Effects of uridine administration on hippocampal matrix metalloproteinases and their endogenous inhibitors in REM sleep-deprived rats. 2022

Aysen Cakir, and Busra Ocalan Esmerce, and Birnur Aydin, and Cansu Koc, and Mehmet Cansev, and Guldal Gulec Suyen, and Nevzat Kahveci
Bursa Uludag University School of Medicine, Department of Physiology, Bursa, Turkey. Electronic address: aysencakir@uludag.edu.tr.

Rapid eye movement (REM) sleep is associated with synaptic plasticity which is considered essential for long-term potentiation (LTP). The composition of extracellular matrix (ECM), in part, plays a role in REM sleep-associated synaptic functioning. The objective of this study was to investigate the effects of uridine administration on levels of matrix metalloproteinases (MMPs) and their endogenous inhibitors (TIMPs) in rats subjected to REM sleep deprivation (REMSD). REMSD was induced by modified multiple platform method for 96-hour. Rats were randomized to receive either saline or uridine (1 mmol/kg) intraperitoneally twice a day for four days. Rats were then decapitated and their hippocampi were dissected for analyzing the levels of MMP-2, MMP-3, MMP-9, TIMP-1, TIMP-2 and TIMP-3 by Western-blotting and the activities of MMP-2 and MMP-9 by Gelatin zymography. REMSD resulted in reduced levels of MMP-3, MMP-9, TIMP-3 and activity of MMP-9 in saline-treated rats, while uridine treatment significantly enhanced their impairment. TIMP-1 was enhanced following REMSD but uridine treatment had no significant effect on TIMP-1 levels. MMP-2, TIMP-2 levels and MMP-2 activity were not affected by either REMSD or uridine administration. These data show that REMSD significantly affects ECM composition which is ameliorated by uridine administration suggesting a possible use of uridine in sleep disorders.

UI MeSH Term Description Entries
D006624 Hippocampus A curved elevation of GRAY MATTER extending the entire length of the floor of the TEMPORAL HORN of the LATERAL VENTRICLE (see also TEMPORAL LOBE). The hippocampus proper, subiculum, and DENTATE GYRUS constitute the hippocampal formation. Sometimes authors include the ENTORHINAL CORTEX in the hippocampal formation. Ammon Horn,Cornu Ammonis,Hippocampal Formation,Subiculum,Ammon's Horn,Hippocampus Proper,Ammons Horn,Formation, Hippocampal,Formations, Hippocampal,Hippocampal Formations,Hippocampus Propers,Horn, Ammon,Horn, Ammon's,Proper, Hippocampus,Propers, Hippocampus,Subiculums
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012895 Sleep, REM A stage of sleep characterized by rapid movements of the eye and low voltage fast pattern EEG. It is usually associated with dreaming. Fast-Wave Sleep,Paradoxical Sleep,Rapid Eye Movements,Rhombencephalic Sleep,Sleep, Fast-Wave,REM Sleep,Eye Movement, Rapid,Eye Movements, Rapid,Fast Wave Sleep,Movement, Rapid Eye,Movements, Rapid Eye,Rapid Eye Movement,Sleep, Fast Wave,Sleep, Paradoxical,Sleep, Rhombencephalic
D014529 Uridine A ribonucleoside in which RIBOSE is linked to URACIL. Allo-Uridine,Allouridine,Allo Uridine
D051381 Rats The common name for the genus Rattus. Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus
D019278 Matrix Metalloproteinase 3 An extracellular endopeptidase of vertebrate tissues similar to MATRIX METALLOPROTEINASE 1. It digests PROTEOGLYCAN; FIBRONECTIN; COLLAGEN types III, IV, V, and IX, and activates procollagenase. (Enzyme Nomenclature, 1992) Stromelysin 1,Transin,MMP-3 Metalloproteinase,MMP3 Metalloproteinase,Stromelysin,MMP 3 Metalloproteinase,Metalloproteinase 3, Matrix,Metalloproteinase, MMP-3,Metalloproteinase, MMP3
D019715 Tissue Inhibitor of Metalloproteinase-1 A member of the family of TISSUE INHIBITOR OF METALLOPROTEINASES. It is a N-glycosylated protein, molecular weight 28 kD, produced by a vast range of cell types and found in a variety of tissues and body fluids. It has been shown to suppress metastasis and inhibit tumor invasion in vitro. TIMP-1,Metalloproteinase-1 Tissue Inhibitor,Tissue Inhibitor of Metalloproteinase 1
D019716 Tissue Inhibitor of Metalloproteinase-2 A member of the family of TISSUE INHIBITOR OF METALLOPROTEINASES. It is a 21-kDa nonglycosylated protein found in tissue fluid and is secreted as a complex with progelatinase A by human fibroblast and uncomplexed from alveolar macrophages. An overexpression of TIMP-2 has been shown to inhibit invasive and metastatic activity of tumor cells and decrease tumor growth in vivo. TIMP-2,Metalloproteinase-2 Tissue Inhibitor,Tissue Inhibitor of Metalloproteinase 2
D019717 Tissue Inhibitor of Metalloproteinase-3 A member of the family of tissue inhibitor of metalloproteinases. Mutations of the gene for TIMP3 PROTEIN causes Sorsby fundus dystrophy. TIMP-3,TIMP-3 Protein,TIMP3 Protein,Metalloproteinase-3 Tissue Inhibitor,TIMP 3 Protein,Tissue Inhibitor of Metalloproteinase 3
D020778 Matrix Metalloproteinase 2 A secreted endopeptidase homologous with INTERSTITIAL COLLAGENASE, but which possesses an additional fibronectin-like domain. Gelatinase A,72-kDa Gelatinase,72-kDa Type IV Collagenase,MMP-2 Metalloproteinase,MMP2 Metalloproteinase,Matrix Metalloproteinase-2,72 kDa Gelatinase,72 kDa Type IV Collagenase,Gelatinase, 72-kDa,MMP 2 Metalloproteinase,Metalloproteinase 2, Matrix,Metalloproteinase, MMP-2,Metalloproteinase, MMP2

