90% complete. Rho
protein is an RNA-dependent ATPase and exists as a hexamer of identical subunits
in its activated (RNA-liganded) form. We find that chemical modification of rho
at Cys-202 does not significantly change the properties of the protein; subunit
assembly, RNA binding, and poly(rC)-activated ATP hydrolysis are all relatively
unperturbed by the covalent attachment of these fluorescent moieties. On the
other hand, the spectral, quenching, and anisotropy properties of the
fluorescent groups are all significantly modified by attachment to the protein.
No energy transfer is seen between fluorescein-labeled subunits within rho
hexamers, indicating that the Cys-202 residues on these subunits are located at
least 40 A apart. These fluorescently labeled rho molecules should represent
useful probes to study the conformations and inter- and intrasubunit geometries
of this termination factor at various stages of its interaction with nascent RNA
transcripts.
- Language of Publication
- English
- Unique Identifier
- 88330870
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- MeSH Heading (Major)
- Cysteine|*; Escherichia coli|*AN; Fluorescent Dyes|*; Rho Factor|*/ME/PD;
Transcription Factors|*/ME/PD
- MeSH Heading
- Adenosinetriphosphatase|ME; Chemistry; Cross-Linking Reagents; Energy
Transfer; Fluoresceins; Macromolecular Systems; Naphthalenesulfonates; RNA|ME;
Spectrophotometry; Sulfhydryl Reagents; Support, U.S. Gov't, P.H.S.;
Transcription, Genetic|DE
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0021-9258
- Country of Publication
- UNITED STATES
Record 11 from database: MEDLINE
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- Title
- Adult chronic granulomatosis disease-like neutrophil granulocyte disorder
corrected by dialysable leukocyte extract.
- Author
- Lukács K; Szabó G; Schröder I; Szegedi G
- Address
- 3rd Department of Medicine, University Medical School, Debrechen, Hungary.
- Source
- Allergol Immunopathol (Madr), 1988 Mar, 16:2, 121-5
- Abstract
- A 47 year old female presented with a septic clinical picture including
fever, abscesses, late cachexia, and unmanageable by disease. Similar
characteristics to chronic granulomatosis disease (CGD) seriously decreased
intracellular killing activity and chemiluminescence, granulomas in the
histology, and the role of genetic factors were found, suggesting that our case
is CGD-like disorder, manifested in an adult. Dialysable leukocyte extract (DLE)
therapy, complemented with fresh normal plasma, resulted in a striking clinical
improvement and there was an increase in the in vitro PMNL intracellular killing
activity, too. Although it is generally accepted that DLE derives from monocytes
and lymphocytes, it is possible that DLE is a family of DNA-oligopeptide
molecules, including factors derived from PMNLs which are capable of influencing
PMNL function, transferring information from normal cells. Our results also
suggest that it would be worth trying DLE in patients with classic CGD.
- Language of Publication
- English
- Unique Identifier
- 88279301
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- MeSH Heading (Major)
- Neutrophils|IM/*PA; Phagocyte Bactericidal Dysfunction|CO/*TH; Transfer
Factor|IP/*TU
- MeSH Heading
- Abscess|ET; Case Report; Chemotaxis, Leukocyte; Female; Human;
Leukocytes|AN; Middle Age; Phagocytosis; Rosette Formation
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0301-0546
- Country of Publication
- SPAIN
Record 12 from database: MEDLINE
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- Title
- Growth factors modulate junctional cell-to-cell communication.
- Author
- Maldonado PE; Rose B; Loewenstein WR
- Address
- Department of Physiology and Biophysics, University of Miami School of
Medicine, Florida 33101.
- Source
- J Membr Biol, 1988 Dec, 106:3, 203-10
- Abstract
- The epidermal growth factor (EGF) and the platelet-derived growth factor
(PDGF) inhibit gap junctional communication in the mammalian cell lines NRK and
BalbC 3T3: cell-to-cell transfer of a 400-dalton tracer molecule is reduced and
junctional conductance is reduced. The inhibition of cell-to-cell transfer is
reversible and dose dependent; half-maximal effects are obtained at 10(-9) and
10(-11) M concentrations of EGF and PDGF, respectively. The response of
junctional conductance is detectable within 2 min of EGF application and reaches
a maximum within 10 min. It is among the earliest cellular responses to this
growth factor and may be significant in the regulation of growth. The response
is lacking in EGF receptor-deficient NIH 3T3 cells. The transforming factor beta
(TGF beta) enhances junctional communication in BalbC 3T3: cell-to-cell transfer
is increased over a period of 8 hr. But in NRK cells, where it upregulates EGF
receptors, TGF beta reduces junctional communication synergistically with EGF.
- Language of Publication
- English
- Unique Identifier
- 89216868
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- MeSH Heading (Major)
- Cell Communication|*; Growth Substances|*PH; Intercellular Junctions|*PH
- MeSH Heading
- Animal; Cell Membrane Permeability; Cells, Cultured; Mice; Microelectrodes;
Platelet-Derived Growth Factor; Rats; Receptors, Cell Surface|PH; Receptors,
Epidermal Growth Factor-Urogastrone|PH; Support, U.S. Gov't, P.H.S.;
Transforming Growth Factors|PH
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0022-2631
- Country of Publication
- UNITED STATES
Record 13 from database: MEDLINE
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- Title
- The elongation factor EF-Tu from E. coli binds to the upstream activator
region of the tRNA-tufB operon.
