“Day, n. A period of twenty-four hours, mostly misspent.” Ambrose Bierce (1842-1913)

"Gross ignorance: 144 times worse than ordinary ignorance. " Bennet Cerf (1898-1971)

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Future Brain Talks


None currently planned.


_____________________________________________

Previous Brain Talks


June 20th, 2014

Presenter: Ramsay B.

Topic:  A 'Google Maps' for the brain.


April 11th, 2014

Presenter: Bart DJ. (UPenn, Profile)

Topic:  The neural control of nausea and emesis.


February 24th, 2014

Presenter: Mihail B.

Topic: The rat cerebral cortex macro-connectome.


January 27th, 2014

Presenter: Ruth W.

Topic: Investigations into the addictive properties of anabolic steroids.


December 6, 2013

Presenter: Scott K.

Topic Gut brain signalling and the cognitive control of ingestive behavior.


October 21st, 2013

Presenter: Alan W.

Topic Relating the circuits for neuroendocrine control to the integrated control of behavior.


September 13, 2013

Presenter: Joel H.

Topic Towards an understanding of the structure and function of the lateral hypothalamic area.


May 10, 2012

Presenter: Joel H.

Topic From the discovery of antibodies to the development of ingenious methods for their use as tools in immunohistolology.

Presentation (PDF format, with some additions and revisions from the presented slides) [FILE LINK]

Some points of clarification

    Figure 1 in Ludwig Sternberger’s (et al.) 1970 article on the horseradish peroxidase (HRP) anti HRP method (HRP anti HRP; condensed to the abbreviation PAP) (Fig. 1 reproduced below) looks rather crude to contemporary eyes, with rod-shaped oblongs representing the antibodies, and nondescript blobs representing the HRP molecules.


    It’s also potentially misleading, because the enzyme-bound antibodies are represented by kinked oblongs which resemble the typical current representation of the fragment antigen binding (Fab) region of an antibody (the arms of the familiar ‘Y’ shape), rather than the entire antibody including the fragment crystalizable (Fc) region (which is what in fact they are). Looking again at Fig. 1 one can see that although a rod-shaped appearance was used for all the antibodies depicted (with an angular fold for the PAP antibodies), confusingly the anti HRP antibodies are shown without the concave ends (presumably representing binding sites) depicted on the other antibodies. Adding to the confusion, a more typical ‘Y’-shaped representation is shown for the PAP antibody complex in the same paper in Fig. 12 (reproduced below).


    An appreciation of the historical context helps to resolve the confusion. In 1970 when the Sternberger et al. article was published, our understanding of antibody structure was still in its infancy. In fact it was just a year later that a three-dimensional model of antibody structure based on X-ray crystallography data was put forward: It was shown as a ‘T’ shape (Sarma et al. 1971). A clue to the choice of antibody depiction in Fig. 1 may also be found in the text of the Sternberger article, where in the discussion (and citing earlier work – i.e. work even less likely to be informative of antibody structure) he writes “Free antibody or antibody combined with particulate antigen in excess apparently is rod-shaped.”

    If that wasn’t confusing enough, in 1980 a different group of researchers did produce immunoglobulins composed solely of the anti-HRP Fab region! (Slemmon et al. 1980) The rationale for the use of Fab fragments instead of the whole antibody was simple and two-fold: It was hypothesized that antibodies lacking the Fc region would be (1) less prone to non-specific attachments, and that a smaller complex would achieve (2) better tissue penetration; for thoughts on this at around the same time see Brandon (1984). Subsequently it was realized that there are numerous possible applications for antibody fragments. For some thoughts on their practical use in relation to immunohistochemistry, the following technical note (produced by ThermoScientific in 2007) is an informative starting point (specifically in relation to secondary antibodies, but more generally informative too): [FILE LINK] Choosing a secondary antibody: A guide to fragment specificity.

    Another question that arose from the talk was the nomenclature applied to describe the various parts of an antibody. In particular what “Fab” represents in relation to “(Fab’)2”. Well, to begin with the antibody schematic that I showed in the talk was plundered from the internet (in fact from the site of the commercial antibody supplier abcam) [reproduced below, and WEB LINK], and it is incorrectly labeled.


