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Article: Effects of Epinephrine, Detomidine, and Butorphanol on Assessments of Insulin Sensitivity in Mares.

Kerrigan, Lauren E / Thompson, Donald L / Chapman, Ann M / Oberhaus, Erin L

2019 Volume 85, Page(s) 102842

Abstract: Sympathoadrenal stimulation may perturb results of endocrine tests performed on fractious horses. Sedation may be beneficial; however, perturbation of results may preclude useful information. Four experiments were designed to 1) determine the effects of ... ...

Abstract	Sympathoadrenal stimulation may perturb results of endocrine tests performed on fractious horses. Sedation may be beneficial; however, perturbation of results may preclude useful information. Four experiments were designed to 1) determine the effects of epinephrine on insulin response to glucose (IR2G), 2) assess the effects of detomidine (DET), alone or combined with butorphanol (DET/BUT), on IR2G and glucose response to insulin (GR2I), and 3) assess the effects of BUT alone on IR2G. In Experiment 1, mares were administered saline or epinephrine (5 μg/kg BW) immediately before infusion of glucose (100 mg/kg BW). Glucose stimulated (P < .05) insulin release in controls at 5 minutes that persisted through 30 minutes; insulin was suppressed (P < .05) by epinephrine from 5 to 15 minutes, rising gradually through 30 minutes. Experiments 2 (IR2G) and 3 (GR2I) were conducted as triplicated 3 × 3 Latin squares with the following treatments: saline (SAL), DET, and DET/BUT (all administered at .01 mg/kg BW). Glucose stimulated (P < .05) insulin release that persisted through 30 minutes in SAL mares; DET and DET/BUT severely suppressed (P < .0001) the IR2G. Sedation did not affect resting glucose and had inconsistent effects on the GR2I when mares were treated with 50 mIU/kg BW recombinant human insulin. Butorphanol had no effect on IR2G. In conclusion, adrenergic agonists severely suppress the IR2G and cannot be used for sedation for this test. The use of DET did not alter the GR2I, and therefore may be useful for conducting this test in fractious horses.
MeSH term(s)	Animals ; Butorphanol ; Cross-Over Studies ; Epinephrine ; Female ; Horse Diseases ; Horses ; Imidazoles ; Insulin Resistance
Chemical Substances	Imidazoles ; detomidine (7N8K34P2XH) ; Butorphanol (QV897JC36D) ; Epinephrine (YKH834O4BH)
Language	English
Publishing date	2019-12-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2102631-2
ISSN	1542-7412 ; 0737-0806
ISSN (online)	1542-7412
ISSN	0737-0806
DOI	10.1016/j.jevs.2019.102842
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Article: Effects of Epinephrine, Detomidine, and Butorphanol on Assessments of Insulin Sensitivity in Mares

Kerrigan, Lauren E / Thompson, Donald L / Chapman, Ann M / Oberhaus, Erin L

Journal of equine veterinary science. 2020 Feb., v. 85

2020

Abstract	Sympathoadrenal stimulation may perturb results of endocrine tests performed on fractious horses. Sedation may be beneficial; however, perturbation of results may preclude useful information. Four experiments were designed to 1) determine the effects of epinephrine on insulin response to glucose (IR2G), 2) assess the effects of detomidine (DET), alone or combined with butorphanol (DET/BUT), on IR2G and glucose response to insulin (GR2I), and 3) assess the effects of BUT alone on IR2G. In Experiment 1, mares were administered saline or epinephrine (5 μg/kg BW) immediately before infusion of glucose (100 mg/kg BW). Glucose stimulated (P < .05) insulin release in controls at 5 minutes that persisted through 30 minutes; insulin was suppressed (P < .05) by epinephrine from 5 to 15 minutes, rising gradually through 30 minutes. Experiments 2 (IR2G) and 3 (GR2I) were conducted as triplicated 3 × 3 Latin squares with the following treatments: saline (SAL), DET, and DET/BUT (all administered at .01 mg/kg BW). Glucose stimulated (P < .05) insulin release that persisted through 30 minutes in SAL mares; DET and DET/BUT severely suppressed (P < .0001) the IR2G. Sedation did not affect resting glucose and had inconsistent effects on the GR2I when mares were treated with 50 mIU/kg BW recombinant human insulin. Butorphanol had no effect on IR2G. In conclusion, adrenergic agonists severely suppress the IR2G and cannot be used for sedation for this test. The use of DET did not alter the GR2I, and therefore may be useful for conducting this test in fractious horses.
Keywords	adrenergic agonists ; butorphanol ; detomidine ; epinephrine ; glucose ; humans ; insulin ; insulin resistance ; mares ; sedation
Language	English
Dates of publication	2020-02
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	2102631-2
ISSN	1542-7412 ; 0737-0806
ISSN (online)	1542-7412
ISSN	0737-0806
DOI	10.1016/j.jevs.2019.102842
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Article ; Online: Phagocytes: fussy about carbs.

