scholarly journals The Role of Olfactory Genes in the Expression of Rodent Paternal Care Behavior

Genes ◽  
2020 ◽  
Vol 11 (3) ◽  
pp. 292 ◽  
Author(s):  
Tasmin L. Rymer
Keyword(s):  
Paternal Care ◽  
Sensory Modality ◽  
Odor Cues ◽  
Laboratory Rodents ◽  
Formyl Peptide ◽  
Parental Aggression ◽  
Olfactory Detection ◽  
Membrane Spanning ◽  
Care Behavior

Olfaction is the dominant sensory modality in rodents, and is crucial for regulating social behaviors, including parental care. Paternal care is rare in rodents, but can have significant consequences for offspring fitness, suggesting a need to understand the factors that regulate its expression. Pup-related odor cues are critical for the onset and maintenance of paternal care. Here, I consider the role of olfaction in the expression of paternal care in rodents. The medial preoptic area shares neural projections with the olfactory and accessory olfactory bulbs, which are responsible for the interpretation of olfactory cues detected by the main olfactory and vomeronasal systems. The olfactory, trace amine, membrane-spanning 4-pass A, vomeronasal 1, vomeronasal 2 and formyl peptide receptors are all involved in olfactory detection. I highlight the roles that 10 olfactory genes play in the expression of direct paternal care behaviors, acknowledging that this list is not exhaustive. Many of these genes modulate parental aggression towards intruders, and facilitate the recognition and discrimination of pups in general. Much of our understanding comes from studies on non-naturally paternal laboratory rodents. Future studies should explore what role these genes play in the regulation and expression of paternal care in naturally biparental species.

The Role of Formyl Peptide Receptors in Microbial Infection and Inflammation

2003 ◽  
Vol 2 (1) ◽  
pp. 83-93 ◽  
Author(s):  
Yingying Le ◽  
Ronghua Sun ◽  
Guoguang Ying ◽  
Pablo Iribarren ◽  
Ji Wang
Keyword(s):  
Microbial Infection ◽  
Peptide Receptors ◽  
Formyl Peptide Receptors ◽  
Formyl Peptide ◽  
Infection And Inflammation

scholarly journals The Possible Role of the Uropygial Gland on Mate Choice in Domestic Chicken

2011 ◽  
Vol 2011 ◽  
pp. 1-5 ◽  
Author(s):  
Atsushi Hirao
Keyword(s):  
Mate Choice ◽  
Visual Cues ◽  
Individual Recognition ◽  
Copulatory Behavior ◽  
Uropygial Gland ◽  
Odor Cues ◽  
Histocompatibility Complex ◽  
Efferent Projections ◽  
Opposite Sex

In avian mating systems, male domestic fowls are polygamous and mate with a number of selected members of the opposite sex. The factors that influence mating preference are considered to be visual cues. However, several studies have indicated that chemosensory cues also affect socio-sexual behavior, including mate choice and individual recognition. The female uropygial gland appears to provide odor for mate choice, as uropygial gland secretions are specific to individual body odor. Chicken olfactory bulbs possess efferent projections to the nucleus taeniae that are involved in copulatory behavior. From various reports, it appears that the uropygial gland has the potential to act as the source of social odor cues that dictate mate choice. In this review, evidence for the possible role of the uropygial gland on mate choice in domestic chickens is presented. However, it remains unclear whether a relationship exists between the uropygial gland and major histocompatibility complex-dependent mate choice.

The role of the membrane-spanning domain and stalk region of N-acetylglucosaminyltransferase I in retention, kin recognition and structural maintenance of the Golgi apparatus in HeLa cells

1996 ◽  
Vol 109 (7) ◽  
pp. 1975-1989 ◽  
Author(s):  
T. Nilsson ◽  
C. Rabouille ◽  
N. Hui ◽  
R. Watson ◽  
G. Warren
Keyword(s):  
Golgi Apparatus ◽  
Cell Lines ◽  
Hela Cells ◽  
Kin Recognition ◽  
Dramatic Effect ◽  
Golgi Stack ◽  
Stable Cell Lines ◽  
Membrane Spanning ◽  
Necessary And Sufficient

Using a series of chimeric and truncated N-acetylglucosaminyltransferase I (NAGT I) molecules we have shown that part of the lumenal stalk region is both necessary and sufficient for kin recognition of mannosidase II and retention in the Golgi stack. The membrane-spanning domain was not required for retention, but replacing part or all of this domain with leucine residues did have a dramatic effect on Golgi morphology. In stable cell lines, stacked cisternae were replaced by tubulo-vesicular clusters containing the mutated NAGT I. The loss of stacked cisternae was proportional to the number of leucines used to replace the membrane-spanning domain.

