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Evidence for a cooperative role of gelatinase A and membrane type-1 matrix metalloproteinase during Xenopus laevis development.
Mech Dev 2007; 124(1):11-22MD

Abstract

Matrix metalloproteinases (MMPs) are a large family of extracellular or membrane-bound proteases. Their ability to cleave extracellular matrix (ECM) proteins has implicated a role in ECM remodeling to affect cell fate and behavior during development and in pathogenesis. We have shown previously that membrane-type 1 (MT1)-MMP [corrected] is coexpressed temporally and spatially with the MMP gelatinase A (GelA) in all cell types of the intestine and tail where GelA is expressed during Xenopus laevis metamorphosis, suggesting a cooperative role of these MMPs in development. Here, we show that Xenopus GelA and MT1-MMP interact with each other in vivo and that overexpression of MT1-MMP and GelA together in Xenopus embryos leads to the activation of pro-GelA. We further show that both MMPs are expressed during Xenopus embryogenesis, although MT1-MMP gene is expressed earlier than the GelA gene. To investigate whether the embryonic MMPs play a role in development, we have studied whether precocious expression of these MMPs alters development. Our results show that overexpression of both MMPs causes developmental abnormalities and embryonic death by a mechanism that requires the catalytic activity of the MMPs. More importantly, we show that coexpression of wild type MT1-MMP and GelA leads to a cooperative effect on embryonic development and that this cooperative effect is abolished when the catalytic activity of either MMP is eliminated through a point mutation in the catalytic domain. Thus, our studies support a cooperative role of these MMPs in embryonic development, likely through the activation of pro-GelA by MT1-MMP.

Authors+Show Affiliations

Section on Molecular Morphogenesis, Laboratory of Gene Regulation and Development, National Institute of Child Health and Human Development, National Institutes of Health, Bldg. 18T, Rm. 106, Bethesda, MD 20892, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, N.I.H., Intramural

Language

eng

PubMed ID

17055228

Citation

Hasebe, Takashi, et al. "Evidence for a Cooperative Role of Gelatinase a and Membrane Type-1 Matrix Metalloproteinase During Xenopus Laevis Development." Mechanisms of Development, vol. 124, no. 1, 2007, pp. 11-22.
Hasebe T, Hartman R, Fu L, et al. Evidence for a cooperative role of gelatinase A and membrane type-1 matrix metalloproteinase during Xenopus laevis development. Mech Dev. 2007;124(1):11-22.
Hasebe, T., Hartman, R., Fu, L., Amano, T., & Shi, Y. B. (2007). Evidence for a cooperative role of gelatinase A and membrane type-1 matrix metalloproteinase during Xenopus laevis development. Mechanisms of Development, 124(1), pp. 11-22.
Hasebe T, et al. Evidence for a Cooperative Role of Gelatinase a and Membrane Type-1 Matrix Metalloproteinase During Xenopus Laevis Development. Mech Dev. 2007;124(1):11-22. PubMed PMID: 17055228.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Evidence for a cooperative role of gelatinase A and membrane type-1 matrix metalloproteinase during Xenopus laevis development. AU - Hasebe,Takashi, AU - Hartman,Rebecca, AU - Fu,Liezhen, AU - Amano,Tosikazu, AU - Shi,Yun-Bo, Y1 - 2006/09/10/ PY - 2006/06/23/received PY - 2006/08/10/revised PY - 2006/09/07/accepted PY - 2006/10/24/pubmed PY - 2007/2/28/medline PY - 2006/10/24/entrez SP - 11 EP - 22 JF - Mechanisms of development JO - Mech. Dev. VL - 124 IS - 1 N2 - Matrix metalloproteinases (MMPs) are a large family of extracellular or membrane-bound proteases. Their ability to cleave extracellular matrix (ECM) proteins has implicated a role in ECM remodeling to affect cell fate and behavior during development and in pathogenesis. We have shown previously that membrane-type 1 (MT1)-MMP [corrected] is coexpressed temporally and spatially with the MMP gelatinase A (GelA) in all cell types of the intestine and tail where GelA is expressed during Xenopus laevis metamorphosis, suggesting a cooperative role of these MMPs in development. Here, we show that Xenopus GelA and MT1-MMP interact with each other in vivo and that overexpression of MT1-MMP and GelA together in Xenopus embryos leads to the activation of pro-GelA. We further show that both MMPs are expressed during Xenopus embryogenesis, although MT1-MMP gene is expressed earlier than the GelA gene. To investigate whether the embryonic MMPs play a role in development, we have studied whether precocious expression of these MMPs alters development. Our results show that overexpression of both MMPs causes developmental abnormalities and embryonic death by a mechanism that requires the catalytic activity of the MMPs. More importantly, we show that coexpression of wild type MT1-MMP and GelA leads to a cooperative effect on embryonic development and that this cooperative effect is abolished when the catalytic activity of either MMP is eliminated through a point mutation in the catalytic domain. Thus, our studies support a cooperative role of these MMPs in embryonic development, likely through the activation of pro-GelA by MT1-MMP. SN - 0925-4773 UR - https://www.unboundmedicine.com/medline/citation/17055228/Evidence_for_a_cooperative_role_of_gelatinase_A_and_membrane_type_1_matrix_metalloproteinase_during_Xenopus_laevis_development_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0925-4773(06)00152-3 DB - PRIME DP - Unbound Medicine ER -