gossypol chemistry
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Gossypium , chemistry
Latest Paper:
Genetika. 2007 Apr ;43 (4):508-15 17555127
[Species-specific features of the protein patterns of diploid cotton
seeds with A and D genomes and of some amphidiploids]
Sh Iu Iunuskhanov , D Iu Ataev , I Zh Kurbanbaev
Differences between species were revealed in electrophoretic patterns of
seed proteins of various diploid cotton species with A and D genomes and
some amphidiploids. Reference spectra and electrophoretic formulas were
compiled for representatives of diploid and amphidiploid species, and the
electrophoretic spectra were visually evaluated. They would allow
identification of various cotton species, varieties, and lines. Homology
between cotton species was estimated from the results of electrophoretic
protein studies. The homology between species of a single genome group
was shown to be closer than between species belonging to different
genome groups.
Mesh-terms: Diploidy; Genome, Plant; Gossypium, chemistry;
Gossypium, genetics; Plant Proteins, analysis; Plant Proteins, genetics;
Seeds, chemistry; Seeds, genetics; Species Specificity;
Most cited papers:
Anal Biochem. 1994 Nov 15;223 (1):7-12 7535022 [Cited: 24]
A modified hot borate method significantly enhances the yield of
high-quality RNA from cotton (Gossypium hirsutum L.).
C Y Wan , T A Wilkins
The isolation of biologically active RNA from cotton (Gossypium
hirsutum L.) is difficult due to interference by high levels of endogenous
phenolics, polysaccharides, and secondary metabolites. A modified hot
borate procedure was developed to combat these cellular constituents
during tissue homogenization, resulting in the quantitative recovery of
RNA suitable for hybridization analysis, in vitro translation, and cDNA
synthesis. The efficacy of several hot borate buffer adjuvants for the
qualitative and quantitative recovery of leaf RNA was monitored by
absorbance spectra, gel electrophoresis, protein, and cDNA synthesis. Of
the buffer adjuvants evaluated, polyvinylpyrrolidone-40 (PVP-40)
exhibited the single, most significant impact on the yield and quality of
RNA isolated from cotton leaves, although inclusion of deoxycholate
and/or Nonident-40 (NP-40) further enhanced the quality of the RNA.
The unsurpassed qualitative and quantitative recovery of total RNA from
cotton by hot borate buffer at alkaline pH, supplemented with PVP-40,
deoxycholate, and/or NP-40 had also proven satisfactory for other
recalcitrant plant species as well as for especially difficult tissue types.
Mesh-terms: Boric Acids; DNA, Complementary, biosynthesis;
Gossypium, chemistry; RNA, isolation & purification; Support, Non-U.S.
Gov't; Translation, Genetic;
Biochim Biophys Acta. 2001 Jan 12;1544 (1-2):196-206 11341929
[Cited: 5]
Isolation and characterization of a D-7 LEA protein from pollen that
stabilizes glasses in vitro.
W F Wolkers , S McCready , W F Brandt , G G Lindsey , F A Hoekstra
A heat-soluble protein present in substantial quantities in Typha latifolia
pollen was purified to homogeneity. The protein was subjected to
cyanogen bromide cleavage, and the peptides produced were separated by
HPLC chromatography and sequenced. The two sequences determined
were found to be related to the putative D76 LEA protein from Brassica
napus seeds and one of them to the D-7 LEA protein from upland cotton.
This suggests the pollen protein to be a member of the LEA group III
family of proteins. The secondary structure of the protein in solution and
in the dry state was investigated using Fourier transform IR spectroscopy.
Whereas the protein in solution was highly unordered, being largely in a
random coil conformation, the conformation was largely alpha-helical
after fast drying. Slow drying reversibly led to both alpha-helical and
intermolecular extended beta-sheet structures. When dried in the presence
of sucrose, the protein adopted alpha-helical conformation, irrespective of
drying rate. The effect of the protein on the stability of sucrose glasses
was also investigated. The dehydrated mixture of sucrose and the LEA
protein had higher glass transition temperatures and average strength of
hydrogen bonding than dehydrated sucrose alone. We suggest that LEA
proteins may play a role together with sugars in the formation of a tight
hydrogen bonding network in the dehydrating cytoplasm, thus conferring
long-term stability.
Mesh-terms: Amino Acid Sequence; Brassica, chemistry; Carbohydrate
Conformation; Electrophoresis, Polyacrylamide Gel; Glass; Gossypium,
chemistry; Plant Proteins, chemistry; Plant Proteins, isolation &
purification; Pollen, chemistry; Protein Structure, Secondary;
Spectroscopy, Fourier Transform Infrared; Sucrose, chemistry; Support,
Non-U.S. Gov't;
Plant Physiol. 1995 Aug ;108 (4):1691-701 7659756 [Cited: 5]
Solubilization and partial characterization of extensin fragments
from cell walls of cotton suspension cultures. Evidence for a covalent
cross-link between extensin and pectin.
X Qi , B X Behrens , P R West , A J Mort
Extensin, a major hydroxyproline (Hyp)-rich glycoprotein in walls of
cultured cells of dicotyledonous plants, is very difficult to solubilize. To
learn about the nature of the insolubilization, we have tested the ability of
a variety of selective hydrolytic methods, and combinations of them, to
liberate extensin or fragments of extensin from suspension-culture cell
walls. After the complete deglycosylation of cotton (Gossypium hirsutum
L.) walls, trypsinization solubilized 80% of the Hyp. The sequences of
three abundant peptides were: (a) serine-Hyp-Hyp-Hyp-Hyp-Hyp-Hyp-
serine-Hyp-Hyp-lysine, (b) serine-Hyp-Hyp-Hyp-Hyp-valine-lysine, and
(c) serine-Hyp-Hyp-serine-alanine-Hyp-lysine. After a sequential
treatment of walls with endopolygalacturonase, cellulase, -73 degrees C
anhydrous hydrogen fluoride solvolysis, and ammonium bicarbonate
extraction, only sugars indicative of rhamnogalacturonan I and protein
remained insoluble. Trypsin treatment of this residue liberated 50% of the
Hyp. A significant proportion of rhamnogalacturonan-associated sugars
co-solubilized and co-purified along with the extensin fragments
following the trypsinization. By sodium dodecyl sulfate gel
electrophoresis and gel filtration, the glycopeptides fell into two classes.
