Pancreatic lipase-related protein 1 (PLRP1) is present in the pancreatic juice of several species

被引:45
作者
De Caro, J
Carrière, F
Barboni, P
Giller, T
Verger, R
De Caro, A
机构
[1] CNRS, UPR 9025, IFRC 1, Lipolyse Enzymat Lab, F-13402 Marseille 20, France
[2] F Hoffmann La Roche & Co Ltd, CH-4002 Basel, Switzerland
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1998年 / 1387卷 / 1-2期
关键词
pancreatic juice; pancreatic lipase-related protein; baculovirus expression system; (man); (dog); (pig); (rat);
D O I
10.1016/S0167-4838(98)00143-5
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
Pancreatic lipase-related protein 1 (PLRP1) was purified from human, canine, porcine and rat pancreatic juices. The four PLRPls were identified using microsequencing methods after performing gel filtration on Ultrogel AcA-54 followed by chromatography on Heparin-Sepharose cation-exchanger. Polyclonal antibodies specific to human PLRP1 (HPLRP1) were raised in the rabbit using a synthetic decapeptide from HPLRP1. The results of Western blotting analysis showed that these antibodies recognized native HPLRP1 and recombinant HPLRP1 produced by insect cells, and cross-reacted only with rat PLRP1 (RPLRP1). No significant lipolytic activity was observed with native canine PLRP1 and recombinant HPLRP1 on various glycerides, phospholipid and vitamin esters, or on cholesterol esters. It was established for the first time that this protein is secreted in variable amounts by the adult exocrine pancreas of several species. (C) 1998 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:331 / 341
页数:11
相关论文
共 40 条
[1]   Pancreatic lipase-related protein 2 but not classical pancreatic Lipase hydrolyzes galactolipids [J].
Andersson, L ;
Carriere, F ;
Lowe, ME ;
Nilsson, A ;
Verger, R .
BIOCHIMICA ET BIOPHYSICA ACTA-LIPIDS AND LIPID METABOLISM, 1996, 1302 (03) :236-240
[2]  
[Anonymous], SILICON GRAPHICS GEO
[3]   An inactive pancreatic lipase-related protein is activated into a triglyceride-lipase by mutagenesis based on the 3-D structure [J].
Bezzine, S ;
Roussel, A ;
de Caro, J ;
Gastinel, L ;
de Caro, A ;
Carrière, F ;
Leydier, S ;
Verger, R ;
Cambillau, C .
CHEMISTRY AND PHYSICS OF LIPIDS, 1998, 93 (1-2) :103-114
[4]   CELL-SPECIFIC ENHANCERS IN THE RAT EXOCRINE PANCREAS [J].
BOULET, AM ;
ERWIN, CR ;
RUTTER, WJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1986, 83 (11) :3599-3603
[5]   STRUCTURE-FUNCTION-RELATIONSHIPS IN NATURALLY-OCCURRING MUTANTS OF PANCREATIC LIPASE [J].
CARRIERE, F ;
THIRSTRUP, K ;
BOEL, E ;
VERGER, R ;
THIM, L .
PROTEIN ENGINEERING, 1994, 7 (04) :563-569
[6]   Pancreatic lipase structure-function relationships by domain exchange [J].
Carriere, F ;
Thirstrup, K ;
Hjorth, S ;
Ferrato, F ;
Nielsen, PF ;
WithersMartinez, C ;
Cambillau, C ;
Boel, E ;
Thim, L ;
Verger, R .
BIOCHEMISTRY, 1997, 36 (01) :239-248
[7]   INACTIVATION OF PANCREATIC LIPASES BY AMPHIPHILIC REAGENTS 5-(DODECYLDITHIO)-2-NITROBENZOIC ACID AND TETRAHYDROLIPSTATIN - DEPENDENCE UPON PARTITIONING BETWEEN MICELLAR AND OIL PHASES [J].
CUDREY, C ;
VANTILBEURGH, H ;
GARGOURI, Y ;
VERGER, R .
BIOCHEMISTRY, 1993, 32 (50) :13800-13808
[8]  
DATTA S, 1988, J BIOL CHEM, V263, P1107
[9]   ASSIGNMENT OF THE HUMAN PANCREATIC COLIPASE GENE TO CHROMOSOME-6P21.1 TO PTER [J].
DAVIS, RC ;
XIA, YR ;
MOHANDAS, T ;
SCHOTZ, MC ;
LUSIS, AJ .
GENOMICS, 1991, 10 (01) :262-265
[10]   PURIFICATION AND PROPERTIES OF PHOSPHOLIPASE A FROM PORCINE PANCREAS [J].
DEHAAS, GH ;
POSTEMA, NM ;
NIEUWENHUIZEN, W ;
VANDEENE.LL .
BIOCHIMICA ET BIOPHYSICA ACTA, 1968, 159 (01) :103-+