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, 452

The 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
 Other papers by authors:

Prepared cotton seed material for

April, solvent extraction and processes for
2594117 Bonotto 260/123.5
1952 preparation and solvent extraction
of cotton seed materials
May, Martinez
3579496 260/123.5
1971 et al.
PROCESS FOR PRODUCING
October, Gastrock
3615657 260/123.5 COTTONSEED PROTEIN
1971 et al.
CONCENTRATE
June, Olson et
3814748 260/123.5
1974 al.