An introduction to matrikines: extracellular matrix-derived peptides which regulate cell activity (original) (raw)
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Advances in experimental medicine and biology, 2014
Collagens are the most abundant components of the extracellular matrix and many types of soft tissues. Elastin is another major component of certain soft tissues, such as arterial walls and ligaments. Many other molecules, though lower in quantity, function as essential components of the extracellular matrix in soft tissues. Some of these are reviewed in this chapter. Besides their basic structure, biochemistry and physiology, their roles in disorders of soft tissues are discussed only briefly as most chapters in this volume deal with relevant individual compounds. Fibronectin with its muldomain structure plays a role of "master organizer" in matrix assembly as it forms a bridge between cell surface receptors, e.g., integrins, and compounds such collagen, proteoglycans and other focal adhesion molecules. It also plays an essential role in the assembly of fibrillin-1 into a structured network. Laminins contribute to the structure of the extracellular matrix (ECM) and modula...
Duca et al (2004) Elastin as a matrikine
The fact that elastin peptides, the degradation products of the extracellular matrix protein elastin, are chemotactic for numerous cell types, promote cell cycle progression and induce release of proteolytic enzymes by stromal and cancer cells, strongly suggests that their presence in tissues could contribute to tumour progression. Thus, elastin peptides qualify as matrikines, i.e. peptides originating from the fragmentation of matrix proteins and presenting biological activities. After a brief description of their origin, the biological activities of these peptides are reviewed, emphasising their potential role in cancer. The nature of their receptor and the signalling events it controls are also discussed. Finally, the structural selectivity of the elastin complex receptor is presented, leading to the concept of elastokine (matrikine originating from elastin fragmentation) and morpho-elastokine, i.e. peptides presenting a conformation similar to that of bioactive elastin peptides and mimicking their effects.
Control of Tumor Progression by Extracellular Matrix Molecule Fragments, the Matrikines
Journal of Carcinogenesis & Mutagenesis, 2013
Tumor microenvironment is a complex system composed of a largely altered Extracellular Matrix (ECM) with different cell types that determine tumor progression. Upon the influence of hypoxia, tumor cells secrete cytokines that activate stromal cells to produce proteases and angiogenic factors. The proteases degrade the stromal ECM and participate in the release of various ECM fragments, named matrikines or matricryptins, capable to control tumor invasion and metastasis dissemination. The putative targets of the matrikine action are the proliferation and invasive properties of tumor or inflammatory cells, and the angiogenic and lymphangiogenic responses. In the present review, we will describe pro-tumorigenic effects triggered by soluble elastin or Elastin-Derived Peptides (EDPs), as well as the anti-tumorigenic or anti-angiogenic activities the matrikines derived from basement membrane associated collagens and several proteoglycans such as perlecan or lumican. Matrikines constitute a new family of potent anticancer agents that could be used under various therapeutic strategies: i) induction of their overexpression by cancer cells or by the host, ii) use of recombinant proteins or synthetic peptides or structural analogs designed from the structure of the active sequences. Matrikines could be used in combination with conventional chemotherapy or radiotherapy to limit tumor progression.
Structure and biological activity of the extracellular matrix
Journal of Molecular Medicine, 1998
The extracellular matrix is formed by complex and intricate networks within which molecules are precisely organized. These molecular networks determine the specific histoarchitecture of tissues and provide cells with information and a scaffold. Most of the structural extracellular matrix molecules -collagens, noncollage-nous glycoproteins, and proteoglycans -are chimeric and share common domains. Studies of the interactions between extracellular matrix molecules and mapping of the interaction sites to defined structural modules have led to the concept that the function of the extracellular matrix relies largely in the polymers that they form. Furthermore, determination of the tertiary structure of protein motifs involved either in the assembly of the various molecules into polymers or in cell-extracellular matrix interactions has recently opened the field of structural biology of the extracellular matrix.