One class contained distinctly sized molecules with relative molecular
weights in the range of 4,000 to 24,000. The other class did not enter the
resolving gel and was hetero-disperse. After complete deglycosylation by
a 0 degrees C anhydrous hydrogen fluoride treatment, the first class was
little affected in its electrophoretic mobility, whereas the larger
heterogeneous material mostly entered the separating gel. After further
trypsinization of the deglycosylated peptides and analysis by capillary
zone electrophoresis, the peptides in both size classes were shown to
contain the sequences described above. From our observations we suggest
that cotton extensin becomes insolubilized into cell walls in part by
pectin-protein cross-links in addition to the protein-protein (or protein-
phenolic-protein) cross-links that have been repeatedly suggested.
Mesh-terms: Amino Acid Sequence; Amino Acids, analysis;
Carbohydrates, analysis; Cell Wall, chemistry; Cells, Cultured;
Glycoproteins, chemistry; Gossypium, chemistry; Hydroxyproline,
analysis; Molecular Sequence Data; Pectins, chemistry; Peptide
Fragments, chemistry; Plant Proteins, chemistry; Sequence Analysis;
Solubility; Spectrometry, Mass, Secondary Ion; Support, Non-U.S. Gov't;
Support, U.S. Gov't, Non-P.H.S.;
Biochim Biophys Acta. 1997 Apr 10;1351 (3):305-12 9130594
[Cited: 3]
Identification of a cotton fiber-specific acyl carrier protein cDNA by
differential display.
P Song , R D Allen
Transcripts from immature fibers and stripped ovules (fibers removed) of
cotton (Gossypium hirsutum L.) were compared by differential display to
identify cDNA fragments that represent mRNAs that are expressed
primarily in cotton fibers. Eight independent fiber-specific cDNA
fragments were isolated. One of these cDNAs had strong sequence
similarity with acyl carrier protein (ACP). A full-length cDNA for the
cotton fiber-specific ACP was isolated using a PCR cDNA library
screening technique. This 713 bp cDNA has an open reading frame that
encodes a 136 amino acid polypeptide. Overall nucleotide and amino acid
sequence identities with other plant ACP gene sequences averaged 66%
and 60% respectively. A 19 amino acid sequence surrounding the
prosthetic group attachment site is nearly identical to other plant ACP
genes. Northern blot analyses showed that transcripts homologous to this
fiber-specific ACP cDNA were predominantly expressed during the
elongation stage of fiber development. Initial genomic Southern blot
analysis indicated that a single copy of the fiber-specific ACP gene may
be present in both the cotton A and D genomes, since diploid Gossypium
species with A or D genomes gave identical bands. We speculate that this
putative fiber-specific ACP may play an important role in rapidly
elongating cotton fibers by contributing to the synthesis of membrane
lipids. It is also apparent that during the evolution of cotton a member of
the ACP gene family has been recruited for specific expression in cotton
fibers.
Mesh-terms: Acyl Carrier Protein, genetics; Acyl Carrier Protein,
metabolism; Amino Acid Sequence; Blotting, Northern; Blotting,
Southern; DNA, Complementary, genetics; Gene Expression Regulation,
Plant; Gene Library; Genetic Techniques; Gossypium, chemistry;
Gossypium, genetics; Gossypium, growth & development; Molecular
Sequence Data; Plant Proteins, genetics; Plant Proteins, metabolism;
Polymerase Chain Reaction, methods; RNA, Messenger, biosynthesis;
RNA, Plant, chemistry; RNA, Plant, genetics; Sequence Analysis, DNA;
Tissue Distribution;
Plant Physiol. 1995 Sep ;109 (1):269-75 7480326 [Cited: 3]
N-acylphosphatidylethanolamine in dry and imbibing cottonseeds.
Amounts, molecular species, and enzymatic synthesis.
J A Sandoval , Z H Huang , D C Garrett , D A Gage , K D Chapman
N-Acylphosphatidylethanolamine (NAPE), an unusual acylated derivative
of phosphatidylethanolamine (PE), was recently shown to be synthesized
from PE and free fatty acids in cotyledons of cotton (Gossypium hirsutum
L.) seedlings (K.D. Chapman, T.S. Moore [1993] Plant Physiol 102: 761-
769). Here we report that NAPE is present in dry seeds of cotton and
increases with time of imbibition from 2.31 nmol/seed in dry seeds to
4.26 nmol/seed in 4-h-soaked seeds. Total phospholipid/seed also
increased such that the relative percentage of NAPE was similar in dry
and soaked seeds (2.3 mol% compared to 2.6 mol%, respectively). The
major molecular species of NAPE were identified in both dry and soaked
seeds by fast atom bombardment mass spectrometry and collisionally
activated dissociation tandem mass spectrometry as 16:0/18:2-PE(N-
palmitoyl), 16:0/18:2-PE(N-linoleoyl), and 18:2/18:2-PE(N-palmitoyl).
The specific activity of NAPE synthase in seed extracts increased with
increasing time of imbibition from 35 pmol h-1 mg-1 protein in dry seeds
to 129 pmol h-1 mg-1 protein in 4-h-soaked seeds. Collectively, our
results indicate that NAPE is present in dry cottonseeds and synthesized
during imbibition. The biosynthesis of NAPE provides a mechanism for
maintaining membrane integrity during seed rehydration and may indicate
that NAPE plays a protective role in intracellular membranes of plant
tissues, as has been suggested for intracellular membranes of animal
tissues.
