TISSUE DISTRIBUTION OF GLYCINE N-METHYLTRANSFERASE, A MAJOR FOLATE-BINDING PROTEIN OF LIVER

被引:113
作者
YEO, EJ
WAGNER, C
机构
[1] VANDERBILT UNIV,MED CTR,SCH MED,NASHVILLE,TN 37232
[2] DEPT VET AFFAIRS MED CTR,NASHVILLE,TN 37232
关键词
S-ADENOSYLMETHIONINE; METHYLATION; GLUCONEOGENESIS; EXOCRINE SECRETION; NUCLEUS;
D O I
10.1073/pnas.91.1.210
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Glycine N-methyltransferase (GNMT; S-adenosyl-L-methionine:glycine N-methyltransferase, EC 2.1.1.20) is a major protein in rat liver that binds 5-methyltetrahydrofolate polyglutamate in vivo. This enzyme is believed to function in the regulation of the availability of S-adenosylmethionine, the primary donor of methyl groups in the body. The distribution of GNMT in a variety of rat tissues was examined immunohistochemically. In liver, GNMT was most abundant in the periportal region, whereas in kidney it was seen primarily in the proximal convoluted tubules. In pancreas, GNMT was abundant, principally in the exocrine tissue. GNMT was present in the striated duct cells of the submaxillary gland. In the jejunum, GNMT was found in the epithelial cells of the villi. Close examination of the liver indicated GNMT in the nucleus; this site was confirmed by purification of the nuclei and measurement of enzyme activity. The location of GNMT in the liver and kidney suggests that this enzyme plays a role in gluconeogenesis, while its presence in the exocrine cells suggests it may also be a factor in secretion.
引用
收藏
页码:210 / 214
页数:5
相关论文
共 29 条
[1]  
CANTONI GL, 1978, TRANSMETHYLATION, P155
[2]   DISTRIBUTION AND CHEMICAL NATURE OF RADIOACTIVE FOLATES IN RAT-LIVER CELLS AND RAT-LIVER MITOCHONDRIA [J].
COOK, RJ ;
BLAIR, JA .
BIOCHEMICAL JOURNAL, 1979, 178 (03) :651-659
[3]   GLYCINE N-METHYLTRANSFERASE IS A FOLATE BINDING-PROTEIN OF RAT-LIVER CYTOSOL [J].
COOK, RJ ;
WAGNER, C .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1984, 81 (12) :3631-3634
[4]   CELL-SPECIFIC IMMUNOHISTOCHEMICAL LOCALIZATION OF A CELLULAR RETINOL-BINDING PROTEIN (TYPE-2) IN THE SMALL-INTESTINE OF RAT [J].
CROW, JA ;
ONG, DE .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1985, 82 (14) :4707-4711
[5]  
GUDER WG, 1974, HOPPESEYLERS Z PHYSL, V235, P273
[6]  
HARLOW E, 1988, ANTIBODIES LABORATOR
[7]  
HEADY JE, 1973, J BIOL CHEM, V248, P69
[8]   USE OF AVIDIN-BIOTIN-PEROXIDASE COMPLEX (ABC) IN IMMUNOPEROXIDASE TECHNIQUES - A COMPARISON BETWEEN ABC AND UNLABELED ANTIBODY (PAP) PROCEDURES [J].
HSU, SM ;
RAINE, L ;
FANGER, H .
JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY, 1981, 29 (04) :577-580
[9]   PROTEIN PRENYLCYSTEINE ANALOG INHIBITS AGONIST RECEPTOR-MEDIATED SIGNAL TRANSDUCTION IN HUMAN PLATELETS [J].
HUZOORAKBAR ;
WANG, WJ ;
KORNHAUSER, R ;
VOLKER, C ;
STOCK, JB .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (03) :868-872
[10]   REGULATION OF THE ACTIVITY OF HEPATIC PHENYLALANINE-HYDROXYLASE [J].
KAUFMAN, S .
ADVANCES IN ENZYME REGULATION, 1986, 25 :37-64