scholarly journals Structure and Function of Human Matrix Metalloproteinases

Cells ◽  
2020 ◽  
Vol 9 (5) ◽  
pp. 1076 ◽  
Author(s):  
Helena Laronha ◽  
Jorge Caldeira

The extracellular matrix (ECM) is a macromolecules network, in which the most abundant molecule is collagen. This protein in triple helical conformation is highly resistant to proteinases degradation, the only enzymes capable of degrading the collagen are matrix metalloproteinases (MMPs). This resistance and maintenance of collagen, and consequently of ECM, is involved in several biological processes and it must be strictly regulated by endogenous inhibitors (TIMPs). The deregulation of MMPs activity leads to development of numerous diseases. This review shows MMPs complexity.

2020 ◽  
Author(s):  
Reena Singh ◽  
Richard Tan ◽  
Clara Tran ◽  
Thomas Loudovaris ◽  
Helen E. Thomas ◽  
...  

2020 ◽  
Vol 27 (11) ◽  
pp. 1068-1081
Author(s):  
Xi Liu ◽  
Dongwu Liu ◽  
Yangyang Shen ◽  
Mujie Huang ◽  
Lili Gao ◽  
...  

Matrix Metalloproteinases (MMPs) belong to a family of metal-dependent endopeptidases which contain a series of conserved pro-peptide domains and catalytic domains. MMPs have been widely found in plants, animals, and microorganisms. MMPs are involved in regulating numerous physiological processes, pathological processes, and immune responses. In addition, MMPs play a key role in disease occurrence, including tumors, cardiovascular diseases, and other diseases. Compared with invertebrate MMPs, vertebrate MMPs have diverse subtypes and complex functions. Therefore, it is difficult to study the function of MMPs in vertebrates. However, it is relatively easy to study invertebrate MMPs because there are fewer subtypes of MMPs in invertebrates. In the present review, the structure and function of MMPs in invertebrates were summarized, which will provide a theoretical basis for investigating the regulatory mechanism of MMPs in invertebrates.


2001 ◽  
Vol 12 (5) ◽  
pp. 373-398 ◽  
Author(s):  
Bjorn Steffensen ◽  
Lari Häkkinen ◽  
Hannu Larjava

During wound-healing, cells are required to migrate rapidly into the wound site via a proteolytically generated pathway in the provisional matrix, to produce new extracellular matrix, and, subsequently, to remodel the newly formed tissue matrix during the maturation phase. Two classes of molecules cooperate closely to achieve this goal, namely, the matrix adhesion and signaling receptors, the integrins, and matrix-degrading and -processing enzymes, the matrix metalloproteinases (MMPs). There is now substantial experimental evidence that blocking key molecules of either group will prevent or seriously delay wound-healing. It has been known for some time now that cell adhesion by means of the integrins regulates the expression of MMPs. In addition, certain MMPs can bind to integrins or other receptors on the cell surface involved in enzyme activation, thereby providing a mechanism for localized matrix degradation. By proteolytically modifying the existing matrix molecules, the MMPs can then induce changes in cell behavior and function from a state of rest to migration. During wound repair, the expression of integrins and MMPs is simultaneously up-regulated. This review will focus on those aspects of the extensive knowledge of fibroblast and keratinocyte MMPs and integrins in biological processes that relate to wound-healing.


Oncotarget ◽  
2017 ◽  
Vol 8 (11) ◽  
pp. 17981-17994 ◽  
Author(s):  
Balaji Krishnamachary ◽  
Ioannis Stasinopoulos ◽  
Samata Kakkad ◽  
Marie-France Penet ◽  
Desmond Jacob ◽  
...  

2012 ◽  
Vol 180 (5) ◽  
pp. 1863-1878 ◽  
Author(s):  
Gerald C. Koenig ◽  
R. Grant Rowe ◽  
Sharlene M. Day ◽  
Farideh Sabeh ◽  
Jeffrey J. Atkinson ◽  
...  

2014 ◽  
Vol 2014 ◽  
pp. 1-15 ◽  
Author(s):  
Manoel Luís Costa

The function of muscle is to contract, which means to exert force on a substrate. The adaptations required for skeletal muscle differentiation, from a prototypic cell, involve specialization of housekeeping cytoskeletal contracting and supporting systems into crystalline arrays of proteins. Here I discuss the changes that all three cytoskeletal systems (microfilaments, intermediate filaments, and microtubules) undergo through myogenesis. I also discuss their interaction, through the membrane, to extracellular matrix and to other cells, where force will be exerted during contraction. The three cytoskeletal systems are necessary for the muscle cell and must exert complementary roles in the cell. Muscle is a responsive system, where structure and function are integrated: the structural adaptations it undergoes depend on force production. In this way, the muscle cytoskeleton is a portrait of its physiology. I review the cytoskeletal proteins and structures involved in muscle function and focus particularly on their role in myogenesis, the process by which this incredible muscle machine is made. Although the focus is on skeletal muscle, some of the discussion is applicable to cardiac and smooth muscle.


1991 ◽  
Vol 69 (3) ◽  
pp. 618-627 ◽  
Author(s):  
William R. Bates ◽  
Joan E. Mallett

Molgula pacifica embryos exhibit anural development in which embryogenesis proceeds directly to the development of a juvenile, without the development of a tailed larva. The purpose of this study was to investigate the key events that are responsible for the development of M. pacifica juveniles. The results of the present investigation indicate that the timing and spatial rearrangements of the egg cytoplasm that occur after fertilization (termed ooplasmic segregation) are similar in M. pacifica eggs as compared with those that occur in typical urodele species. These observations suggest that the mechanism that is responsible for the urodele pattern of ooplasmic segregation was conserved during the evolution of anural species. The cleavage patterns displayed by M. pacifica embryos up to the eight-cell stage were similar to those exhibited by urodele embryos. However, gastrulation in M. pacifica embryos differed from the typical urodele mode of gastrulation. The mode of gastrulation exhibited by M. pacifica embryos is likely a consequence of their eggs containing a greater quantity of yolk than the less yolky eggs of species more commonly studied. In the second part of this investigation, ampullar development, structure, and function were studied. Two conclusions were made from these studies. First, the extracellular matrix materials comprising the tunic are secreted by the epidermal ampullar cells. Second, a shift in the timing of ampullar rudiment development in M. pacifica embryos suggests the possibility of a heterochronic mechanism of evolutionary change within the epidermal cell lineage.


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