Mesh-terms: Acyltransferases, metabolism; Gossypium, chemistry;
Gossypium, metabolism; Kinetics; Molecular Structure;
Phosphatidylethanolamines, analysis; Phosphatidylethanolamines,
biosynthesis; Phosphatidylethanolamines, chemistry; Seeds, chemistry;
Seeds, metabolism; Spectrometry, Mass, Fast Atom Bombardment;
Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.; Support, U.S.
Gov't, P.H.S.; Water;
J Exp Bot. 2002 Feb ;53 (367):323-31 11807136 [Cited: 2]
Plant allocation to defensive compounds: interactions between
elevated CO(2) and nitrogen in transgenic cotton plants.
Carlos E Coviella , Robert D Stipanovic , John T Trumble
Plant allocation to defensive compounds in response to growth in elevated
atmospheric CO(2) in combination with two levels of nitrogen was
examined. The aim was to discover if allocation patterns of transgenic
plants containing genes for defensive chemicals which had not evolved in
the species would respond as predicted by the Carbon Nutrient Balance
(CNB) hypothesis. Cotton plants (Gossypium hirsutum L.) were sown
inside 12 environmental chambers. Six of them were maintained at an
elevated CO(2) level of 900 micromol mol(-1) and the other six at the
current level of approximately 370 micromol mol(-1). Half the plants in
each chamber were from a transgenic line producing Bacillus
thuringiensis (Bt) toxin and the others were from a near isogenic line
without the Bt gene. The allocation to total phenolics, condensed tannins,
and gossypol and related terpenoid aldehydes was measured. All the
treatments were bioassayed against a non-target insect herbivore found on
cotton, Spodoptera exigua (Hübner) (Lepidoptera: Noctuidae). Plants had
lower N concentrations and higher C:N ratios when grown in elevated
CO(2). Carbon defensive compounds increased in elevated CO(2), low N
availability or both. The increase in these compounds in elevated CO(2)
and low N, adversely affected growth and survival of S. exigua. The
production of the nitrogen-based toxin was affected by an interaction
between CO(2) and N; elevated CO(2) decreased N allocation to Bt, but
the reduction was largely alleviated by the addition of nitrogen. The CNB
hypothesis accurately predicted only some of the results, and may require
revision. These data indicate that for the future expected elevated CO(2)
concentrations, plant allocation to defensive compounds will be affected
enough to impact plant-herbivore interactions.
Mesh-terms: Adaptation, Physiological; Animals; Bacillus thuringiensis,
pathogenicity; Bacterial Toxins, metabolism; Biological Assay; Carbon
Dioxide, metabolism; Carbon, metabolism; Gossypium, chemistry;
Gossypium, metabolism; Gossypium, parasitology; Gossypol,
biosynthesis; Host-Parasite Relations; Insecticides, metabolism; Nitrogen,
metabolism; Pest Control, Biological; Phenols, metabolism; Plant
Diseases, parasitology; Plant Leaves, chemistry; Plant Leaves,
metabolism; Plant Leaves, parasitology; Plants, Genetically Modified;
Protein Precursors, metabolism; Spodoptera, growth & development;
Support, Non-U.S. Gov't; Tannins, biosynthesis; Time Factors;
Plant Mol Biol. 1997 May ;34 (1):111-8 9177317 [Cited: 2]
Identification of a delta-TIP cDNA clone and determination of
related A and D genome subfamilies in Gossypium species.
D L Ferguson , R B Turley , R H Kloth
Tonoplast intrinsic proteins (TIPs) have been implicated in the process of
cell elongation, such as occurs in the developing cotton fiber. We have
isolated a cDNA clone (997 bp in length) from a cotton (Gossypium
hirsutum L.) library which putatively encodes a protein of 248 residues
(Mr 25079) with 85% identity to Arabidopsis delta-TIP. The derived
amino acid sequence included two conserved sequences associated with
major intrinsic proteins (SGxHxNPA at residues 78 to 85, NPA residues
at 197 to 199) and a cysteine residue at 116 which is reported to bind
mercury in Arabidopsis delta-TIP. The polymerase chain reaction was
used to generate partial genomic clones of the cotton delta-TIP. In
comparison to other genomic TIP sequences, the number (two) and
position of the introns were conserved in cotton. Comparing the TIP
sequences from cotton revealed two subfamilies, which were consistently
distinguished by a Tsp45I restriction site polymorphism. This
polymorphism was used to demonstrate that TIP subfamilies were
specific to either the A or D genomes of Gossypium. When delta-TIP
DNA fragments were amplified from cDNA of fiber 14 days after
anthesis, the A and D were found, indicating the presence of delta-TIP
transcripts in these elongating cells.
Mesh-terms: Amino Acid Sequence; Aquaporins; Arabidopsis Proteins;
Base Sequence; Cloning, Molecular; DNA, Complementary, isolation &
purification; DNA, Complementary, metabolism; DNA, Plant, chemistry;
DNA, Plant, genetics; Genome, Plant; Gossypium, chemistry;
Gossypium, genetics; Molecular Sequence Data; Multigene Family; Plant
Proteins, classification; Plant Proteins, genetics; Polymerase Chain
Reaction; Porins, classification; Porins, genetics;
Protoplasma. 2003 Jun ;221 (3-4):175-84 12802624 [Cited: 1]
Localization of sucrose synthase and callose in freeze-substituted
secondary-wall-stage cotton fibers.
Vadim V Salnikov , Mark J Grimson , Robert W Seagull , Candace H
Haigler
Methods for cryogenic fixation, freeze substitution, and embedding were
developed to preserve the cellular structure and protein localization of
secondary-wall-stage cotton (Gossypium hirsutum L.) fibers accurately
for the first time. Perturbation by specimen handling was minimized by
freezing fibers still attached to a seed fragment within 2 min after removal
of seeds from a boll still attached to the plant. These methods revealed
native ultrastructure, including numerous active Golgi bodies,
multivesicular bodies, and proplastids. Immunolocalization in the context
of accurate structure was accomplished after freeze substitution in acetone
only. Quantitation of immunolabeling identified sucrose synthase both
near the cortical microtubules and plasma membrane and in a proximal
exoplasmic zone about 0.2 microm thick. Immunolabeling also showed
that callose (beta-1,3-glucan) was codistributed with sucrose synthase
within this exoplasmic zone. Similar results were obtained from cultured
cotton fibers. The distribution of sucrose synthase is consistent with its
having a dual role in cellulose and callose synthesis in secondary-wall-
stage cotton fibers.
