Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0028754 (obesity)
 124,988 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Investigation of lysosomal hydrolase activity in platelets of patients has revealed drastic activation of cathepsins B, C and phospholipase A1, the degree of which rose in the following range: coronary heart disease; coronary heart disease aggravated by obesity: obesity and hyperlipidemia (type II). Administration of the adequate dietotherapy resulted in normalization of enzymologic parameters, whereas the results of the clinico-biochemical analysis of the blood were less informative in all cases. The data obtained could be used in the evaluation of the dietotherapy effectiveness, as well as for the early diagnosis of the corresponding diseases.
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PMID:[Thrombocyte lysosomal hydrolase activity in patients with ischemic heart disease, hyperlipidemia and obesity against a background of different diets]. 343 81

The activity of cathepsins A, B, C, D, phospholipases A1 and A2, and aryl sulphatases A and B was studied in hepatic lysosomas, adipocytes of epididymal fatty tissue and in platelets of rats aged 2,5 and 24 months differing in the character of milk feeding. It was found that excessive feeding in the neonatal period resulted in a decrease of the lysosomal proteinase activity by 18-33% in 24-month animals, while phospholipase A2 activity rose 1,4-2.2-fold. Phospholipase A2 activity proved to be also increased in adipocytes of obese rats. Obese rats' platelets were characterized by a drastic (2-3.5-fold) activation of cathepsin C, and phospholipase A1 activity rose by 55% at all the stages of the ontogenesis. It is suggested that the changes in the lysosomal hydrolases activity may reflect the platelet function in the disordered lipoprotein metabolism.
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PMID:[Effect of neonatal nutrition on the enzyme activity of liver lysosomes, adipocytes and thrombocytes in young and old rats]. 370 43

Lysophosphatidic acid (LPA, 1- or 2-acyl-sn-glycerol 3-phosphate) is a simple phospholipid but displays an intriguing cell biology that is mediated via interactions with G protein-coupled seven transmembrane receptors (GPCRs). So far, five GPCRs, designated LPA1-5, and, more recently, two additional GPCRs, GPR87 and P2Y5, have been identified as receptors for LPA. These LPA receptors can be classified into two families, the EDG and P2Y families, depending on their primary structures. Recent studies on gene targeting mice and family diseases of these receptors revealed that LPA is involved in both pathological and physiological states including brain development (LPA1), neuropathy pain (LPA1), lung fibrosis (LPA1), renal fibrosis (LPA1) protection against radiation-induced intestinal injury (LPA2), implantation (LPA3) and hair growth (P2Y5). LPA is produced both in cells and biological fluids, where multiple synthetic reactions occur. There are at least two pathways for LPA production. In serum or plasma, LPA is predominantly produced by a plasma enzyme called autotaxin (ATX). ATX is a multifunctional ectoenzyme and is involved in many patho-physiological conditions such as cancer, neuropathy pain, lymphocyte tracking in lymph nodes, obesity, diabetes and embryonic blood vessel formation. LPA is also produced from phosphatidic acid (PA) by its deacylation catalyzed by phospholipase A (PLA)-type enzymes. However, the physiological roles of this pathway as well as the enzymes involved remained to be solved. A number of phospholipase A1 and A2 isozymes could be involved in this pathway. One PA-selective PLA1 called mPA-PLA1alpha/LIPH is specifically expressed in hair follicles, where it has a critical role in hair growth by producing LPA through a novel LPA receptor called P2Y5.
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PMID:Two pathways for lysophosphatidic acid production. 1862 Nov 44