Kerrigan, Ann M / Brown, Gordon D

Current biology : CB

2011 Volume 21, Issue 13, Page(s) R500–2

Abstract: A new mechanistic model based on the formation of a phagocytic synapse explains how immune cells detect and respond to direct contact with fungal pathogens. ...

Abstract	A new mechanistic model based on the formation of a phagocytic synapse explains how immune cells detect and respond to direct contact with fungal pathogens.
MeSH term(s)	Animals ; Cell Wall/chemistry ; Cell Wall/immunology ; Cells, Cultured ; Humans ; Immunity, Innate/immunology ; Immunological Synapses/immunology ; Lectins, C-Type ; Membrane Proteins/chemistry ; Membrane Proteins/immunology ; Membrane Proteins/metabolism ; Mice ; Models, Immunological ; Nerve Tissue Proteins/chemistry ; Nerve Tissue Proteins/immunology ; Nerve Tissue Proteins/metabolism ; Phagocytosis/immunology ; Reactive Oxygen Species/metabolism ; Saccharomyces cerevisiae/immunology ; Signal Transduction ; beta-Glucans/chemistry ; beta-Glucans/immunology ; beta-Glucans/metabolism
Chemical Substances	Lectins, C-Type ; Membrane Proteins ; Nerve Tissue Proteins ; Reactive Oxygen Species ; beta-Glucans ; dectin 1
Language	English
Publishing date	2011-07-12
Publishing country	England
Document type	Journal Article
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2011.05.041
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Article ; Online: Syk-coupled C-type lectins in immunity.

Kerrigan, Ann M / Brown, Gordon D

Trends in immunology

2011 Volume 32, Issue 4, Page(s) 151–156

Abstract: The Syk-coupled C-type lectin receptor Dectin-1 was the first non-Toll like receptor described that could mediate its own intracellular signalling. It was initially identified as important for the innate recognition of and response to fungal pathogens ... ...

Abstract	The Syk-coupled C-type lectin receptor Dectin-1 was the first non-Toll like receptor described that could mediate its own intracellular signalling. It was initially identified as important for the innate recognition of and response to fungal pathogens but later studies revealed that it is also involved in triggering adaptive immune responses. It subsequently emerged that Dectin-1 is one of a number of spleen tyrosine kinase-coupled C-type lectin receptors that have been implicated not just in fungal immunity, but also in viral, mycobacterial and helminth infections. Here, we consider the ability of these receptors to trigger different aspects of immunity and highlight their emerging roles in a number of infection scenarios.
MeSH term(s)	Animals ; Humans ; Intracellular Signaling Peptides and Proteins/metabolism ; Lectins, C-Type/immunology ; Lectins, C-Type/metabolism ; Ligands ; Membrane Proteins/immunology ; Nerve Tissue Proteins/immunology ; Protein Binding ; Protein-Tyrosine Kinases/metabolism ; Receptors, Calcitonin/immunology ; Syk Kinase
Chemical Substances	Intracellular Signaling Peptides and Proteins ; Lectins, C-Type ; Ligands ; Membrane Proteins ; Nerve Tissue Proteins ; Receptors, Calcitonin ; dectin 1 ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; SYK protein, human (EC 2.7.10.2) ; Syk Kinase (EC 2.7.10.2)
Language	English
Publishing date	2011-02-18
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2036831-8
ISSN	1471-4981 ; 1471-4906
ISSN (online)	1471-4981
ISSN	1471-4906
DOI	10.1016/j.it.2011.01.002
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Article ; Online: Syk-coupled C-type lectin receptors that mediate cellular activation via single tyrosine based activation motifs.

Kerrigan, Ann M / Brown, Gordon D

Immunological reviews

2010 Volume 234, Issue 1, Page(s) 335–352

Abstract: Different dendritic cell (DC) subsets have distinct specialized functions contributed in part by their differential expression of pattern recognition receptors (PRRs). C-type lectin receptors (CLRs) are a group of PRRs expressed by DCs and other myeloid ... ...