    The label “(Fab’)2” should in fact be “F(ab’)2“. It is also not entirely clear what part(s) of the antibody each label represents. By way of answer to the original question, an amended diagram is shown below (also amended on the slide in the presentation file), and this illustrates the difference between the terms “Fab” and “F(ab’)2


    An aside: The answer to the question also alludes to how the molecular structure of antibodies was discovered, and with regard to the people at the forefront of that discovery, in addition to Gerald Edelman whom I mentioned, I neglected to mention the contribution of the biochemist Rodney Porter: In 1972 both men were jointly awarded a Nobel prize for their work.

    Returning to the original question, and with reference to the amended diagram above, in this context the prime (‘) symbol is a loose borrowing of the chemical notation used to distinguish between different functional groups connected to an atom in a single molecule (and should not be confused with its other uses – which are numerous – in particular its use in molecular biology to indicate the location of a ribose or deoxyribose on a carbon ring, viz. 3’ or 5’). Here the different ‘functional groups’ are the two configurations indicated by the red and green boxes. Taken together (if one includes both Fab moieties) they are chemically rather similar but differ as a result of a difference in the site of cleavage at the hinge region of the antibody (shown in black). Cleavage on the N-terminus side of the disulfide bonds (achieved by the action of the enzyme papain – obtained from the papaya fruit!) results in two separate moieties, each identical; whereas cleavage on the C-terminus side of the disulfide bonds (achieved by the action of the enzyme pepsin) results in a single moiety. The use of parenthesis and a subscript “2” simply indicate that the fragment (F) is composed of two of identical “ab(prime)” moities, with the prime symbol being used to indicate specifically that there is a molecular difference between these two identical and linked “ab(prime)“ moieties (produced by the action of pepsin) and the non-linked “ab” moities produced by the action of papain. In contrast, the incorrect notation (Fab’)2 implies two separate ab´ fragments, but clearly this is not the case: There is one fragment, composed of two ab’ moieties linked by disulfide bonds on the heavy chains, hence F(ab’)2.

    A nicely succinct piece on the discovery of antibody molecular structure can be found here [WEB LINK]. For a more in-depth exploration of the discovery of antibody structure, an alternative starting point is the web site of the Nobel Prize: [WEB LINK] 1972 prize in physiology or medicine awarded to the English biochemist Rodney Porter and the American biologist Gerald Edelman.

    Moving on: A question was raised on the issue of ‘background’ signal; on that point, the following recent and controversial article provides much food for thought: [ARTICLE] Non-specific binding of antibodies in immunohistochemistry: fallacies and facts. Igor Buchwalow et al. Nature Scientific Reports (2011).

    And finally, an additional person of interest in development of immunohistochemical methods whom I did not mention (but they deserve a mention) is Paul Nakane. His most widely known contribution (probably) is the direct labeling of antibodies with enzymes (in contrast to using enzymes as an immunogen – as in the PAP method). A selection of Nakane's papers is given in the reference list below (with direct links to some).

Some points of trivia for the curious / nerds

    Three of the articles I referred to in the talk (each a classic in the history of immunohistochemistry) are among the most cited articles (as of 2012) published in the Journal of Histochemistry and Cytochemistry

The No. 1 spot goes to:

Su-Ming Hsu, L Raine and H Fanger. Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: a comparison between ABC and unlabeled antibody (PAP) procedures. J Histochem Cytochem April 1981 29: 577-80.

At number 7:

Ludwig A. Sternberger, PH Hardy, jr., JJ Cuculis and HG Meyer. The unlabeled antibody enzyme method of immunohistochemistry preparation and properties of soluble antigen-antibody complex (horseradish peroxidase-antihorseradish peroxidase) and its use in identification of spirochetes j histochem cytochem may 1970 18: 315-333.

And at number 13:

Joe C. Adams. Biotin amplification of biotin and horseradish peroxidase signals in histochemical stains. J Histochem Cytochem October 1992 40: 1457-63.

