Plant matrix metalloproteinase
Plant matrix metalloproteinases are metalloproteins and zinc enzymes found in plants.
Matrix Metalloproteinase
catalytic domain.[1]
MMPs are synthesized primarily by
breast carcinomas. Based on the PUMP sequence and functionality of carcinomas in the progression of malignancy, a new branch of the MMP family could have been discovered.[2]
Extracellular Matrix
The most basic description of the plant
signaling pathways. In mammalian animals, extracellular matrix metalloproteinases (MMPs) modify the ECM to play significant roles in biological processes. The important role of MMP function in the extracellular matrix modification and subsequent mammalian development and signaling suggests that further study on the structure and function of these extracellular metalloproteinases may reveal new aspects of ECM modification in plant development.[3]
Plant MMPs
All known MMPs have been studied in vertebrates; it is hypothesized that they are involved in remodeling connective tissue during development and
aspartate that is found in all of the other MMPs.[4]
Studies of plant MMPs
Protein inhibitors of
metalloproteinase inhibitors (MPIs) can prevent unwanted proteolysis by denaturing their target proteases through non-competitive inhibition at an allosteric site. Five novel Lupinus albus MPIs were found and constitute the first reported protein inhibitors of metalloproteinases in plants and the first reported plant peptide inhibitors against a matrixin proteinase.[5]
MtMMPL1, a
exopolysaccharides (EPSs) and lipopolysaccharides (LPSs) of various rhizobia led to the formation of enlarged infection threads (ITs) with thickened cell walls, which is often associated with plant defense reactions, and to the production of ineffective nodules in their plant host. Even though its precise role is classified as unknown, MTMMPL1 is noted as the first member of this biologically important protein family with a clear function in plant-microbe symbiotic associations.[6]
At2-MMP from
pistils, ovules, and receptacles. It was concluded that the At2-MMP has a physiological role in mature aging tissue and the possibility of being involved in plant senescence.[7]
The fungus
embryogenesis, it is still unclear as to the role they play in plants. To try to better understand MMPs’ role in plant tissue, the SMEP1 is cloned and analyzed using a polymerase chain reaction (PCR) and the rapid amplification of cDNA ends (RACE) reaction. It was found only to be present in mature leaves, which suggest that SEMP1 may play an important role in tissue modeling.[8]
References
- Notes
- ^ Cao, J. & Zucker, S. (n.d.). Introduction to the MMP and TIMP families (structures, substrates) and an overview of diseases where MMPs have been incriminated. Biology and chemistry of matrix metalloproteinases (MMPs). Retrieved from http://www.abcam.com/index.html?pageconfig=resource&rid=11034
- ^ Flinn, B. (2008). Review: Plant extracellular matrix metalloproteinases. Functional Plant Biology, 35, 1183-1193.
- ^ McGeehan, G., Burkhart, W., Anderegg, R., Becherer, J. D., Gillikin, J. W., & Graham, J. S. (1992). Sequencing and Characterization of the Soybean Leaf Metalloproteinase. Plant Physiol., 99, 1179-1183.
- ^ Carrilho, D., Duarte, I., Francisco, R., Ricardo, C., & Duque-Magalhaes, M. (2009). Discovery of Novel Plant Peptides as Strong Inhibitors of Metalloproteinases. Protein and Peptide Letters, 16, 543-551.
- ^ Combier, J., Vernie, T., Billy, F., Yahyaoui, F., Mathis, R., & Gamas, P. (2007). The MtMMPL1 Early Nodulin is a novel member of the matrix metalloproteinase family with a role in Medicago truncatula infection by Sinorhizobium meliloti. Plan Physiology, 144, 703-716.
- ^ Golldack, D., Popova, O., & Dietz, K. (2002). Mutation of the Matrix Metalloproteinase At2-MMP Inhibits Growth and Causes Late Flowering and Early Senescence in Arabidopsis. The Journal of Biological Chemistry, 277 (7) 5541-5547.
- ^ . Graham, J. S., Xiong, J., & Gillikin, J. W. (1991). Purification and Developmental Analysis of a Metalloendoproteinase from the Leaves of Glycine max. Plant Physiol., 97, 786-792
- Bibliography
- Cao, J. & Zucker, S. (n.d.). Introduction to the MMP and TIMP families (structures, substrates) and an overview of diseases where MMPs have been incriminated. Biology and chemistry of matrix metalloproteinases (MMPs). Retrieved from http://www.abcam.com/index.html?pageconfig=resource&rid=11034
- Murphy, G., Murphy, G., & Reynolds, J. (1991). The origin of matrix metalloproteinases and their familial relationships. Federation of European Biochemical Societies, 289 (1), 4-7.
- Flinn, B. (2008). Review: Plant extracellular matrix metalloproteinases. Functional Plant Biology, 35, 1183-1193.
- McGeehan, G., Burkhart, W., Anderegg, R., Becherer, J. D., Gillikin, J. W., & Graham, J. S. (1992). Sequencing and Characterization of the Soybean Leaf Metalloproteinase. Plant Physiol., 99, 1179-1183.
- Carrilho, D., Duarte, I., Francisco, R., Ricardo, C., & Duque-Magalhaes, M. (2009). Discovery of Novel Plant Peptides as Strong Inhibitors of Metalloproteinases. Protein and Peptide Letters, 16, 543-551.
- Combier, J., Vernie, T., Billy, F., Yahyaoui, F., Mathis, R., & Gamas, P. (2007). The MtMMPL1 Early Nodulin is a novel member of the matrix metalloproteinase family with a role in Medicago truncatula infection by Sinorhizobium meliloti. Plan Physiology, 144, 703-716.
- Golldack, D., Popova, O., & Dietz, K. (2002). Mutation of the Matrix Metalloproteinase At2-MMP Inhibits Growth and Causes Late Flowering and Early Senescence in Arabidopsis. The Journal of Biological Chemistry, 277 (7) 5541-5547.
- Graham, J. S., Xiong, J., & Gillikin, J. W. (1991). Purification and developmental Analysis of a Metalloendoproteinase from the Leaves of Glycine max. Plant Physiol., 97, 786-792.
- Ao, C., Li, A., Elzaawely, A., & Tawata, S. (2008). MMP-13 Inhibitory Activity of Thirteen Selected Plant Species from Okinawa. International Journal of Pharmacology, 4 (3), 202-207.