Abstract	Different dendritic cell (DC) subsets have distinct specialized functions contributed in part by their differential expression of pattern recognition receptors (PRRs). C-type lectin receptors (CLRs) are a group of PRRs expressed by DCs and other myeloid cells that can recognize endogenous ligands as well as a wide range of exogenous structures present on pathogens. Dual roles in homeostasis and immunity have been demonstrated for some members of this receptor family. Largely due to their endocytic ability and subset specific expression, DC-expressed CLRs have been the focus of significant antigen-targeting studies. A number of CLRs function on the basis of signaling via association with immunoreceptor tyrosine-based activation motif (ITAM)-containing adapter proteins. Others contain ITAM-related motifs or immunoreceptor tyrosine-based inhibitory motifs (ITIMs) in their cytoplasmic tails. Here we review CLRs that induce intracellular signaling via a single tyrosine-based ITAM-like motif and highlight their relevance in terms of DC function.
MeSH term(s)	Amino Acid Motifs ; Animals ; Dendritic Cells/enzymology ; Dendritic Cells/immunology ; Humans ; Intracellular Signaling Peptides and Proteins/immunology ; Lectins, C-Type/chemistry ; Lectins, C-Type/immunology ; Ligands ; Membrane Proteins/immunology ; Nerve Tissue Proteins/immunology ; Protein-Tyrosine Kinases/immunology ; Receptors, Mitogen/immunology ; Signal Transduction/immunology ; Syk Kinase ; Tyrosine
Chemical Substances	CLEC9a protein, human ; Intracellular Signaling Peptides and Proteins ; Lectins, C-Type ; Ligands ; Membrane Proteins ; Nerve Tissue Proteins ; Receptors, Mitogen ; dectin 1 ; Tyrosine (42HK56048U) ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; SYK protein, human (EC 2.7.10.2) ; Syk Kinase (EC 2.7.10.2)
Language	English
Publishing date	2010-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	391796-4
ISSN	1600-065X ; 0105-2896
ISSN (online)	1600-065X
ISSN	0105-2896
DOI	10.1111/j.0105-2896.2009.00882.x
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Article ; Online: Keeping a track on leptomeningeal disease in non-small cell lung cancer: A single-institution experience with CNSide

Puri, Sonam / Malani, Rachna / Chalmers, Anna / Kerrigan, Kathleen / Patel, Shiven B / Monynahan, Kelly / Cannon, Laura / Blouw, Barbara / Akerley, Wallace

Neuro-oncology advances

2023 Volume 6, Issue 1, Page(s) vdad150

Abstract: ... amplifications with therapeutic potential. The median survival for LMD patients was 16.1 m (5.2-NR ...

Abstract	Background: Leptomeningeal disease (LMD) is a devastating complication for patients with advanced cancer. Diagnosis and monitoring the response to therapy remains challenging due to limited sensitivity and specificity of standard-of-care (SOC) diagnostic modalities, including cerebrospinal fluid (CSF) cytology, MRI, and clinical evaluation. These hindrances contribute to the poor survival of LMD patients. CNSide is a CLIA-validated test that detects and characterizes CSF-derived tumor cells and cell-free (cf) DNA. We performed a retrospective analysis on the utility of CNSide to analyze CSF obtained from advanced non-small cell lung cancer (aNSCLC) patients with suspected LMD treated at the Huntsman Cancer Institute in Salt Lake City, UT. Methods: CNSide was used to evaluate CSF from 15 patients with aNSCLC. CSF tumor cell quantification was performed throughout treatment for 5 patients. CSF tumor cells and cfDNA were characterized for actionable mutations. Results: In LMD-positive patients, CNSide detected CSF tumor cells in 88% (22/25) samples versus 40% (10/25) for cytology (matched samples). CSF tumor cell numbers tracked response to therapy in 5 patients where CNSide was used to quantify tumor cells throughout treatment. In 75% (9/12) of the patients, genetic alterations were detected in CSF, with the majority representing gene mutations and amplifications with therapeutic potential. The median survival for LMD patients was 16.1 m (5.2-NR). Conclusions: We show that CNSide can supplement the management of LMD in conjunction with SOC methods for the diagnosis, monitoring response to therapy, and identifying actionable mutations unique to the CSF in patients with LMD.
Language	English
Publishing date	2023-12-09
Publishing country	England
Document type	Journal Article
ZDB-ID	3009682-0
ISSN	2632-2498 ; 2632-2498
ISSN (online)	2632-2498
ISSN	2632-2498
DOI	10.1093/noajnl/vdad150
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Article ; Online: C-type lectins and phagocytosis.

Kerrigan, Ann M / Brown, Gordon D

Immunobiology

2009 Volume 214, Issue 7, Page(s) 562–575

Abstract: To recognise and respond to pathogens, germ-line encoded pattern recognition receptors (PRRs) bind to conserved microbial structures and activate host defence systems, including microbial uptake by phagocytosis. Phagocytosis is a complex process that is ... ...