Of related interest, and also in the top 20 list (at number 4), an alternative to Sternberger’s P-A-P method, employing a different enzyme (namely alkaline phosphatase), that was published more than a decade later:

L Cordell, B Falini, W N Erber, A K Ghosh, Z Abdulaziz, S MacDonald, K A Pulford, H Stein and D Y Mason. Immunoenzymatic labeling of monoclonal antibodies using immune complexes of alkaline phosphatase and monoclonal anti-alkaline phosphatase (APAAP complexes). J Histochem Cytochem February 1984 32: 219-29.

    On a side note, the work of Coons and Kaplan predated the first edition of the Journal of Histochem and Cytochem, which appeared in January 1953. For the very curious / excessively nerdy, the J Histochem Cytochem most-cited list makes for interesting reading [LINK].

Reference List

(Includes additional articles of interest not mentioned in the talk or text above.)

Adams JC. 1992. Biotin amplification of biotin and horseradish peroxidase signals in histochemical stains. J Histochem Cytochem 40(10):1457-63. [PDF]

Brandon C. 1985. Improved immunocytochemical staining through the use of Fab fragments of primary antibody, Fab-specific second antibody, and Fab-horseradish peroxidase. J Histochem Cytochem 33(7):715-9.

Buchwalow I, Samoilova V, Boecker W, Tiemann M. 2011. Non-specific binding of antibodies in immunohistochemistry: fallacies and facts. Sci Rep 1:28. [PDF]

Coons AH, Creech HJ, Jones N, Berliner E. 1942. The demonstration of pneumococcal antigen in tissues by the use of fluorescent antibody. J Immunol 45:159-70. [PDF]

Coons AH, Kaplan MH. 1950. Localization of antigen in tissue cells; improvements in a method for the detection of antigen by means of fluorescent antibody. J Exp Med 91(1):1-13. [PDF]

Davies DR, Sarma R, Labaw LW, Silverton E, Segal D, Terry WD. 1971. X-ray diffraction and electron microscope studies on a crystalline human immunoglobulin. Ann N Y Acad Sci 190:122-9.

Edelman GM, Cunningham BA, Gall WE, Gottlieb PD, Rutishauser U, Waxdal MJ. 1969. The covalent structure of an entire gammaG immunoglobulin molecule. Proc Natl Acad Sci U S A 63(1):78-85. [PDF]

Harris LJ, Larson SB, Hasel KW, Day J, Greenwood A, McPherson A. 1992. The three-dimensional structure of an intact monoclonal antibody for canine lymphoma. Nature 360(6402):369-72. [PDF]

Hsu S-MM. 1993. Avidin-Biotin detection methods (Current Contents Classic Citation). Current Contents 36(18):9. [PDF]

Hsu SM, Raine L, Fanger H. 1981. Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: a comparison between ABC and unlabeled antibody (PAP) procedures. J Histochem Cytochem 29(4):577-80. [PDF]

Kaplan ME, Coons AH, Deane HW. 1950. Localization of antigen in tissue cells; cellular distribution of pneumococcal polysaccharides types II and III in the mouse. J Exp Med 91(1):15-30, 4.

Nakane PK, Pierce GB, Jr. 1967. Enzyme-labeled antibodies for the light and electron microscopic localization of tissue antigens. J Cell Biol 33(2):307-18. [PDF]

Nakane PK, Kawaoi A. 1974. Peroxidase-labeled antibody. A new method of conjugation. J Histochem Cytochem 22(12):1084-91. [PDF]

Nakane PK. 1975. Recent progress in the peroxidase-labeled antibody method. Ann N Y Acad Sci 254:203-11. [PDF]

Nakane PK. 1992. Modern histochemical methods using enzymes as markers. J Immunol Methods 150(1-2):151-8.