Mesh-terms: Cell Wall, chemistry; Cell Wall, ultrastructure; Cellulose,
biosynthesis; Cotton Fiber; Cryopreservation; Glucans, analysis;
Glucosyltransferases, analysis; Gossypium, chemistry; Gossypium,
enzymology; Immunohistochemistry; Microscopy, Electron; Polymers,
analysis; Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.;
J Agric Food Chem. 2002 Nov 20;50 (24):7017-21 12428953 [Cited:
1]
Toxicity of (+)- and (-)-gossypol to the plant pathogen, Rhizoctonia
solani.
Lorraine S Puckhaber , Michael K Dowd , Robert D Stipanovic , Charles
R Howell
The dimeric sesquiterpene gossypol occurs naturally in cottonseed and
other parts of the cotton plant. Gossypol exists as enantiomers because of
the restricted rotation around the central binaphthyl bond. The (-)-
enantiomer is toxic to nonruminant animals while the (+)-enantiomer
exhibits little, if any, toxicity to these animals. Developing cotton plants
with low levels of the (-)-gossypol could expand the use of cottonseed as
a feed source. Gossypol also may play a role in protecting the plant from
pathogens. The relative toxicity of (+)- and (-)-gossypol to plant
pathogens has not been reported. We measured the concentration of (+)-
and (-)-gossypol in roots from cotton seedlings that were treated with the
biocontrol agent Trichoderma virens that induces biosynthesis of gossypol
and related terpenoids in cotton roots. (-)-Gossypol was the minor
enantiomer in control and treated roots, but levels were slightly higher in
roots from T. virens-treated seed. We also determined the toxicity of the
gossypol enantiomers and the racemate to the seedling disease pathogen
Rhizoctonia solani. The (+)- and (-)-enantiomers of gossypol and the
racemate are equally effective in inhibiting growth of this pathogen. The
lethal doses of the gossypols required to kill the pathogen appeared to be
similar, but their toxicities are significantly less than those of related
cotton and kenaf sesquiterpenes. The results indicate that altering the
enantiomeric ratio in cotton roots will not adversely affect the resistance
of seedlings to the seedling pathogen R. solani.
Mesh-terms: Gossypium, chemistry; Gossypium, microbiology;
Gossypol, analysis; Gossypol, pharmacology; Plant Diseases,
microbiology; Plant Roots, chemistry; Rhizoctonia, drug effects;
Rhizoctonia, growth & development; Seedling, chemistry; Seedling,
microbiology; Seeds, chemistry; Stereoisomerism; Trichoderma;
Plant Physiol. 2001 Nov ;127 (3):1234-42 11706202 [Cited: 1]
Sucrose phosphate synthase activity rises in correlation with high-
rate cellulose synthesis in three heterotrophic systems.
V M Babb , C H Haigler
Based on work with cotton fibers, a particulate form of sucrose (Suc)
synthase was proposed to support secondary wall cellulose synthesis by
degrading Suc to fructose and UDP-glucose. The model proposed that
UDP-glucose was then channeled to cellulose synthase in the plasma
membrane, and it implies that Suc availability in cellulose sink cells
would affect the rate of cellulose synthesis. Therefore, if cellulose sink
cells could synthesize Suc and/or had the capacity to recycle the fructose
released by Suc synthase back to Suc, cellulose synthesis might be
supported. The capacity of cellulose sink cells to synthesize Suc was
tested by analyzing the Suc phosphate synthase (SPS) activity of three
heterotrophic systems with cellulose-rich secondary walls. SPS is a
primary regulator of the Suc synthesis rate in leaves and some Suc-
storing, heterotrophic organs, but its activity has not been previously
correlated with cellulose synthesis. Two systems analyzed, cultured
mesophyll cells of Zinnia elegans L. var. Envy and etiolated hypocotyls
of kidney beans (Phaseolus vulgaris), contained differentiating tracheary
elements. Cotton (Gossypium hirsutum L. cv Acala SJ-1) fibers were also
analyzed during primary and secondary wall synthesis. SPS activity rose
in all three systems during periods of maximum cellulose deposition
within secondary walls. The Z. elegans culture system was manipulated to
establish a tight linkage between the timing of tracheary element
differentiation and rising SPS activity and to show that SPS activity did
not depend on the availability of starch for degradation. The significance
of these findings in regard to directing metabolic flux toward cellulose
will be discussed.
Mesh-terms: Asteraceae, chemistry; Asteraceae, metabolism; Cell
Differentiation; Cell Wall, metabolism; Cells, Cultured; Cellulose,
biosynthesis; Cellulose, chemistry; Fructose, metabolism;
Glucosyltransferases, metabolism; Gossypium, chemistry; Gossypium,
metabolism; Hypocotyl, metabolism; Models, Molecular; Phaseolus,
chemistry; Phaseolus, metabolism; Plant Leaves, cytology; Plant Leaves,
metabolism; Starch, metabolism; Sucrose, metabolism; Support, Non-
U.S. Gov't; Uridine Diphosphate Glucose, metabolism;
Chem Senses. 2008 Jan 8; : 18184638
Sensory Deafferentation Transsynaptically Alters Neuronal GluR1
Expression in the External Plexiform Layer of the Adult Mouse Main
Olfactory Bulb.