Abstract	To recognise and respond to pathogens, germ-line encoded pattern recognition receptors (PRRs) bind to conserved microbial structures and activate host defence systems, including microbial uptake by phagocytosis. Phagocytosis is a complex process that is instrumental in the control of extracellular pathogens, and this activity is mediated by several PRRs, including a number of C-type lectins. While some of these receptors have clearly been shown to mediate or regulate the uptake of pathogens, others are more contentious and are less well understood in terms of their phagocytic potential. Furthermore, very little is known about the underlying phagocytic mechanisms. Here, we review the phagocytic roles of the mannose receptor, Dectin-1, dendritic cell-specific ICAM grabbing non-integrin (DC-SIGN), DCL-1, mannose binding lectin and surfactant proteins A and D.
MeSH term(s)	Animals ; Complement Activation ; Host-Pathogen Interactions ; Humans ; Lectins, C-Type/immunology ; Lectins, C-Type/metabolism ; Phagocytosis/immunology ; Receptors, Pattern Recognition/immunology ; Signal Transduction/immunology
Chemical Substances	Lectins, C-Type ; Receptors, Pattern Recognition
Language	English
Publishing date	2009-03-03
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	563292-4
ISSN	1878-3279 ; 0171-2985
ISSN (online)	1878-3279
ISSN	0171-2985
DOI	10.1016/j.imbio.2008.11.003
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Article: Phagocytes: Fussy about Carbs

Kerrigan, Ann M / Brown, Gordon D

Current biology. 2011 July 12, v. 21, no. 13

2011

Abstract: A new mechanistic model based on the formation of a phagocytic synapse explains how immune cells detect and respond to direct contact with fungal pathogens. ...

Abstract	A new mechanistic model based on the formation of a phagocytic synapse explains how immune cells detect and respond to direct contact with fungal pathogens.
Keywords	direct contact ; fungi ; models ; pathogens ; phagocytes ; synapse
Language	English
Dates of publication	2011-0712
Size	p. R500-R502.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2011.05.041
Database	NAL-Catalogue (AGRICOLA)

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Z 2005/718: Show issues

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Article: Syk-coupled C-type lectins in immunity

Kerrigan, Ann M / Brown, Gordon D

Trends in immunology. 2011 Apr., v. 32, no. 4

2011

Abstract	The Syk-coupled C-type lectin receptor Dectin-1 was the first non-Toll like receptor described that could mediate its own intracellular signalling. It was initially identified as important for the innate recognition of and response to fungal pathogens but later studies revealed that it is also involved in triggering adaptive immune responses. It subsequently emerged that Dectin-1 is one of a number of spleen tyrosine kinase-coupled C-type lectin receptors that have been implicated not just in fungal immunity, but also in viral, mycobacterial and helminth infections. Here, we consider the ability of these receptors to trigger different aspects of immunity and highlight their emerging roles in a number of infection scenarios.
Keywords	fungi ; helminthiasis ; immune response ; lectins ; pathogens ; receptors ; spleen ; tyrosine
Language	English
Dates of publication	2011-04
Size	p. 151-156.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	2036831-8
ISSN	1471-4981 ; 1471-4906
ISSN (online)	1471-4981
ISSN	1471-4906
DOI	10.1016/j.it.2011.01.002
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Article ; Online: Dectin-1: a role in antifungal defense and consequences of genetic polymorphisms in humans.

Marakalala, Mohlopheni J / Kerrigan, Ann M / Brown, Gordon D

Mammalian genome : official journal of the International Mammalian Genome Society

2010 Volume 22, Issue 1-2, Page(s) 55–65

Abstract: The clinical relevance of fungal infections has increased dramatically in recent decades as a consequence of the rise of immunocompromised populations, and efforts to understand the underlying mechanisms of protective immunity have attracted renewed ... ...

Abstract	The clinical relevance of fungal infections has increased dramatically in recent decades as a consequence of the rise of immunocompromised populations, and efforts to understand the underlying mechanisms of protective immunity have attracted renewed interest. Here we review Dectin-1, a pattern recognition receptor involved in antifungal immunity, and discuss recent discoveries of polymorphisms in the gene encoding this receptor which result in human disease.
MeSH term(s)	Animals ; Fungi/immunology ; Fungi/physiology ; Humans ; Lectins, C-Type ; Membrane Proteins/genetics ; Membrane Proteins/immunology ; Mycoses/genetics ; Mycoses/immunology ; Mycoses/microbiology ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/immunology ; Polymorphism, Genetic
Chemical Substances	Lectins, C-Type ; Membrane Proteins ; Nerve Tissue Proteins ; dectin 1
Language	English
Publishing date	2010-08-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1058547-3
ISSN	1432-1777 ; 0938-8990
ISSN (online)	1432-1777
ISSN	0938-8990
DOI	10.1007/s00335-010-9277-3
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