Padlan EA. 1996. X-ray crystallography of antibodies. Adv Protein Chem 49:57-133. [PDF]

Putnam FW. 1969. Immunoglobulin structure: variability and homology. Science 163(3868):633-44. [PDF]

Sarma VR, Silverton EW, Davies DR, Terry WD. 1971. The three-dimensional structure at 6 A resolution of a human gamma Gl immunoglobulin molecule. J Biol Chem 246(11):3753-9. [PDF]

Sarma VR, Davies DR, Labaw LW, Silverton EW, Terry WD. 1972. Crystal structure of an immunoglobulin molecule by x-ray diffraction and electron microscopy. Cold Spring Harb Symp Quant Biol 36:413-9.

Silverton EW, Navia MA, Davies DR. 1977. Three-dimensional structure of an intact human immunoglobulin. Proc Natl Acad Sci U S A 74(11):5140-4. [PDF]

Slemmon JR, Salvaterra PM, Saito K. 1980. Preparation and characterization of peroxidase: antiperoxidase-Fab complex. J Histochem Cytochem 28(1):10-5.

Sternberger LA, Hardy PH, Jr., Cuculis JJ, Meyer HG. 1970. The unlabeled antibody enzyme method of immunohistochemistry: preparation and properties of soluble antigen-antibody complex (horseradish peroxidase-antihorseradish peroxidase) and its use in identification of spirochetes. J Histochem Cytochem 18(5):315-33. [PDF]

External Links

Paul Ehrlich (coined the term antibody) biography and Nobel prize award address [LINK]


May 2, 2012

Presenter: Ramsay B.

Topic Structure, function, and connectivity; intersection, interface, and inference: Proof-of-concept testing a possible new method for simultaneously generating data on both structure/function mappings and neural connectivity. And discussion of recent work to develop new models of integrating and visualizing novel and existing information. Audio recording available on request.


April 19, 2012

Presenter: Mihai B.

Topic Neuroanatomical and gene expression patterns correlations in the rat BST.
Related Reading: Bota M, Sporns O, Swanson LW. (2012) Neuroinformatics analysis of molecular expression patterns and neuron populations in gray matter regions: The rat BST as a rich exemplar.  Brain Res. 1450:174-93. (link to article via PubMed: http://www.ncbi.nlm.nih.gov/pubmed/22421015); see also the revamped (in development) http://brancusi1.usc.edu/ and original (http://brancusi.usc.edu/bkms/) Brain Architecture Management System (BAMS) websites. Audio recording available on request.


April 4, 2012

Presenter: Alan W.

Topic:  Structure-Function Relationships in Central Glucoregulatory Networks.
Related Reading: Watts & Donovan, 2010


March 22, 2012

Presenter: Claudia M.

Topic: An introduction to the lateral hypothalamic area, posterior region (LHAp).

Presentation (click open)

Related reading: Gritti et al., 1994; Allen & Cechetto, 1992, 1993; Saper, 1985


March 8, 2012

Presenter: Rick T. (with input from Chris B.)

Topic: An innovative approach to cataloging and accessing the Swanson group tract-tracing experiments archive.

Presentation (click open)


December 6, 2011

Presenter: Claudia M.

Topic: Studies of embryonic stem cell derived ventral midbrain dopaminergic neurons.

Presentation (click open)

Related readingTamariz et al., 2010Rodriguez-Gomez et al., 2007


November 29, 2011

Presenter: Alan W.

Topic: Discussion of approaches to quantitative analysis of immunohistochemically identified molecules.


November 8, 2011

Presenter: Sarah V.

Topic: (Research Article) A potential role for hypothalamomedullary POMC projections in leptin induced suppression of food intake. Huiyuan Zheng, Laurel M. Patterson, Christopher J. Rhodes, Gwendolyn W. Louis, Karolina P. Skibicka, Harvey J. Grill, Martin G. Myers, Jr., and Hans-Rudolf Berthoud. Am J Physiol Regul Integr Comp Physiol (2010) 298: R720-8


