Molecular cloning, tissue distribution, and chromosomal localization of MMEL2, a gene coding for a novel human member of the neutral endopeptidase-24.11 family

被引:29
作者
Bonvouloir, N
Lemieux, N
Crine, P
Boileau, G
DesGroseillers, L
机构
[1] Univ Montreal, Dept Biochem, Fac Med, Montreal, PQ H3T 1J4, Canada
[2] Univ Montreal, Fac Med, Dept Pathol & Cellular Biol, Montreal, PQ H3T 1J4, Canada
关键词
D O I
10.1089/104454901316976127
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
Members of the neutral endopeptidase (NEP, also known as MME for membrane metallo-endopeptidase in the Human Gene Nomenclature database) family play significant roles in pain perception, arterial pressure regulation, phosphate metabolism, and homeostasis. In this paper, we report the cloning of a new human member of the NEP family that we named MMEL2 for membrane metallo-endopeptidase-like 2. The MMEL2 protein has the structural characteristics of type Il transmembrane proteins, although the presence of a furin-like cleavage site in the ectodomain suggests that it may be released into the medium following proteolytic cleavage. The MMEL2 protein contains the zinc-binding consensus sequence HEXXH and all the residues known to be essential for the enzymatic activity of other members of the family. The MMEL2 mRNA was detected predominantly in testis, but weak expression also was observed in brain, kidney, and heart. The human MMEL2 gene was mapped to 1p36 by fluorescence in situ hybridization. It will be important to test whether MMEL2 defects are associated with diseases such as hereditary motor sensory neuropathy 2A, Schwartz-Jampel-Aberfeld syndrome, or neuroblastoma, which all map to this locus.
引用
收藏
页码:493 / 498
页数:6
相关论文
共 27 条
[1]  
BEAUMONT A, 1991, J BIOL CHEM, V266, P214
[2]  
BENOTHMANE K, 1993, GENOMICS, V17, P370
[3]  
CRINE P, 1997, CELL SURFACE PEPTIDA, P79
[4]   Localization of a human double-stranded RNA-binding protein gene (STAU) to band 20q13.1 by fluorescence in situ hybridization [J].
DesGroseillers, L ;
Lemieux, N .
GENOMICS, 1996, 36 (03) :527-529
[5]   KINETIC EVIDENCE THAT HIS-711 OF NEUTRAL ENDOPEPTIDASE 24.11 IS INVOLVED IN STABILIZATION OF THE TRANSITION-STATE [J].
DION, N ;
LEMOUAL, H ;
CRINE, P ;
BOILEAU, G .
FEBS LETTERS, 1993, 318 (03) :301-304
[6]   EVIDENCE THAT ASN(542) OF NEPRILYSIN (EC-3.4.24.11) IS INVOLVED IN BINDING OF THE P-2' RESIDUE OF SUBSTRATES AND INHIBITORS [J].
DION, N ;
LEMOUAL, H ;
FOURNIEZALUSKI, MC ;
ROQUES, BP ;
CRINE, P ;
BOILEAU, G .
BIOCHEMICAL JOURNAL, 1995, 311 :623-627
[7]   Molecular cloning and biochemical characterization of a new mouse testis soluble-zinc-metallopeptidase of the neprilysin family [J].
Ghaddar, G ;
Ruchon, AF ;
Carpentier, M ;
Marcinkiewicz, M ;
Seidah, NG ;
Crine, P ;
Desgroseillers, L ;
Boileau, G .
BIOCHEMICAL JOURNAL, 2000, 347 :419-429
[8]   STRUCTURE OF THERMOLYSIN REFINED AT 1.6-A RESOLUTION [J].
HOLMES, MA ;
MATTHEWS, BW .
JOURNAL OF MOLECULAR BIOLOGY, 1982, 160 (04) :623-639
[9]   FAMILIES OF ZINC METALLOPROTEASES [J].
HOOPER, NM .
FEBS LETTERS, 1994, 354 (01) :1-6
[10]   Molecular identification and characterization of novel membrane-bound metalloprotease, the soluble secreted form of which hydrolyzes a variety of vasoactive peptides [J].
Ikeda, K ;
Emoto, N ;
Raharjo, SB ;
Nurhantari, Y ;
Saiki, K ;
Yokoyama, M ;
Matsuo, M .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (45) :32469-32477