Kathryn A Hamilton , Stephanie Parrish-Aungst , Frank L Margolis ,
Ferenc Erdélyi , Gabor Szabó , Adam C Puche
Altered distribution of the alpha-amino-3-hydroxy-5-methylisoxazole-4-
propionic acid (AMPA) receptor subunit GluR1 has been linked to
stimulation-dependent changes in synaptic efficacy, including long-term
potentiation and depression. The main olfactory bulb (OB) remains plastic
throughout life; how GluR1 may be involved in this plasticity is
unknown. We have previously shown that neonatal naris occlusion
reduces numbers of interneuron cell bodies that are immunoreactive for
GluR1 in the external plexiform layer (EPL) of the adult mouse OB. Here,
we show that immunoreactivity of mouse EPL interneurons for GluR1 is
also dramatically reduced following olfactory deafferentation in
adulthood. We further show that expression of glutamic acid
decarboxylase (GAD) 65, 1 of 2 GAD isoforms expressed by adult
gamma-aminobutyric acidergic interneurons, is reduced, but to a much
smaller extent, and that in double-labeled cells, immunoreactivity for the
Ca(2+)-binding protein parvalbumin (PV) is also reduced. In addition,
GluR1 expression is reduced in presumptive tufted cells and interneurons
that are negative for GAD65 and PV. Consistent with previous reports,
sensory deafferentation resulted in little neuronal degeneration in the
adult EPL, indicating that these differences were not likely due to death of
EPL neurons. Together, these results suggest that olfactory input regulates
expression of the GluR1 AMPA receptor subunit by tufted cells that may
in turn regulate GluR1 expression by interneurons within the OB EPL.
Ann Intern Med. 1949 Aug ;31 (2):216-27 18136037
Pulmonary disease manifestations of ankylosing spondylarthritis.
K A HAMILTON
Bioorg Med Chem Lett. 2007 Sep 7; : 17900896
Synthesis and evaluation of substituted benzoisoquinolinones as
potent inhibitors of Chk1 kinase.
Robert M Garbaccio , Shaei Huang , Edward S Tasber , Mark E Fraley ,
Youwei Yan , Sanjeev Munshi , Mari Ikuta , Lawrence Kuo , Constanine
Kreatsoulas , Steve Stirdivant , Bob Drakas , Keith Rickert , Eileen S
Walsh , Kelly A Hamilton , Carolyn A Buser , James Hardwick , Xianzhi
Mao , Stephen C Beck , Marc T Abrams , Weikang Tao , Rob Lobell ,
Laura Sepp-Lorenzino , George D Hartman
From HTS lead 1, a novel benzoisoquinolinone class of ATP-competitive
Chk1 inhibitors was devised and synthesized via a photochemical route.
Using X-ray crystallography as a guide, potency was rapidly enhanced
through the installation of a tethered basic amine designed to interact with
an acidic residue (Glu91) in the enzyme pocket. Further SAR was
explored at the solvent front and near to the H1 pocket and resulted in the
discovery of low MW, sub-nanomolar inhibitors of Chk1.
J Neurophysiol. 2007 Jan 10; : 17215500
Group I Metabotropic Glutamate Receptors Are Differentially
Expressed by Two Populations of Olfactory Bulb Granule Cells.
Thomas Heinbockel , Kathryn A Hamilton , Matthew Ennis
In the main olfactory bulb, several populations of granule cells (GCs) can
be distinguished based on the soma location either superficially,
interspersed with mitral cells within the mitral cell layer (MCL), or
deeper, within the GC layer (GCL). Little is known about the
physiological properties of superficial GCs (sGCs) vs. deep GCs (dGCs).
Here, we used patch-clamp recording methods to explore the role of
Group I metabotropic glutamate receptors (mGluRs) in regulating the
activity of GCs in slices from wildtype and mGluR -/- mutant mice. In
wildtype mice, bath application of the selective Group I mGluR agonist
DHPG depolarized and increased the firing rate of both GC subtypes. In
the presence of blockers of fast synaptic transmission (APV, CNQX,
gabazine), DHPG directly depolarized both GC subtypes. The two GC
subtypes responded differentially to DHPG in mGluR1-/- and mGluR5-/-
mice, however. DHPG depolarized sGCs in slices from mGluR5-/- mice,
but it had no effect on sGCs in slices from mGluR1-/- mice. By contrast,
DHPG depolarized dGCs in slices from mGluR1-/- mice, but it had no
effect on dGCs in slices from mGluR5-/- mice. Previous studies have
shown that mitral cells express mGluR1, but not mGluR5. The present
results therefore suggest that sGCs are more similar to mitral cells than
dGCs in terms of mGluR expression.
Trends Microbiol. 2006 Feb 3; : 16460942
Animal movements and the spread of infectious diseases.
Eric M Fèvre , Barend M de C Bronsvoort , Katie A Hamilton , Sarah
Cleaveland
Domestic and wild animal population movements are important in the
spread of disease. There are many recent examples of disease spread that
have occurred as a result of intentional movements of livestock or
wildlife. Understanding the volume of these movements and the risks
associated with them is fundamental in elucidating the epidemiology of
these diseases, some of which might entail zoonotic risks. The importance
of the worldwide animal trade is reviewed and the role of the unregulated
trade in animals is highlighted. A range of key examples are discussed in
which animal movements have resulted in the introduction of pathogens
to previously disease-free areas. Measures based on heightened
surveillance are proposed that mitigate the risks of new pathogen
introductions.
Neuroscience. 2005 ;133:819-29 15896912
Properties of external plexiform layer interneurons in mouse
olfactory bulb slices.
K A Hamilton , T Heinbockel , M Ennis , G Szabó , F Erdélyi , A Hayar
In the external plexiform layer (EPL) of the main olfactory bulb, apical
dendrites of inhibitory granule cells form large numbers of synapses with
mitral and tufted (M/T) cells, which regulate the spread of activity along
the M/T cell dendrites. The EPL also contains intrinsic interneurons, the
functions of which are unknown. In the present study, recordings were
obtained from cell bodies in the EPL of mouse olfactory bulb slices.