AbstractMelanocortin-3/4 receptor ligands administered to the caudal brain stem potently modulate food intake by changing meal size. The origin of the endogenous ligands is unclear, because the arcuate nucleus of the hypothalamus and the nucleus of the solitary tract (NTS) harbor populations of proopiomelanocortin (POMC)-expressing neurons. Here we demonstrate that activation of hypothalamic POMC neurons leads to suppression of food intake and that this suppression is prevented by administration of a melanocortin-3/4 receptor antagonist to the NTS and its vicinity. Bilateral leptin injections into the rat arcuate nucleus produced long-lasting suppression of meal size and total chow intake. These effects were significantly blunted by injection of SHU-9119 into the fourth ventricle, although SHU-9119 increased meal size and food intake during the first, but not the second, 14-h observation period. Leptin effects on meal size and food intake were abolished throughout the 40-h observation period by injection of SHU-9119 into the NTS at a dose that by itself had no effect. Neuron-specific tracing from the arcuate nucleus with a Cre-inducible tract-tracing adenovirus in POMC-Cre mice showed the presence of labeled axons in the NTS. Furthermore, density of .alpha-melanocyte-stimulating hormone-immunoreactive axon profiles throughout the NTS was decreased by ~70% after complete surgical transection of connections with the forebrain in the chronic decerebrate rat model. The results further support the existence of POMC projections from the hypothalamus to the NTS and suggest that these projections have a functional role in the control of food intake.

[Presentation FILE]


September 27, 2011

PART 2 of 2

Presenter: Edward P.

Topic: (Research Article) Critical role of neuropeptides B/W receptor 1 signaling in social behavior and fear memory. Nagata-Kuroiwa R, Furutani N, Hara J, Hondo M, Ishii M, Abe T, Mieda M, Tsujino N, Motoike T, Yanagawa Y, Kuwaki T, Yamamoto M, Yanagisawa M, Sakurai T. PLoS One (2011) 6(2):e16972.


AbstractNeuropeptide B/W receptor 1 (NPBWR1) is a G-protein coupled receptor, which was initially reported as an orphan receptor, and whose ligands were identified by this and other groups in 2002 and 2003. To examine the physiological roles of NPBWR1, we examined phenotype of Npbwr1⁻/⁻ mice. When presented with an intruder mouse, Npbwr1⁻/⁻ mice showed impulsive contact with the strange mice, produced more intense approaches toward them, and had longer contact and chasing time along with greater and sustained elevation of heart rate and blood pressure compared to wild type mice. Npbwr1⁻/⁻ mice also showed increased autonomic and neuroendocrine responses to physical stress, suggesting that impairment of NPBWR1 leads to stress vulnerability. We also observed that these mice show abnormality in the contextual fear conditioning test. These data suggest that NPBWR1 plays a critical role in limbic system function and stress responses. Histological and electrophysiological studies showed that NPBWR1 acts as an inhibitory regulator on a subpopulation of GABAergic neurons in the lateral division of the CeA and terminates stress responses. These findings suggest important roles of NPBWR1 in regulating amygdala function during physical and social stress.


Presentation Materials (click to open files)Power Point,  Article PDF


September 20, 2011

PART 1 of 2

Presenter: Edward P.

Topic: (Research Article) Critical role of neuropeptides B/W receptor 1 signaling in social behavior and fear memory. Nagata-Kuroiwa R, Furutani N, Hara J, Hondo M, Ishii M, Abe T, Mieda M, Tsujino N, Motoike T, Yanagawa Y, Kuwaki T, Yamamoto M, Yanagisawa M, Sakurai T. PLoS One (2011) 6(2):e16972.


AbstractNeuropeptide B/W receptor 1 (NPBWR1) is a G-protein coupled receptor, which was initially reported as an orphan receptor, and whose ligands were identified by this and other groups in 2002 and 2003. To examine the physiological roles of NPBWR1, we examined phenotype of Npbwr1⁻/⁻ mice. When presented with an intruder mouse, Npbwr1⁻/⁻ mice showed impulsive contact with the strange mice, produced more intense approaches toward them, and had longer contact and chasing time along with greater and sustained elevation of heart rate and blood pressure compared to wild type mice. Npbwr1⁻/⁻ mice also showed increased autonomic and neuroendocrine responses to physical stress, suggesting that impairment of NPBWR1 leads to stress vulnerability. We also observed that these mice show abnormality in the contextual fear conditioning test. These data suggest that NPBWR1 plays a critical role in limbic system function and stress responses. Histological and electrophysiological studies showed that NPBWR1 acts as an inhibitory regulator on a subpopulation of GABAergic neurons in the lateral division of the CeA and terminates stress responses. These findings suggest important roles of NPBWR1 in regulating amygdala function during physical and social stress.