- Author
- Vijgenboom E; Nilsson L; Bosch L
- Address
- Department of Biochemistry, University of Leiden, The Netherlands.
- Source
- Nucleic Acids Res, 1988 Nov, 16:21, 10183-97
- Abstract
- The polypeptide chain elongation factor EF-Tu of Escherichia coli is encoded
by two genes, tufA and tufB, located in two different operons. Experiments in
which either tufA or tufB was inactivated demonstrated that expression of the
tRNA-tufB operon is dependent on a functioning tufA and thus on EF-Tu (1, to be
published). In order to study a possible role of EF-Tu as trans-activator of the
tRNA-tufB operon, we have investigated in vitro binding of an EF-Tu. GDP
preparation to various DNA fragments of the operon. We demonstrate that specific
binding occurs to a cis-acting region delimited from position -134 to the
promoter, previously shown to enhance tufB transcription. Electrophoretic
retardation assays reveal the formation of maximally three protein/DNA
complexes, indicating that more than one protein molecule can bind to the DNA.
The EF-Tu preparation used was obtained by affinity chromatography and appeared
to be 95% pure. It lost its DNA binding activity upon further purification. That
EF-Tu is nonetheless involved in the DNA binding is suggested by the observation
that none of the three complexes is formed in the presence of kirromycin, an
antibiotic that binds EF-Tu with high specificity. If so, EF-Tu.GDP most likely
binds to the activator region of the tRNA-tufB operon in combination with
another non-identified protein or component.
- Language of Publication
- English
- Unique Identifier
- 89057457
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- MeSH Heading (Major)
- Escherichia coli|*GE/ME; Gene Expression Regulation|*; Genes, Bacterial|*;
Genes, Structural|*; Operon|*; Peptide Elongation Factor Tu|*GE/ME; RNA,
Transfer|*GE
- MeSH Heading
- DNA, Bacterial|GE/ME; Kinetics; Support, Non-U.S. Gov't
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0305-1048
- Country of Publication
- ENGLAND
Record 14 from database: MEDLINE
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- Title
- Transfer of functional EGF receptors to an IL3-dependent cell line.
- Author
- Collins MK; Downward J; Miyajima A; Maruyama K; Arai K; Mulligan RC
- Address
- Whitehead Institute, Cambridge, Massachusetts 02142.
- Source
- J Cell Physiol, 1988 Nov, 137:2, 293-8
- Abstract
- Epidermal growth factor (EGF) is a small protein that acts as a mitogen for
various epidermal, epithelial, and fibroblastic cells that bear specific EGF
receptors. The molecule that binds EGF is a 175-kD transmembrane protein, with
an extracellular ligand binding domain and an intracellular domain that
possesses tyrosine kinase activity, thought to be involved in the mitogenic
signalling process. Here we have constructed a recombinant murine retrovirus
that transduces a human cDNA encoding the 175-kD protein and used this
retrovirus to infect BAF3, a murine, bone marrow-derived cell line, which is
dependent on the haematopoietic factor interleukin-3 (IL3) for its growth in
culture. The EGF receptors expressed in the infected cells exhibit two affinity
states, as well as EGF-stimulated autophosphorylation. Furthermore, EGF can
replace IL3 in supporting short-term proliferation of these cells. These data
identify functional properties of the EGF receptor upon expression of the 175-kD
EGF binding protein in a haemotopoietic cell that does not express endogenous
receptors. They also suggest that gene transfer of growth factor receptors to
heterologous cells may allow novel growth stimuli to be exploited.
- Language of Publication
- English
- Unique Identifier
- 89054145
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- MeSH Heading (Major)
- Interleukin-3|*PD; Receptors, Epidermal Growth Factor-Urogastrone|GE/*ME
- MeSH Heading
- Animal; Cell Line; DNA|ME; Epidermal Growth Factor-Urogastrone|PD; Mice;
Molecular Weight; Protein-Tyrosine Kinase|ME; Retroviridae|GE; Support, Non-U.S.
Gov't; Support, U.S. Gov't, P.H.S.; Transduction, Genetic
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0021-9541
- Country of Publication
- UNITED STATES
Record 15 from database: MEDLINE
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- Title
- Action of erythromycin and virginiamycin S on polypeptide synthesis in
cell-free systems.
- Author
- Chinali G; Nyssen E; Di Giambattista M; Cocito C
- Address
- Istituto di Strutture Biologiche ed Ultrastruttura Cellulare, Ila FacoltÄa
di Medicina, UniversitÄa di Napoli, Italy.
- Source
- Biochim Biophys Acta, 1988 Nov, 951:1, 42-52
- Abstract
- Erythromycin (a 14-membered macrolide) and virginiamycin S (a type B
synergimycin) block protein biosynthesis in bacteria, but are virtually inactive
on poly(U)-directed poly(Phe) synthesis. We have recently shown, however, that
these antibiotics inhibit the in vitro polypeptide synthesis directed by
synthetic copolymers: this effect is analyzed further in the present work. We
were unable to find any consistent alteration produced by th