Role of the cytoskeleton in rapid activation of CD11b/CD18 function and its subsequent downregulation in neutrophils

2000 ◽  
Vol 113 (15) ◽  
pp. 2737-2745
Author(s):  
S.I. Anderson ◽  
N.A. Hotchin ◽  
G.B. Nash
Keyword(s):  
Cytochalasin D ◽  
Calpain Inhibitor ◽  
Cytoskeletal Rearrangement ◽  
Activated Platelets ◽  
Binding Inhibition ◽  
Formyl Peptide ◽  
Intracellular Ca ◽  
Rapid Activation ◽  
Dose Dependent

When rolling adherent neutrophils are stimulated, they rapidly immobilize through activation of integrin CD11b/CD18, and then modulate attachment through this integrin to allow migration. We investigated links between cytoskeletal rearrangement and changes in function of integrin CD11b/CD18 in neutrophils stimulated with formyl peptide (fMLP). Neutrophils treated with the actin-polymerizing agent jasplakinolide became rolling adherent on monolayers of activated platelets, but could not use CD11b/CD18 to become immobilised when fMLP was perfused over them. If treated with jasplakinolide after fMLP, the cells stopped migrating but could not detach when fMLP was removed. Jasplakinolide did not inhibit changes in intracellular Ca(2+) seen after fMLP treatment, or inhibit neutrophil immobilisation induced by externally added Mn(2+). Thus cytoskeletal rearrangement was directly implicated in upregulation and, later, downregulation of CD11b/CD18 binding. Inhibition of RhoA with C3-transferase caused a dose-dependent reduction of initial rolling adhesion of neutrophils, and reduced the rate of migration after stimulation; however, neither the conversion of rolling to stationary adhesion, nor the ability of neutrophils to detach on removal of the stimulus, were inhibited. Thus, Rho may regulate actin polymerisation and motility in neutrophils, but did not appear to control integrin-mediated adhesion itself. Integrin binding may be promoted by disruption of links to the cytoskeleton, effected through depolymerisation of actin or cleavage of linking protein talin by calpain. Disruption of actin filaments with cytochalasin D did not, however, cause integrin-mediated immobilisation of rolling neutrophils. Although the calpain inhibitor calpeptin did inhibit the adhesion response to fMLP, this was only at doses where actin polymerisation was also ablated. We suggest that the cytoskeleton actively regulates binding conformation of CD11b/CD18 as well as its mobility in the membrane.

scholarly journals Left Inferior Frontal Gyrus Integrates Multisensory Information in Category Learning

2020 ◽  
Vol 30 (8) ◽  
pp. 4410-4423
Author(s):  
You Li ◽  
Carol Seger ◽  
Qi Chen ◽  
Lei Mo
Keyword(s):  
Category Learning ◽  
Information Integration ◽  
Multisensory Processing ◽  
Inferior Frontal Gyrus ◽  
Sensory Modality ◽  
Precentral Gyrus ◽  
General Network ◽  
Multisensory Information ◽  
First Time

Abstract Humans are able to categorize things they encounter in the world (e.g., a cat) by integrating multisensory information from the auditory and visual modalities with ease and speed. However, how the brain learns multisensory categories remains elusive. The present study used functional magnetic resonance imaging to investigate, for the first time, the neural mechanisms underpinning multisensory information-integration (II) category learning. A sensory-modality-general network, including the left insula, right inferior frontal gyrus (IFG), supplementary motor area, left precentral gyrus, bilateral parietal cortex, and right caudate and globus pallidus, was recruited for II categorization, regardless of whether the information came from a single modality or from multiple modalities. Putamen activity was higher in correct categorization than incorrect categorization. Critically, the left IFG and left body and tail of the caudate were activated in multisensory II categorization but not in unisensory II categorization, which suggests this network plays a specific role in integrating multisensory information during category learning. The present results extend our understanding of the role of the left IFG in multisensory processing from the linguistic domain to a broader role in audiovisual learning.

Abstract 3283: The role of formyl peptide receptor 1 (FPR1) in neuroblastoma tumorigenesis

2015 ◽  
Author(s):  
Igor Snapkov ◽  
Carl Otto Öqvist ◽  
Yngve Anton Figenschau ◽  
Per Kogner ◽  
John Inge Johnsen ◽  
...  
Keyword(s):  
Formyl Peptide Receptor ◽  
Peptide Receptor ◽  
Formyl Peptide

Cloning and epitope mapping of a functional partial fusion receptor for human cytomegalovirus gH

Microbiology ◽  
2000 ◽  
Vol 81 (1) ◽  
pp. 27-35 ◽  
Author(s):  
Brenda R. Baldwin ◽  
Chen-Ou Zhang ◽  
Susan Keay
Keyword(s):  
Human Cytomegalovirus ◽  
Viral Envelope ◽  
Nuclear Localization Signals ◽  
Synthetic Receptor ◽  
Hydrophilic Region ◽  
Receptor Cdna ◽  
Cell Membrane Protein ◽  
Membrane Spanning ◽  
Fusion Receptor

A cDNA clone encoding a partial putative human cytomegalovirus (HCMV) gH fusion receptor (CMVFR) was previously identified. In this report, the cDNA sequence of CMVFR was determined and the role of this CMVFR in HCMV/cell fusion was confirmed by rendering fusion-incompetent MOLT-4 cells susceptible to fusion following transfection with receptor cDNA. Blocking experiments using recombinant gH or either of two MAbs (against recombinant gH or purified viral gH:gL) provided additional evidence for the role of gH binding to this protein in virus fusion. An HCMV-binding domain of 12 aa in the middle hydrophilic region of CMVFR was identified by fusion blocking studies using synthetic receptor peptides. The 1368 bp cDNA of CMVFR contained a predicted ORF of 345 aa with two potential membrane-spanning domains and several possible nuclear localization signals. A search of sequence databases indicated that CMVFR is a novel protein. Further characterization of this cell membrane protein that confers susceptibility to fusion with the viral envelope should provide important information about the mechanism by which HCMV infects cells.

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