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Molecules (Basel, Switzerland) Nov 2019Hydrolyzed collagen (HC) is a group of peptides with low molecular weight (3-6 KDa) that can be obtained by enzymatic action in acid or alkaline media at a specific... (Review)
Review
Hydrolyzed collagen (HC) is a group of peptides with low molecular weight (3-6 KDa) that can be obtained by enzymatic action in acid or alkaline media at a specific incubation temperature. HC can be extracted from different sources such as bovine or porcine. These sources have presented health limitations in the last years. Recently research has shown good properties of the HC found in skin, scale, and bones from marine sources. Type and source of extraction are the main factors that affect HC properties, such as molecular weight of the peptide chain, solubility, and functional activity. HC is widely used in several industries including food, pharmaceutical, cosmetic, biomedical, and leather industries. The present review presents the different types of HC, sources of extraction, and their applications as a biomaterial.
Topics: Animals; Collagen; Humans; Protein Hydrolysates
PubMed: 31703345
DOI: 10.3390/molecules24224031 -
Cell and Tissue Research Jan 2010Integrins are cell adhesion receptors that are evolutionary old and that play important roles during developmental and pathological processes. The integrin family is... (Review)
Review
Integrins are cell adhesion receptors that are evolutionary old and that play important roles during developmental and pathological processes. The integrin family is composed of 24 alphabeta heterodimeric members that mediate the attachment of cells to the extracellular matrix (ECM) but that also take part in specialized cell-cell interactions. Only a subset of integrins (8 out of 24) recognizes the RGD sequence in the native ligands. In some ECM molecules, such as collagen and certain laminin isoforms, the RGD sequences are exposed upon denaturation or proteolytic cleavage, allowing cells to bind these ligands by using RGD-binding receptors. Proteolytic cleavage of ECM proteins might also generate fragments with novel biological activity such as endostatin, tumstatin, and endorepellin. Nine integrin chains contain an alphaI domain, including the collagen-binding integrins alpha1beta1, alpha2beta1, alpha10beta1, and alpha11beta1. The collagen-binding integrins recognize the triple-helical GFOGER sequence in the major collagens, but their ability to recognize these sequences in vivo is dependent on the fibrillar status and accessibility of the interactive domains in the fibrillar collagens. The current review summarizes some basic facts about the integrin family including a historical perspective, their structure, and their ligand-binding properties.
Topics: Animals; Collagen; Extracellular Matrix Proteins; Humans; Integrins; Oligopeptides; Protein Structure, Quaternary
PubMed: 19693543
DOI: 10.1007/s00441-009-0834-6 -
Matrix Biology : Journal of the... 2015Most abundant in the extracellular matrix are collagens, joined by elastin that confers elastic recoil to the lung, aorta, and skin. These fibrils are highly resistant... (Review)
Review
Most abundant in the extracellular matrix are collagens, joined by elastin that confers elastic recoil to the lung, aorta, and skin. These fibrils are highly resistant to proteolysis but can succumb to a minority of the matrix metalloproteinases (MMPs). Considerable inroads to understanding how such MMPs move to the susceptible sites in collagen and then unwind the triple helix of collagen monomers have been gained. The essential role in unwinding of the hemopexin-like domain of interstitial collagenases or the collagen binding domain of gelatinases is highlighted. Elastolysis is also facilitated by the collagen binding domain in the cases of MMP-2 and MMP-9, and remote exosites of the catalytic domain in the case of MMP-12.
Topics: Binding Sites; Collagen; Elastin; Humans; Matrix Metalloproteinases; Models, Molecular; Protein Binding; Protein Structure, Secondary; Proteolysis; Substrate Specificity
PubMed: 25599938
DOI: 10.1016/j.matbio.2015.01.005 -
Theranostics 2022The skin epidermis and appendages undergo ongoing renewal throughout life. Stem cells residing in the epidermis and hair follicles are pivotal for sustaining skin... (Review)
Review
The skin epidermis and appendages undergo ongoing renewal throughout life. Stem cells residing in the epidermis and hair follicles are pivotal for sustaining skin homeostasis. The self-renewal ability of stem cells significantly decreases during skin aging but actively increases during wound repair. Residential stem cells reside in niches that provide spatially distinct microenvironments for stem cell maintenance and function. Cell-extracellular matrix (ECM) adhesion is essential for the establishment of niche architecture. Collagen XVII (COL17), as a transmembrane protein constituting hemidesmosomes (HDs), mediates the interactions of stem cells with surrounding cells and the matrix to regulate skin homeostasis, aging and wound repair. This review focuses on the pivotal role of the niche component COL17 in stem cell maintenance and its function in regulation of skin aging and wound repair.