Biocytin-filling confirmed that the recorded cells included interneurons,
tufted cells, and astrocytes. The interneurons had fine, varicose dendrites,
and those located superficially bridged the EPL space below several
adjacent glomeruli. Interneuron activity was characterized by high
frequency spontaneous excitatory postsynaptic potential/currents that
were blocked by the alpha-amino-3-hydroxy-5-methylisoxazole-4-
propionic acid (AMPA)/kainate receptor antagonist 6-cyano-7-
nitroquinoxaline-2,3-dione and largely eliminated by the voltage-sensitive
Na+ channel blocker, tetrodotoxin. Interneuron activity differed markedly
from that of tufted cells, which usually exhibited spontaneous action
potential bursts. The interneurons produced few action potentials
spontaneously, but often produced them in response to depolarization
and/or olfactory nerve (ON) stimulation. The responses to depolarization
resembled responses of late- and fast-spiking interneurons found in other
cortical regions. The latency and variability of the ON-evoked responses
were indicative of polysynaptic input. Interneurons expressing green
fluorescent protein under control of the mouse glutamic acid
decarboxylase 65 promoter exhibited identical properties, providing
evidence that the EPL interneurons are GABAergic. Together, these
results suggest that EPL interneurons are excited by M/T cells via
AMPA/kainate receptors and may in turn inhibit M/T cells within spatial
domains that are topographically related to several adjacent glomeruli.
Mesh-terms: Action Potentials, physiology; Animals; Cell Shape,
physiology; Excitatory Postsynaptic Potentials, physiology; Green
Fluorescent Proteins, genetics; Interneurons, cytology; Interneurons,
physiology; Mice; Mice, Inbred C57BL; Mice, Transgenic; Olfactory
Bulb, cytology; Olfactory Bulb, physiology; Organ Culture Techniques;
Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't;
Research Support, U.S. Gov't, P.H.S.;
J Agric Food Chem. 2004 Nov 17;52 (23):6969-76 15537305
Bollgard II cotton: compositional analysis and feeding studies of
cottonseed from insect-protected cotton (Gossypium hirsutum L.)
producing the Cry1Ac and Cry2Ab2 proteins.
Kathryn A Hamilton , Paul D Pyla , Matthew Breeze , Tammy Olson ,
Menghe Li , Edwin Robinson , Sean P Gallagher , Roy Sorbet , Yin Chen
Bollgard II cotton event 15985 producing the Cry1Ac and Cry2Ab2
proteins has been developed by genetic modification to broaden the
spectrum of insects to which the plant is tolerant and to provide an insect
resistance management tool to impede the onset of resistance. The
purpose of this study was to evaluate the composition and nutrition of
Bollgard II cotton, relative to the use for food and animal feed, compared
to that of conventional cotton varieties. Compositional analyses were
conducted to measure proximate, fiber, amino acid, fatty acid, gossypol,
and mineral contents of cottonseed from a total of 14 U.S. field sites over
two years. Compositional analysis results showed that the cottonseed and
cottonseed oil from Bollgard II cotton were comparable in their
composition to those of the conventional control cotton line and other
commercial varieties. The composition data are supported by nutritional
safety studies conducted with dairy cows, catfish, and quail. Results from
these studies showed that Bollgard II performed similarly to the
conventional control cotton varieties. These data demonstrate that
Bollgard II cotton is compositionally and nutritionally equivalent to
conventional cotton varieties. These data support the conclusion that
Bollgard II cotton is as safe and nutritious as conventional cotton for food
and feed use.
Mesh-terms: Amino Acids, analysis; Animal Feed; Animals; Bacterial
Proteins, genetics; Bacterial Toxins, genetics; Cattle; Cottonseed Oil,
chemistry; Dietary Fiber, analysis; Endotoxins, genetics; Fatty Acids,
analysis; Gossypium, chemistry; Gossypium, genetics; Gossypol,
analysis; Ictaluridae; Minerals, analysis; Plants, Genetically Modified,
chemistry; Plants, Genetically Modified, genetics; Quail;
Can Nurse. 1959 May ;55 (5):409-13 13652065
Emotional problems of the worker.
K A HAMILTON
Mesh-terms: Emotions; Nursing; Occupational Health;
Gossypium spp.
Cotton
Useful references 400, 452The cotton-seed consists of two parts: the hull, from which the staple cotton lint and linters arise, and the kernel, from which the oil and meal are obtained. The nutritive value of cottonseed products depends on proportions of husks and lint.
The husk is sometimes separated from the kernel before
crushing, but often the whole seed is extracted for oil.
Undecorticated oilcake is much richer in fibre and lower in
protein. The term "Egyptian cotton cake" refers to the
undecorticated cake of black seeds, and "Bombay cotton
cake" is the term used for the undecorticated cake of white
seeds. The cotton fibres of white seeds cover the whole
surface and are very difficult to remove; if the cottonseed
cake is broken, the fibres can be seen.
For every ton of lint in seed cotton there are approximately
1.7 tons of cottonseed. One ton of seed yields about 200 kg
of oil, 500 kg of cottonseed meal and 300 kg of hulls. The
residual oil in hydraulic-press cake is usually between 4%
and 8%, in screw-press cake between 3% and 5%, and in
solvent-extracted meal less than 3%.
GOSSYPOL. The seed embryo contains innumerable
glands filled with a yellow pigment called gossypol.
McDonald et al. (553) state that cotton seeds may contain
from 0.3-20 g/kg DM of gossypol, and concentrations of 4-
17 g/kg DM have been quoted for the kernels. Gossypol is
a polyphenolic aldehyde which is an antioxidant and
polymerisation inhibitor and is toxic to monogastric
animals: pigs and rabbits are the most sensitive, whereas
poultry are more tolerant. The general symptoms of
gossypol toxicity are constipation, depressed appetite and
loss of weight; death usually results from circulatory
failure. Although acute toxicity is low, ingestion of a small
amounts over a prolonged period can be lethal. It is
important to distinguish between free (soluble in 70-30 v/v
aqueous acetone) and bound gossypol since only the
former is considered to be physiologically active.
