Quantitative differences in matrix metalloproteinase (MMP)-2, but not in MMP-9, tissue inhibitor of metalloproteinase (TIMP)-1 of TIMP-2, in seminal plasma of normozoospermic and azoospermic patients

被引:40
作者
Baumgart, E [1 ]
Lenk, SV [1 ]
Loening, SA [1 ]
Jung, K [1 ]
机构
[1] Humboldt Univ, Univ Hosp Charite, Dept Urol, D-10117 Berlin, Germany
关键词
male fertility; MMP; seminal plasma; TIMP; zymography;
D O I
10.1093/humrep/17.11.2919
中图分类号
R71 [妇产科学];
学科分类号
100211 ;
摘要
BACKGROUND: Matrix metalloproteinases (MMPs) and their inhibitors, tissue inhibitors of metalloproteinases (TIMPs), have been detected in reproductive tissues and seminal plasma. The purpose of this study was to quantify MMP-2, MMP-9, TIMP-1 and TIMP-2 in human seminal plasma and to evaluate their association with sperm. METHODS: Seminal plasma was analysed using ELISA assays for all four analytes in 12 normozoospermic and 12 azoospermic patients and then for MMP-2 only in another 114 men with azoospermia (n = 16), after vasectomy (n = 20) and with sperm counts within the following ranges: 0.3-19 X 10(6)/ml (n = 20), 20-23 X 10(6)/ml (n = 11), 49-57 X 10(6)/ml (n = 12), 96-110 X 10(6)/ml (n = 12), 139-161 X 10(6)/ml (n = 12) and 215-346 X 10(6)/ml (n = 11). Additional zymographic analyses using SDS-PAGE were performed. RESULTS: All investigated MMPs and TIMPs were detected. MMP-9, TIMP-1 and TIMP-2 were not significantly different in normozoospermia and azoospermia. Only the MMP-2 concentration was significantly decreased in azoospermic compared with normozoospermic patients (mean +/- SD: 650.6 +/- 288.9 versus 1677 +/- 910.4 ng/ml respectively; P = 0.0002) and significantly correlated with the number of sperm (r = 0.54; P < 0.0001). CONCLUSION: MMP-2 in seminal plasma was strongly correlated to the sperm count in a linear fashion. Its origin and potential function remain to be elucidated.
引用
收藏
页码:2919 / 2923
页数:5
相关论文
共 24 条
[1]   PROTEOLYTIC REMODELING OF EXTRACELLULAR-MATRIX [J].
BIRKEDALHANSEN, H .
CURRENT OPINION IN CELL BIOLOGY, 1995, 7 (05) :728-735
[2]   Changing views of the role of matrix metalloproteinases in metastasis [J].
Chambers, AF ;
Matrisian, LM .
JOURNAL OF THE NATIONAL CANCER INSTITUTE, 1997, 89 (17) :1260-1270
[3]   HUMAN PROGELATINASE-A CAN BE ACTIVATED BY AUTOLYSIS AT A RATE THAT IS CONCENTRATION-DEPENDENT AND ENHANCED BY HEPARIN BOUND TO THE C-TERMINAL DOMAIN [J].
CRABBE, T ;
IOANNOU, C ;
DOCHERTY, AJP .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1993, 218 (02) :431-438
[4]   CHARACTERIZATION OF THE FUNCTIONAL DOMAIN OF TISSUE INHIBITOR OF METALLOPROTEINASES-2 (TIMP-2) [J].
DECLERCK, YA ;
YEAN, TD ;
LEE, Y ;
TOMICH, JM ;
LANGLEY, KE .
BIOCHEMICAL JOURNAL, 1993, 289 :65-69
[5]   HUMAN 72-KILODALTON TYPE-IV COLLAGENASE FORMS A COMPLEX WITH A TISSUE INHIBITOR OF METALLOPROTEASES DESIGNATED TIMP-2 [J].
GOLDBERG, GI ;
MARMER, BL ;
GRANT, GA ;
EISEN, AZ ;
WILHELM, S ;
HE, CS .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1989, 86 (21) :8207-8211
[6]   Matrix metalloproteinases as mediators of reproductive function [J].
Hulboy, DL ;
Rudolph, LA ;
Matrisian, LM .
MOLECULAR HUMAN REPRODUCTION, 1997, 3 (01) :27-45
[7]  
LOKESHWAR BL, 1993, CANCER RES, V53, P4493
[8]  
McCauley TC, 2001, MOL REPROD DEV, V58, P336, DOI 10.1002/1098-2795(200103)58:3&lt
[9]  
336::AID-MRD12&gt
[10]  
3.0.CO