Objective: Vascular damage and ischemia-like changes in glutamate distribution occur in primary glaucoma (PG) in dogs. We measured the microvessel density in PG retinas to determine whether microvessel loss may induce ischemia and glutamate redistribution.
Animals Studied: Sections from 12 control and 33 glaucomatous dog retinas.
Procedures: Vessels in retinas were identified by staining with Griffonia simplicifolia isolectin B4 or immunohistochemical staining for laminin or glutamate. Damage to regions of the inner nuclear layer (INL) was classified as mild (< 10% damaged neurons), moderate (> or = 10% damaged neurons, INL > or = 2 cells thick) or severe (INL < 2 cells thick).
Results: Glutamate redistribution was found in some mildly damaged regions and increased as damage increased. Regions with increased glutamate redistribution and increased damage had lower densities of microvessels in plastic sections. However, neuronal damage and glutamate redistribution were seen even in areas adjacent to the remaining microvessels. Microvessel loss in damaged regions was confirmed in paraffin sections with lectin staining and immunohistochemical localization of laminin. The density of larger vessels was not decreased in PG, but larger vessels often had thickened walls, cuffing with leukocytes, and leakage of albumin.
Conclusions: Microvessel loss may occur in regions of glutamate redistribution and neuronal damage in PG retinas. Larger vessels were often damaged. The redistribution of glutamate is associated with a loss of microvessels, even in mildly damaged regions. However, neuronal damage and glutamate redistribution may occur close to remaining microvessels, suggesting microvessel loss was not the sole factor inducing these changes.
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http://dx.doi.org/10.1111/j.1463-5224.2007.00562.x | DOI Listing |
Metab Eng
December 2024
State Key Laboratory of Biocatalysis and Enzyme Engineering, Environmental Microbial Technology Center of Hubei Province, College of Life Sciences, Hubei University, Wuhan, 430062, China. Electronic address:
Microbial cell factories (MCFs) have emerged as a sustainable tool for the production of value-added biochemicals. However, developing high-performance MCFs remains a major challenge to fulfill the burgeoning demands of global markets. This study aimed to establish the B.
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Department of Pharmacological and Biomolecular Sciences 'Rodolfo Paoletti', Università degli Studi di Milano, Milan, Italy.
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Department of Soil and Crop Sciences, Texas A&M University and Texas A&M AgriLife, College Station, TX, United States.
Root exudation of N is a plant input to the soil environment and may be differentially regulated by the plant during drought. Organic N released by root systems has important implications in rhizosphere biogeochemical cycling considering the intimate coupling of C and N dynamics by microbial communities. Besides amino acids, diverse molecules exuded by root systems constitute a significant fraction of root exudate organic N but have yet to receive a metabolomic and quantitative investigation during drought.
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Centre for Brain Research and Department of Pharmacology and Clinical Pharmacology, University of Auckland, New Zealand. Electronic address:
Alzheimer's disease (AD) has complex pathophysiology involving numerous cell types and brain processes. Astrocyte involvement in AD is gaining increased attention, however a complete characterisation of astrocytic changes in the AD human brain is warranted. Astrocytes perform important homeostatic functions including regulation of the extracellular microenvironment, critical for the health of all brain cells.
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School of Life Science, Lanzhou University, No. 222 South Tianshui Road, Lanzhou, 730000, Gansu, P R China.
Protein tyrosine phosphatases (PTPs) catalyze the dephosphorylation of several pain-related substrates in spinal cord dorsal horn and are critically involved in the modification of pain transmission. The current study demonstrated that protein tyrosine phosphatase 1B (PTP1B), a unique endoplasmic reticulum-resident member of PTP family, displayed an activity-dependent increase in its protein expression and synaptic localization in spinal dorsal horn of adult male rats. PTP1B interacted with the Src Homology 3 (SH3) domain of Synapse-Associated Protein 102 (SAP102), one of the postsynaptic scaffolding proteins that anchored PTP1B at postsynaptic sites.
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