The free gossypol content of cottonseed meal decreases
during processing and varies according to the methods
used. In new seed, free gossypol accounts for 0.4-1.4% of
the weight of the kernel. Screw pressed materials have
200-500 mg free gossypol/kg, pre-
pressed solvent extracted meals 200-700 and solvent
extracted
1000-5000 mg/kg. Processing conditions have to be
carefully controlled to prevent loss of protein quality
owing to binding of gossypol to lysine at high
temperatures. Fortunately the shearing effect of the screw
press in the expeller process is an efficient gossypol
inactivator at temperatures which do not reduce protein
quality.
It is generally considered that pig and poultry diets should
not contain more than 100 mg free gossypol/kg and that
inclusions of cottonseed meal should be between 50-100
kg/t of feed. Particular care is required with laying hens
since comparatively low levels of the meal may cause an
olive green discoloration of the yolk in storage. An
associated pink discoloration of the albumen is now
considered to be due to cyclopropenoids and not gossypol
as was once thought. Treatment with ferrous sulphate can
ameliorate the biological effects of gossypol; the amount
of iron to be added is largely empirical. To reduce the
effects of gossypol on growth, the following proportions of
iron to free gossypol have been used: for cattle 1:1, for
broilers 2:1, for layers 4:l and for pigs 1:1.
Mature ruminant animals do not show ill-effects even
when they consume large quantities of cottonseed meal but
young cattle are much more susceptible to its toxic effects.
USES
COTTONSEED MEAL or COTTONSEED CAKE.
Cottonseed meal is an excellent protein supplement for
cattle. The limitations on effective utilization of this
product in rations for swine and poultry are of minor
significance for ruminant animals.
Both decorticated and undecorticated cottonseed meal
have a constipating effect on cattle, which is beneficial in
feeds with a high molasses content. Calves are susceptible
to the harmful effects of gossypol because of incomplete
rumen development; hence it is recommended that
concentrates for calves under five months of age contain
no more than 10-15% cottonseed meal.
Cottonseed meal has a relatively low rumen degradability
and is therefore a good source of by-pass protein and
especially useful in rations for milking cows.
With Creole and crossbred village cows in Mauritius
(normal milk yield 4-5 litres), Boodoo et al. (573) reported
that producers obtained over 9 litres milk/day over 300
days with peak milk yield at 12 litres/day, by
supplementing sugarcane tops and roadside grasses with
0.25 kg cottonseed cake/litre milk. The results were the
same as those obtained with 0.5 kg/litre of commercial
compound feed (17% CP).
Cottonseed meal can be used safely and profitably in pig
rations. Rations containing up to 0.01% free gossypol can
be used without the addition of iron salts. On the basis of a
typical analysis this means that the safe upper limit for a
good screw-press or prepress solvent meal is about 20%
and for direct solvent-extracted meal about 5%. Over these
levels, iron must be added in a 1:1 weight ratio to free
gossypol.
Cottonseed meal can also be used in rations for growing
chickens if the free gossypol does not exceed 0.03%.
Below this level, iron (2:1 iron to free gossypol) will
completely overcome the depressing effect. As cottonseed
is low in lysine, it may be necessary to make up for this
deficiency by adding lysine. Prepress solvent-extracted
meal may be used in layer feed if the gossypol has been
inactivated with iron (4:1 iron to free gossypol), if the free
gossypol content is not above 0.4%.
As determination of the amount of free gossypol in a meal
requires laboratory facilities, ferrous sulphate may
routinely be added to diets containing cottonseed meal. For
instance, for layers 0.05% iron (corresponding to 0.25%
ferrous sulphate septahydrate) can routinely be included in
diets containing up to 10% cottonseed meal and up to
0.16% iron in rations containing greater amounts. Broilers
cannot tolerate more than 0.07% iron in the diet.
WHOLE COTTONSEED
Whole cottonseed may be used as a feed for mature cattle,
as is often done where proper milling equipment is not
available. It is usually soaked in water and fed in small
quantities as a supplement to green feed.
Compared to the extracted meal, it has a lower protein
content and a much higher oil content. High levels may
cause scouring. The degradability characteristics of the
protein should be similar. Delinting of FUZZY WHOLE
COTTONSEED to DELINTED WHOLE COTTONSEED
results in a higher protein and fat content and lower fibre
content.
Neill et al. (574) report the use of up to 20-30% WCS in
intensive finishing rations for Brahman-cross steers.
Although OM digestibility declined, intake was unaffected
and LWG maintained 0.86 kg/day. They advise that WCS
can be used without detriment to at least 20% in finishing
diets, as a total feed during drought and for male animals
(rams) without affecting libido. No evidence of gossypol
toxicity was found but they suggest caution when feeding
WCS to young stock.
By treating with 5% ferrous sulphate solution, it can safely
be included in small quantities in pig rations.
COTTONSEED HULLS
Cottonseed hulls are the parts of the cottonseed head that is
left after the cotton and meal have been extracted and are
normally considered to be a very low quality feed for
ruminants. The results of two recent trials have shown that
they are capable of supporting moderate growth rates in
sheep. When a small amount of by-pass protein was added
to the diet of cottonseed hulls + urea + 50 g lucerne +
vitamins/minerals, the growth rate of lambs exceeded 130
g/day (567) and wool growth was increased from 6 to 9
g/day.
Investigation of the rumens of these animals showed that
protozoa were either eliminated or in very low population
densities. This could be the reason why cottonseed hulls
support such reasonable growth rates, even without
supplementation with by-pass protein. Intake of cottonseed
hulls by sheep is higher (c. 1 kg DM/day) than would be
expected of a 40% digestible feed and this is possibly
associated with a rapid breakdown of the indigestible
material in the rumen (567).
Norbaev (568) reports problems of hepatosis associated
with the feeding of cottonseed husks in Russia. Meat
inspection of 1004 Karakul sheep slaughtered in
Uzbekistan revealed hepatosis in 41%, cirrhosis in 10.7%
and multiple abscesses of the liver in 3.7%. In a feeding
experiment on 30 sheep, in which the daily ration
comprised 2 kg cotton husks, 0.5 kg oatmeal and 0.2 kg
lucerne hay. Liver disease developed within 2 months.
