|
|
||||||||
a Center for Research on Reproduction and Women's Health, Departments of Obstetrics and Gynecology and
b Pathology and Laboratory Medicine, University of Pennsylvania Medical Center, Philadelphia, Pennsylvania 19104
c Division of Nephrology, Department of Medicine, Beth Israel Hospital and Harvard Medical School, Boston, Massachusetts 02215
d Department of Population Health and Reproduction, University of California, Davis, California 95616
e Department of Biochemistry and Molecular Biology, Albany Medical College, Albany, New York 12208
f Department of Biochemistry, University of Pennsylvania School of Dental Medicine, Philadelphia, Pennsylvania 19104
The membranes surrounding the chick embryo undergo striking morphological changes before hatching, which include structural degradation of the allantoic membrane. The fibrillar collagen content of the membranes declined by embryonic day (ED) 20 (the day of hatching). By ED 19, a 55-kDa matrix metalloproteinase (MMP) activity appeared in the extraembryonic fluid, and by ED 20 there was substantial 55-kDa MMP activity in embryonic membrane extracts. Reverse transcription-polymerase chain reaction was employed to clone a partial cDNA representing the chicken homologue of MMP-13, a 55- to 57-kDa enzyme. MMP-13 mRNA dramatically increased in abundance in embryonic membranes by ED 19, reaching a peak on ED 20. Introduction of the MMP inhibitor batimastat into the extraembryonic fluid prevented the structural changes in the embryonic membranes before hatching. We conclude that, like mammalian fetal membranes, chick embryonic membranes undergo terminal remodeling before hatching, in part as a result of increased MMP activity. The chicken egg system represents a novel in vivo model for exploring biochemical events leading to embryonic membrane remodeling prior to birth and to test inhibitors of MMPs for their ability to prevent collagenolysis and fetal membrane rupture.
2 Correspondence: Jerome F. Strauss, III, 778 Clinical Research Building, 415 Curie Boulevard, Philadelphia, PA 19104. FAX: 215 573-5408; jfs3{at}mail.med.upenn.edu
This article has been cited by other articles:
![]() |
A. Zijlstra, R. T. Aimes, D. Zhu, K. Regazzoni, T. Kupriyanova, M. Seandel, E. I. Deryugina, and J. P. Quigley Collagenolysis-dependent Angiogenesis Mediated by Matrix Metalloproteinase-13 (Collagenase-3) J. Biol. Chem., June 25, 2004; 279(26): 27633 - 27645. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Seandel, K. Noack-Kunnmann, D. Zhu, R. T. Aimes, and J. P. Quigley Growth factor-induced angiogenesis in vivo requires specific cleavage of fibrillar type I collagen Blood, April 15, 2001; 97(8): 2323 - 2332. [Abstract] [Full Text] [PDF] |
||||
![]() |
H. Enomoto, M. Enomoto-Iwamoto, M. Iwamoto, S. Nomura, M. Himeno, Y. Kitamura, T. Kishimoto, and T. Komori Cbfa1 Is a Positive Regulatory Factor in Chondrocyte Maturation J. Biol. Chem., March 17, 2000; 275(12): 8695 - 8702. [Abstract] [Full Text] [PDF] |
||||
![]() |
E. A. Hahn-Dantona, R. T. Aimes, and J. P. Quigley The Isolation, Characterization, and Molecular Cloning of a 75-kDa Gelatinase B-like Enzyme, a Member of the Matrix Metalloproteinase (MMP) Family. AN AVIAN ENZYME THAT IS MMP-9-LIKE IN ITS CELL EXPRESSION PATTERN BUT DIVERGES FROM MAMMALIAN GELATINASE B IN SEQUENCE AND BIOCHEMICAL PROPERTIES J. Biol. Chem., December 22, 2000; 275(52): 40827 - 40838. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |