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Related post: thymus produces a different set of LSF than that produced by the spleen.
There does appear to be a considerable overlap, however. In addition, the
profile of LSF produced by the thymus appears to change as the animal ages.
Further biochemical and biological characterization of the
individual LSF are planned. Initially this will be to determine the effect
of LSF on specific antibody responses and to isolate and characterize the B
cell stimulating material. Further exploration of the subsets of thymocytes
and splenic Buy Vibramycin T cells Vibramycin 100mg which produce each LSF and the cells which are the primary
target of LSF activity are planned. These probably will involve the use of
alloantisera and other lectins for the characterization and fractionation
of the cellular subsets.
Biochemical Events in Transmembrane Signaling
The objectives of our research in this project is to determine the
earlier (first few minutes) Vibramycin Price biochemical events and pathways which are important
in the activation of B and T lymphocytes.
Previously, we eludicated a series of biochemical steps in the cell
membrane using Con A to activate murine T cells. These include the successive
methyl at ion of phosphatidyl ethanol amine to form phosphatidyl choline
(lecithin), followed by the degradation of lecithin to yield arachidonic acid
and lysolecithin. Our current studies have shown that this pathway is also
stimulated by several other mitogenic lectins, but not by non-mitogenic
lectins. Furhtermore, in preliminary experiments we have also found that
LAF on T cells and anti-y chain on B cells both activate this biochemical
pathway. Stimulation Purchase Vibramycin of cultured human T cell lines with PHA produced T cell
Growth Factor (TCGH) also stimulate the same biochemical events. These
observations suggest that this pathway is common to several different modes
of lymphocyte activation.
The biochemical observations we have made on Vibramycin 100 this system will be studied
in further detail. The elucidation of the membrane events by which the
binding of mitogenic lectins to the cell surface acceptors activates the
transmethylase enzymes will be sought. The activation of the calcium
dependent phospholipase A2 by mitogens will also be studied. One of the
approaches planned to study these membrane associated enzymes is by raising
antisera directed against the isolated proteins. These antisera will be
fluoresceinated and used to detect changes in the distribution or availability
of these enzymes on the cell surface during the activation.
The biochemical pathways will also be followed downstream in an attempt
to link subsequent events (such as changes in the levels of cyclic nucleotides,
protein phosphorylation, etc) to the currently delineated events. These
studies will be p rsued by the use of radioactive metabolites, specific in-
hibitors, and enzyme assays.
Lectin Fractionation of Lymphoid Cell Subsets
In collaboration with LMI/NIAID and LCI/NIAID we have extended to human
tissue our studies on the preferential binding of approximately 40 lectins
to subsets of lymphoid cells.
Lectins used in these experiments were either isolated by this laboratory,
obtained from other researchers, or purchased commercially. In most cases
the lectins were assayed for purity by polyacryl amide gel electrophoresis in
sodium dodecyl sulfate, ion-exchange chromatography, and/or affinity chromato-
graphy. Lectins were fluorescein labeled and agglutination titers were
determined for each cell type with each lectin. For each analysis fluorescence
was measured on 50,000 viable lymphocytes Vibramycin 100 Mg by flow microfluorometry on a
Fluorescence Activated Cell Sorter (FACS).
Several lectins were found which showed bi- or polymodal staining to
human peripheral T cells, B cells monocytes, and to 'null' cells. It was
noted that this group included lectins which gave only unimodal staining
when tested on murine lymphocytes. Our studies on the identification of
subsets of murine lymphocytes have progressed to the use of lectins to
fractionate these subsets. We have explored several methods for the lectin
fractionation of cells. These include but are not limited to: lectin
affinity column chromatography, covalent binding of the lectin to culture
plates, and covalent binding of glycoproteins to culture plates followed by
affinity binding of the lectin to the glycoprotein. To avoid having to design
a specific technique for each lectin, we are attempting to delineate a
general procedure by which many different lectins may Vibramycin Buy be Vibramycin Doxycycline individually bound
to culture plates and used for the fractionation of lymphoid and other cells.
At the same time, and dependent upon the development of fractionation
techniques, we are characterizing the subsets by other cell surface markers.
We Doxycycline Vibramycin have also initiated functional characterization of these fractionated
subsets of murine and human lymphocytes by their biological activities.
These include helper activity, production of LSF, and suppressor activities.
The future course of this project will be to emphasize the development
of separation techniques for the Vibramycin D subsets recognized by the lectins and to
characterize the fractionated subsets of both human and murine lymphocytes.
Structure Studies on Guinea Pin la Antigens
Inbred strain 2 and strain 13 guinea pigs, and alloantisera to their la
antigens were obtained from Dr. E. Shevach, LI. The la antigens were labeled
by the metabolic incorporation of a mixture of ten radiolabeled amino acids,
single amino acids, and sugars into spleen cells. The cells were lysed with
NP-40 and the la antigens isolated by affinity chromatography on columns of
lentil lectin followed by immunoaffinity chromatography or immune precipitation,
The alpha and beta chains were isolated by polyacryl amide gel electrophoresis
in sodium dodecyl sulfate with and without prior reduction of the disulfide
bonds. Amino acid sequence studies of the amino terminal regions have pre-
vously been performed on the isolated chains. During this past year, we
extended our studies of the homology and differences between the chains of
the guinea pig la antigens to include internal regions thru the use of peptide
Peptide mapping studies by ion-exchange chromatography of tryptic pep-
tides of the alpha and beta chains from la. 3,5 labeled with 10 amino acids
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