The complete amino acid sequence of human placental oxytocinase

被引：51

作者：

Laustsen, PG

Rasmussen, TE

Petersen, K

PedrazaDiaz, S

Moestrup, SK

Gliemann, J

SottrupJensen, L

Kristensen, T

机构：

[1] AARHUS UNIV,DEPT CHEM,DEPT BIOL MOL & STRUCT,DK-8000 AARHUS,DENMARK

[2] AARHUS UNIV,DEPT MED BIOCHEM,DK-8000 AARHUS,DENMARK

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 1997年 / 1352卷 / 01期

关键词：

zinc metallopeptidase; aminopeptidase; oxytocinase; placenta; heart; muscle;

D O I：

10.1016/S0167-4781(97)00036-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The complete amino acid sequence of human placental oxytocinase (placental leucine aminopeptidase) has been determined by cDNA cloning and sequencing. Oxytocinase is a type II integral membrane protein of 1025 amino acid residues, consisting of an acidic intracellular region of 110 amino acids followed by a hydrophobic transmembrane segment of 22 residues and 893 extracellular residues containing the characteristic Zn2+ coordination sequence element His-Glu-Xaa-Xaa-His-(18 residues)-Glu found in gluzincins. Two sets of cDNA clones with different 5'-ends were isolated and suggested to represent different spliced products of 3.6 kb (mature mRNA) and 12 kb, respectively. Oxytocinase mRNA is present in large amounts in placenta, heart and skeletal muscle and in small amounts in brain, kidney, liver and pancreas. A conserved sequence element, the GAMEN motif, which distinguishes the aminopeptidase family among gluzincins from other gluzincins, has been identified.

引用

页码：1 / 7

页数：7

共 30 条

[1] AHMAD S, 1990, J PHARMACOL EXP THER, V252, P643
[2] BOTBOL V, 1991, J BIOL CHEM, V266, P2151
[3] Chen HJ, 1996, J IMMUNOL, V157, P2593
[4] PUROMYCIN-SENSITIVE AMINOPEPTIDASE - SEQUENCE-ANALYSIS, EXPRESSION, AND FUNCTIONAL-CHARACTERIZATION
CONSTAM, DB
TOBLER, AR
RENSINGEHL, A
KEMLER, I
HERSH, LB
FONTANA, A
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (45) : 26931 - 26939
[5] DETERMINANTS ESSENTIAL FOR THE TRANSMISSIBLE GASTROENTERITIS VIRUS-RECEPTOR INTERACTION RESIDE WITHIN A DOMAIN OF AMINOPEPTIDASE-N THAT IS DISTINCT FROM THE ENZYMATIC SITE
DELMAS, B
GELFI, J
KUT, E
SJOSTROM, H
NOREN, O
LAUDE, H
[J]. JOURNAL OF VIROLOGY, 1994, 68 (08) : 5216 - 5224
[6] IDENTIFICATION, ISOLATION, AND CLONING OF A BACILLUS-THURINGIENSIS CRYIAC TOXIN-BINDING PROTEIN FROM THE MIDGUT OF THE LEPIDOPTERAN INSECT HELIOTHIS-VIRESCENS
GILL, SS
COWLES, EA
FRANCIS, V
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (45) : 27277 - 27282
[7] INHIBITION OF THERMOLYSIN AND NEUTRAL ENDOPEPTIDASE-24.11 BY A NOVEL GLUTARAMIDE DERIVATIVE - X-RAY STRUCTURE DETERMINATION OF THE THERMOLYSIN INHIBITOR COMPLEX
HOLLAND, DR
BARCLAY, PL
DANILEWICZ, JC
MATTHEWS, BW
JAMES, K
[J]. BIOCHEMISTRY, 1994, 33 (01) : 51 - 56
[8] FAMILIES OF ZINC METALLOPROTEASES
HOOPER, NM
[J]. FEBS LETTERS, 1994, 354 (01) : 1 - 6
[9] CLONING AND CHARACTERIZATION OF A NOVEL INSULIN-REGULATED MEMBRANE AMINOPEPTIDASE FROM GLUT4 VESICLES
KELLER, SR
SCOTT, HM
MASTICK, CC
AEBERSOLD, R
LIENHARD, GE
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (40) : 23612 - 23618
[10] MOLECULAR-CLONING OF AN INSECT AMINOPEPTIDASE-N THAT SERVES AS A RECEPTOR FOR BACILLUS-THURINGIENSIS CRYIA(C) TOXIN
KNIGHT, PJK
KNOWLES, BH
ELLAR, DJ
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (30) : 17765 - 17770

← 1 2 3 →