Presentation Materials (click to open files)Power Point,  Article PDF


August 30, 2011

Presenter: Scott W.

Topic: (Research Article) A Study of the Rat Neuropeptide B/Neuropeptide W System Using In Situ Techniques. Jackson, VR., Lin, SH., Wang, Z., Nothacker, H-S and Civelli, O. Journal of Comparative Neurology (2006) 497: 367-383.


Abstract: In the rat, the neuropeptide B/neuropeptide W (NPB/NPW) system is composed of two ligands, neuropeptide B (NPB) and neuropeptide W (NPW), and one receptor, GPR7. Although preliminary analyses show roles in feeding, hormone secretion, and analgesia, the lack of a detailed anatomical map impairs our understanding of the NPB/NPW system. We demonstrate in this report the expression patterns of GPR7, NPB, and NPW precursor messenger ribonucleic acid (mRNA) in the rat brain by using in situ hybridization and in situ binding experiments. The amygdala expresses the highest levels of GPR7 mRNA and binding signals. Other nuclei with high levels of expression and binding are the suprachiasmatic and the ventral tuberomamillary nuclei. Moderate levels are seen in the dorsal endopiriform, dorsal tenia tecta, bed nucleus, and the red nucleus. Low levels are in the olfactory bulb, parastrial nucleus, hypothalamus, laterodor-sal tegmentum, superior colliculus, locus coeruleus, and the nucleus of the solitary tract. Al-though the NPB precursor is mostly expressed at low levels in the brain, moderate expression is seen in anterior olfactory nucleus, piriform cortex, median preoptic nucleus, basolateral amyg-dala, hippocampus, medial tuberal nucleus, substantia nigra, dorsal raphe nucleus, Edinger-Westphal nucleus, and the locus coeruleus. To our surprise, the expression of NPW precursor was not detected. Our study greatly expands the preliminary in situ data previously reported. With this map of the NPB/NPW system in the rat brain, a better understanding of the functional implications of the system in various behavioral paradigms is now possible. 


Presentation Materials (click to open files)Power Point,  Article PDF


August 15, 2011

Presenter: Josh N.

Topic: (Research Article) Neuropeptide B immunoreactivity in the central nervous system of the rat. Dun SL., Brailoiu GC., Mizuo, K., Yang, J., Chang, JK and Dun, NJ. Brain Research (2005) 1045: 157-163.


Abstract: Neuropeptide B (NPB) is a recently identified endogenous ligand for the orphan G protein-coupled receptors GPR7 and GPR8. NPB mRNA is expressed in the human, rat, and mouse brain. With the use of an antiserum directed against the rat NPB, immunoreactivity to NPB (irNPB) was detected in several discrete areas of the hypothalamus and midbrain. In the hypothalamus, irNPB cells were present in the medial preoptic area and nucleus, ventromedial preoptic nucleus, retrochiasmatic nucleus, paraventricular hypothalamic nucleus, supraoptic nucleus, accessory neurosecretory nuclei, periventricular hypothalamic nucleus, dorsomedial hypothalamic nucleus, supraoptic retrochiasmatic nucleus, lateral hypothalamic area, posterior hypothalamic area, dorsal hypothalamic area, and zona incerta. A few irNPB perikarya were noted in the arcuate nucleus, whereas a dense network of nerve fibers was present in the median eminence. In the midbrain, irNPB somata were noted in the substantia nigra (compact, reticular, medial, and lateral parts), paranigral nucleus, ventral tegmental area, interfascicular nucleus, and dorsal raphe nucleus. Neurons in the Edinger–Westphal were strongly labeled. Labeled cells were not detected in the cortex, medulla oblongata, and spinal cord; few lightly labeled cells were occasionally seen in the hippocampus. Double labeling the hypothalamic sections with NPB antiserum and vasopressin or oxytocin antibody revealed that a population of vasopressin- but not oxytocin immunoreactive cells was irNPB. Tyrosine hydroxylase-positive neurons in the midbrain, presumably dopaminergic, were irNPB. The distribution of irNPB neurons in several areas of the hypothalamus and midbrain together with the colocalization with vasopressin or tyrosine hydroxylase suggests that the peptide may subserve neuroendocrine, autonomic, and motor functions.


