Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0262471 (ENT)
 5,307 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Expression of intercellular adhesion molecule-1 (ICAM-1) on targets has been reported to be a relevant factor for leukocyte migration, adhesion and function. Because stimulated chondrocytes have been shown to express molecules of immunological import (like HLA class II antigens) and because rejected or resorbed cartilage grafts used in the field of ENT are often characterized by adjacent infiltrating leukocytes, the presence of ICAM-1 on human nasal, auricular and costal cartilage was investigated. For this study, cartilage tissue sections and chondrocytes in suspension as well as cultured chondrocytes were prepared. Specific monoclonal antibodies (mAb) were used for immunocyto- and immunohistochemical Alkaline-Phosphatase-anti-Alkaline-Phosphatase staining (APAAP staining) as well as for flow cytometry analysis. ICAM-1 on healthy cartilage tissue sections was not found. On the other hand, both chondrocytes freed from matrix and cultured chondrocytes showed strongly positive staining patterns for ICAM-1. This result was obtained for chondrocytes from nasal, auricular as well as costal cartilage. This observed expression of ICAM-1 on chondrocytes with defective extracellular matrix demonstrates that cartilage cells are able to synthesize ICAM-1 without any paracrine stimulus from non-chondrocyte cells. It suggests that ICAM-1 plays a role in processes where tissue damage leads to the exposure of chondrocyte surfaces. Therefore, ICAM-1 expression on chondrocytes may also be a factor in destructive cartilage graft resorption.
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PMID:Expression of ICAM-1 on isolated human nasal, auricular and costal chondrocytes. 751 Apr 48

Nicotinamide adenine dinucleotide (NAD(+)) is an essential cofactor involved in various cellular biochemical reactions. To date the signaling pathways that regulate NAD(+) metabolism remain unclear due to the dynamic nature and complexity of the NAD(+) metabolic pathways and the difficulty of determining the levels of the interconvertible pyridine nucleotides. Nicotinamide riboside (NmR) is a key pyridine metabolite that is excreted and re-assimilated by yeast and plays important roles in the maintenance of NAD(+) pool. In this study we establish a NmR-specific reporter system and use it to identify yeast mutants with altered NmR/NAD(+) metabolism. We show that the phosphate-responsive signaling (PHO) pathway contributes to control NAD(+) metabolism. Yeast strains with activated PHO pathway show increases in both the release rate and internal concentration of NmR. We further identify Pho8, a PHO-regulated vacuolar phosphatase, as a potential NmR production factor. We also demonstrate that Fun26, a homolog of human ENT (equilibrative nucleoside transporter), localizes to the vacuolar membrane and establishes the size of the vacuolar and cytosolic NmR pools. In addition, the PHO pathway responds to depletion of cellular nicotinic acid mononucleotide (NaMN) and mediates nicotinamide mononucleotide (NMN) catabolism, thereby contributing to both NmR salvage and phosphate acquisition. Therefore, NaMN is a putative molecular link connecting the PHO signaling and NAD(+) metabolic pathways. Our findings may contribute to the understanding of the molecular basis and regulation of NAD(+) metabolism in higher eukaryotes.
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PMID:Phosphate-responsive signaling pathway is a novel component of NAD+ metabolism in Saccharomyces cerevisiae. 2157 49