Values for blood albumin and glucose were low.
As cotton hulls are available at the mills where the meal is
produced, mixtures of meal and hulls can be bought. An
economical fattening ration for cattle is 20% meal and
80% hulls, together with 3-4 kg of grass daily and a
mineral supplement.
Various experiments with dairy cows cited by Coppock et
al. (569) show that the roughage value of CSH is better
than grass hays and nearly equal to high quality
bermudagrass but inferior to mixed clover hay. There is no
effect when CSH is substituted for corn or barley. There is
some evidence that CSH fibre maintains milk and fat yield
even when DM digestibility of the diet declines as a result
of substitution of CSH for lucerne hay (570). In some
diets, CSH may have a special value because of a
stimulatory effect on feed intake, not through improvement
in digestibility.
Cottonseed hulls have frequently been included in
complete diets for young, growing and lactating cattle.
Replacement of rice bran with up to 20% CSH did not
effect the milk yield or fat content of Murrah buffaloes
(571).
One novel application is reported by Yang et al. (572) of
the feeding of cottonseed hulls to pigs in China, after use
as a growth medium for 4 harvests of mushrooms
(Pleurotus sp.). The optimum dose was 10% of the diet
mixed with concentrates, which gave the same growth rate
and carcass quality as a control diet.
COTTON WOOD
Cotton wood is also used in some countries as a cattle
fodder. Stems, branches and leaves can be ground, ensiled
or hydrolysed with sodium hydroxide for feeding to beef
cattle.
As % of dry matter
DM CP CF Ash EE NFECa P Ref
Whole seeds, India
94.320.621.54.9 20.132.9 378
Whole seeds, Egypt
91.221.523.25.5 26.223.6 512
Bombay cotton cake
87.723.024.76.6 5.5 40.2 "
Egyptian cotton cake 87.926.424.26.6 5.7 37.1 "
Oilcake with hulls, mechanically extr-acted, Israel 91.426.924.05.0 6.8 37.3 0.22 0.63 365
Oilcake with hulls, mechanically extr-acted, Uganda 88.026.225.66.2 5.7 36.3 69
Oilcake with hulls, mechanically extr-acted, Zimbabwe 94.530.57.9 7.0 7.6 47.0 499
Oilcake without hulls, mechanically extracted, Israel 92.347.712.56.6 5.4 27.8 0.22 1.34 365
Oil meal without hulls, solventextracted, Iraq 94.340.315.76.8 0.6 36.6 0.31 1.11 182
Oil meal without hulls, prepresssolvent extracted, USA 89.946.115.17.1 0.7 31.0 0.17 1.36 452
Cottonseed hulls, West Indies 86.213.930.03.6 8.8 43.7 191
Cotton wood, Venezuela 5.3 64.98.1 0.9 20.8 537
Digestibility (%)
Animal CP CF EE NFEME Ref
Seeds, Indian variety Cattle 68.421.691.2 22.2 2.46 378
Seeds, Egyptian variety
Sheep 68.475.986.6 49.8 3.45 512
Bombay cotton cake
Sheep 77.220.393.8 53.7 2.13 "
Cake with hulls, expressed Sheep 75.038.095.0 66.0 2.59 365
Cake with hulls, expressed Cattle 72.057.091.3 80.4 3.02 499
Cake without hulls, expressed Sheep 83.045.097.0 74.0 3.06 365
Hulls Sheep 0.0 49.078.0 43.0 1.74 "
Nylon bag degradability
a b c 12hr 48hrRef(%) (%) (/hour) (%) (%)
Whole cotton seed, Ghana
DM 21.253.00.0320 62.8 627
Cotton seed, Korea
DM 27.141.70.0398 60.6 "
Cotton hulls, Brazil DM 2.8 51.00.0098 13.0 "[P (rumen degradability at time t) = a+b*(1-exp(-c*t))]
Amino acid composition as % of crude
protein
Oilcake Ref 452
Arg Cys GlyHisIls Leu Lys Met Phe Thr Try Tyr Val11.1 1.5 4.1 2.6 3.2 5.9 4.1 1.3 5.4 3.2 1.1 2.7 4.5
References69, 182, 191, 365, 378, 400, 452, 499, 512, 537, 553, 567, 568, 569, 570, 571, 572, 573, 574, 627
AbstractsBuffaloes(232), Cattle(77), Cattle(108), Cattle(179), Cattle(181), Cattle(200), Cattle(275), Cattle(283), Cattle(330), Cattle(333), Cattle(334), Cattle(380), Cattle(444), Cattle(476), Cattle(589), Cattle(630), Cattle(656), Cattle(683), Composition(156), Composition(186), Composition(207), Composition(476), Dairy(83), Dairy(218), Dairy(220), Dairy(319), Dairy(618), Degradability(419), Goats(38), Goats(212), Guinea-pigs(347), NaOH treatment(266), Pigs(73), Pigs(75), Pigs(144), Pigs(183), Pigs(462), Poultry(111), Poultry(149), Poultry(196), Poultry(217), Poultry(261), Poultry(318), Poultry(349), Poultry(423), Poultry(424), Poultry(531), Rabbits(57), Rabbits(216), Rabbits(221), Rabbits(347), Sheep(96), Sheep(212), Sheep(271), Sheep(441), Sheep(457), Sheep(682), Silage(108), Steam treatment(266), Tannin treatment(457), Toxicity(169), Toxicity(217), Toxicity(237), Toxicity(465), Turkeys(422)
Other papers by authors:
2594117April, 1952
Bonotto 260/123.5
Prepared cotton seed material for solvent extraction and processes for preparation and solvent extraction of cotton seed materials
3579496May, 1971
Martinez et al.
260/123.5
3615657October, 1971
Gastrock et al.
260/123.5PROCESS FOR PRODUCING COTTONSEED PROTEIN CONCENTRATE
3814748June, 1974
Olson et al.
260/123.5
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