Topics: Autoantigens; Non-Fibrillar Collagens; Skin Aging; Stem Cell Niche; Collagen Type XVII
PubMed: 36185608
DOI: 10.7150/thno.78016 -
Clinical and Translational Medicine Dec 2022
Topics: Humans; Keloid; Collagen; Fibroblasts; Macrophages; Osteopontin; Extracellular Matrix Proteins
PubMed: 36480415
DOI: 10.1002/ctm2.1115 -
Ageing Research Reviews Mar 2021Elastic fibers are essential constituents of the extracellular matrix of higher vertebrates and endow several tissues and organs including lungs, skin and blood vessels... (Review)
Review
Elastic fibers are essential constituents of the extracellular matrix of higher vertebrates and endow several tissues and organs including lungs, skin and blood vessels with elasticity and resilience. During the human lifespan, elastic fibers are exposed to a variety of enzymatic, chemical and biophysical influences, and accumulate damage due to their low turnover. Aging of elastin and elastic fibers involves enzymatic degradation, oxidative damage, glycation, calcification, aspartic acid racemization, binding of lipids and lipid peroxidation products, carbamylation and mechanical fatigue. These processes can trigger an impairment or loss of elastic fiber function and are associated with severe pathologies. There are different inherited or acquired pathological conditions, which influence the structure and function of elastic fibers and microfibrils predominantly in the cardiorespiratory system and skin. Inherited elastic-fiber pathologies have a direct or indirect impact on elastic-fiber formation due to mutations in the fibrillin genes (fibrillinopathies), in the elastin gene (elastinopathies) or in genes encoding proteins that are associated with microfibrils or elastic fibers. Acquired elastic-fiber pathologies appear age-related or as a result of multiple factors impairing tissue homeostasis. This review gives an overview on the fate of elastic fibers over the human lifespan in health and disease.
Topics: Aging; Animals; Elastic Tissue; Elastin; Fibrillins; Humans; Microfilament Proteins
PubMed: 33434682
DOI: 10.1016/j.arr.2021.101255 -
Journal of Dental Research Feb 2023Fibromodulin (FMOD) is an archetypal member of the class II small leucine-rich proteoglycan family. By directly binding to extracellular matrix structural components,... (Review)
Review
Fibromodulin (FMOD) is an archetypal member of the class II small leucine-rich proteoglycan family. By directly binding to extracellular matrix structural components, such as collagen and lysyl oxidase, FMOD regulates collagen cross-linking, packing, assembly, and fibril architecture via a multivalent interaction. Meanwhile, as a pluripotent molecule, FMOD acts as a ligand of various cytokines and growth factors, especially those belonging to the transforming growth factor (TGF) β superfamily, by interacting with the corresponding signaling molecules involved in cell adhesion, spreading, proliferation, migration, invasion, differentiation, and metastasis. Consequently, FMOD exhibits promigratory, proangiogenic, anti-inflammatory, and antifibrogenic properties and plays essential roles in cell fate determination and maturation, progenitor cell recruitment, and tissue regeneration. The multifunctional nature of FMOD thus enables it to be a promising therapeutic agent for a broad repertoire of diseases, including but not limited to arthritis, temporomandibular joint disorders, caries, and fibrotic diseases among different organs, as well as to be a regenerative medicine candidate for skin, muscle, and tendon injuries. Moreover, FMOD is also considered a marker for tumor diagnosis and prognosis prediction and a potential target for cancer treatment. Furthermore, FMOD itself is sufficient to reprogram somatic cells into a multipotent state, creating a safe and efficient cell source for various tissue reconstructions and thus opening a new avenue for regenerative medicine. This review focuses on the recent preclinical efforts bringing FMOD research and therapies to the forefront. In addition, a contemporary understanding of the mechanism underlying FMOD's function, particularly its interaction with TGFβ superfamily members, is also discussed at the molecular level to aid the discovery of novel FMOD-based treatments.
Topics: Fibromodulin; Collagen; Wound Healing; Cell Adhesion; Cell Differentiation; Transforming Growth Factor beta; Extracellular Matrix Proteins
PubMed: 36515321
DOI: 10.1177/00220345221138525 -
International Journal of Molecular... Aug 2022Cartilage oligomeric matrix protein (COMP) is an extracellular matrix (ECM) glycoprotein that is critical for collagen assembly and ECM stability. Mutations of COMP... (Review)
Review
Cartilage oligomeric matrix protein (COMP) is an extracellular matrix (ECM) glycoprotein that is critical for collagen assembly and ECM stability. Mutations of COMP cause endoplasmic reticulum stress and chondrocyte apoptosis, resulting in rare skeleton diseases. The bouquet-like structure of COMP allows it to act as a bridging molecule that regulates cellular phenotype and function. COMP is able to interact with many other ECM components and binds directly to a variety of cellular receptors and growth factors. The roles of COMP in other skeleton diseases, such as osteoarthritis, have been implied. As a well-established biochemical marker, COMP indicates cartilage turnover associated with destruction. Recent exciting achievements indicate its involvement in other diseases, such as malignancy, cardiovascular diseases, and tissue fibrosis. Here, we review the basic concepts of COMP and summarize its novel functions in the regulation of signaling events. These findings renew our understanding that COMP has a notable function in cell behavior and disease progression as a signaling regulator. Interestingly, COMP shows distinct functions in different diseases. Targeting COMP in malignancy may withdraw its beneficial effects on the vascular system and induce or aggravate cardiovascular diseases. COMP supplementation is a promising treatment for OA and aortic aneurysms while it may induce tissue fibrosis or cancer metastasis.
Topics: Cardiovascular Diseases; Cartilage; Cartilage Oligomeric Matrix Protein; Chondrocytes; Extracellular Matrix Proteins; Fibrosis; Humans; Matrilin Proteins; Osteoarthritis
PubMed: 36012514
DOI: 10.3390/ijms23169253 -
Circulation Research May 2022
Topics: Extracellular Matrix; Extracellular Matrix Proteins; Fibronectins; Tenascin
PubMed: 35617358
DOI: 10.1161/CIRCRESAHA.122.321196 -
Circulation. Cardiovascular Imaging Aug 2018
Topics: Atherosclerosis; Elastin; Humans; Plaque, Atherosclerotic; Tropoelastin
PubMed: 30354504
DOI: 10.1161/CIRCIMAGING.118.008147