Related Publications

Aysen Cakir, and Busra Ocalan Esmerce, and Birnur Aydin, and Cansu Koc, and Mehmet Cansev, and Guldal Gulec Suyen, and Nevzat Kahveci
April 1979, Life sciences,
Aysen Cakir, and Busra Ocalan Esmerce, and Birnur Aydin, and Cansu Koc, and Mehmet Cansev, and Guldal Gulec Suyen, and Nevzat Kahveci
June 2011, Naunyn-Schmiedeberg's archives of pharmacology,
Aysen Cakir, and Busra Ocalan Esmerce, and Birnur Aydin, and Cansu Koc, and Mehmet Cansev, and Guldal Gulec Suyen, and Nevzat Kahveci
March 2024, Physiology international,
Aysen Cakir, and Busra Ocalan Esmerce, and Birnur Aydin, and Cansu Koc, and Mehmet Cansev, and Guldal Gulec Suyen, and Nevzat Kahveci
January 2001, Methods in molecular medicine,
Aysen Cakir, and Busra Ocalan Esmerce, and Birnur Aydin, and Cansu Koc, and Mehmet Cansev, and Guldal Gulec Suyen, and Nevzat Kahveci
October 1995, Acta orthopaedica Scandinavica. Supplementum,
Aysen Cakir, and Busra Ocalan Esmerce, and Birnur Aydin, and Cansu Koc, and Mehmet Cansev, and Guldal Gulec Suyen, and Nevzat Kahveci
January 1999, Anticancer research,
Aysen Cakir, and Busra Ocalan Esmerce, and Birnur Aydin, and Cansu Koc, and Mehmet Cansev, and Guldal Gulec Suyen, and Nevzat Kahveci
January 2012, International journal of impotence research,
Aysen Cakir, and Busra Ocalan Esmerce, and Birnur Aydin, and Cansu Koc, and Mehmet Cansev, and Guldal Gulec Suyen, and Nevzat Kahveci
March 1982, Brain research bulletin,
Aysen Cakir, and Busra Ocalan Esmerce, and Birnur Aydin, and Cansu Koc, and Mehmet Cansev, and Guldal Gulec Suyen, and Nevzat Kahveci
June 2004, FEBS letters,
Aysen Cakir, and Busra Ocalan Esmerce, and Birnur Aydin, and Cansu Koc, and Mehmet Cansev, and Guldal Gulec Suyen, and Nevzat Kahveci
December 1969, Journal of psychiatric research,
Copied contents to your clipboard!