Presentation Materials (click to open files): Power Point,  Article PDF


July 29, 2011

Presenter: Joel H.

Topic: (Editorial) Magic Peptides, Magic Antibodies: Guidelines for Appropriate Controls for Immunohistochemistry. Saper CB and Sawchenko PE. Journal of Comparative Neurology (2003) 465: 161-163

Abstract: Since the earliest days of immunohistochemistry, the field has been troubled by the tendency for these methods to give spurious results. There are a number of reasons why various antibody preparations may provide variable and even erroneous results, and a series of steps one can take to control for this. Unfortunately, these are not as widely known as we feel they should be, even as we enter the fourth decade in which these methods have been widely available to neuroanatomists. Hence, we provide this editorial to help guide aspiring authors through the rocky shoals of immunolocalization in the nervous system.

Presentation Materials (click to open files): PowerPointArticle PDF

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Previous Brain Walks


January 18th 2006

Presenter: Gert Holstege 

Topic: Neuroscience and the End of Philosophy

This talk was given as a special seminar to students enrolled on the course "Brain Control of the Emotions" (aimed at senior undergraduates in biological science/neuroscience - USC course code BISC 462). Prof Holstege talked about his research, including recent work on the expression of sexual emotions in humans, and the implications of this work for neurobiology and philosophy. A selection of research articles from Prof. Holstege relevant to this talk are posted below.

1. Georgiardis JR et al - EJN 24(11) 2006 - brain activity during female orgasm (PDF)

2. Georgiadis JR & Holstege G - JCN 493(1) 2005 - human brain activation during sexual penile stimulation (PDF)

3. Holstege G - JCN 493(1) 2005 - micturition and the soul (PDF)

 

December 21st 2006

Presenter: Floyd G

Topic: Swallowing (part II).


December 14th 2006

Presenter: Floyd G

Topic: Swallowing (part I).

Hamdy S - GI Motility Online (2006) - Role of cerebral cortex in the control of swallowing.

  

November 16th 2006

Presenter: Larry S. 

Topic: The enteric nervous system

Furness JB et al - Prog in Neurobiol 72 (2) 2004 - Intrinsic primary afferent neurons and nerve circuits within the intestine.

Szurszewski JH et al - Gut 51(1) 2002 - Prevertebral ganglia and intestinofugal afferent neruones.

 

November 2nd 2006

Presenter: Larry S.

Topic: Sympathetic ganglia 

October 26sth 2006 

Presenter: Larry S. 

Topic: The origin and course of the wandering nerve (aka the vagus nerve)


September 21st 2006

Presenter: Larry S.

Topic: Cranial parts of the parasympathetic system.


Presenters: Larry S.

Topic: From the somatic to the visceral nervous system with a historical perspective.


June 1st 2006 

Presenters: Larry S.

Topic: The peripheral nervous system: somatic motor/sensory system (part III).

 

May 25th 2006

Presenter: Larry S.

Topic: The peripheral nervous system: somatic motor/sensory system (part II).

 

May 11th 2006

Presenter: Larry S.

Topic: The peripheral nervous system: somatic motor/sensory (part I).

 

April 27th 2006

Speaker: Larry S.

Topic: Somatic and autonomic divisions of the visceral nervous system (part II).

 

April 20th 2006

Speaker: Larry S.

Topic: Somatic and autonomic divisions of the visceral nervous system (part I).

 

April 13th 2006 

Presenter: Larry S.

Topic: Overview of the development of the visceral nervous system: evolutionary and embryological perspective.