Trends in extracellular matrix biology
Molecular Biology Reports, 2022
y cell communication that guides cellular behavior in normal homeostasis and disease conditions [1, 2]. The multitasking ECM is formed by hundreds of different building blocks, interacting macromolecules and bioactive modulators that upon cell-matrix communication affect cell phenotype and functions [3]. The core of ECM network is consisted of structural and functional macromolecules, such as proteoglycans and glycosaminoglycans (PGs/GAGs), collagens, elastin, laminins, tenascins, nidogens as well as cell surface receptors and co-receptors, including integrins and hyaluronan (HA) receptor, CD44. Matrix remodeling is finely tuned by the enzymatic actions of matrix-degrading enzymes, as proteases, including matrix metalloproteinases (MMPs), adamalysins and glycosidases, such as heparanase and hyaluronidases (Fig. 1) [4, 5]. The content and structural features of matrix components segregate ECMs into interstitial and pericellular ones, the latter being the basement membrane (ΒΜ). Interstitial matrices mainly consist of fibrillar collagens, fibronectin, PGs and matricellular proteins. The main ECM components of the ΒΜ consist of collagen IV, laminins, nidogens, and ECMs: dynamic regulatory networks in tissue remodeling and integrity Human tissues are mainly constituted of cells including fibroblasts, immune, endothelial, and epithelial cells, and various types of non-cellular ECM networks. The composition of ECMs differs between tissues, developmental stages, and pathophysiological conditions. ECM macromolecular networks orchestrate cellular properties through signaling cascades, exhibiting paramount importance in
A guide to the composition and functions of the extracellular matrix
The FEBS Journal, 2021
Extracellular matrix (ECM) is a dynamic 3-dimensional network of macromolecules that provides structural support for the cells and tissues. Accumulated knowledge clearly demonstrated over the last decade that ECM plays key regulatory roles since it orchestrates cell signaling, functions, properties and morphology. Extracellularly secreted as well as cell-bound factors are among the major members of the ECM family. Proteins/glycoproteins, such as collagens, elastin, laminins and tenascins, proteoglycans and glycosaminoglycans, hyaluronan, and their cell receptors such as CD44
The matrilins: a novel family of oligomeric extracellular matrix proteins
Matrix Biology, 1999
The matrilin family at present has four members that all share a structure made up of von Willebrand factor A domains, Ž epidermal growth factor-like domains and a coiled coil ␣-helical module. The first member of the family, matrilin-1 previously . called cartilage matrix protein or CMP , is expressed mainly in cartilage. Matrilin-3 has a similar tissue distribution, while matrilin-2 and -4 occur in a wide variety of extracellular matrices. Matrilin-1 is associated with cartilage proteoglycans as well as being a component of both collagen-dependent and collagen-independent fibrils and on the basis of the related structures other matrilins may play similar roles. The matrilin genes are strictly and differently regulated and their expression may serve as markers for cellular differentiation. ᮊ
Principles of Medical Biochemistry, 2012
The exTracellular MaTrix chapter 14 The cells of soft tissues such as liver, brain, and epithelia are separated only by narrow clefts about 20nm wide. The mechanical properties of these tissues are determined by the cytoskeleton and by specialized cell-cell adhesions. Connective tissues, in contrast, consist mainly of extracellular matrix. The mechanical properties of these tissues are determined by the composition of the extracellular matrix. Several building materials contribute to the extracellular matrix (Fig. 14.1): * Bone from which the inorganic components (mainly calcium phosphates) have been removed by acid treatment. † Mainly in the dermis. The major structural proteins of the epidermis are the keratins (see Chapter 13). p0010 p0015 o0010 o0015 o0020 o0025 s0010 p0040 p0045 p0050 f0090 t0010 To protect the rights of the author(s) and publisher we inform you that this PDF is an uncorrected proof for internal business use only by the author(s), editor(s), reviewer(s), Elsevier and typesetter SPi. It is not allowed to publish this proof online or in print. This proof copy is the copyright property of the publisher and is confidential until formal publication. These proofs may contain colour figures. Those figures may print black and white in the final printed book if a colour print product has not been planned. The colour figures will appear in colour in all electronic versions of this book.