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The Extracellular Matrix as a Substrate for Stem Cell Growth and Development and Tissue Repair
Published in Richard K. Burt, Alberto M. Marmont, Stem Cell Therapy for Autoimmune Disease, 2019
Stephen F. Badylak, Mervin C. Yoder
Collagen types other than type I collagen exist in the ECM of virtually every tissue and organ, albeit in much lower quantities. These alternative collagen types each provide distinct mechanical and physical properties to the ECM and contribute to the population of ligands that interact with the resident cell populations. By way of example, Type III collagen exists within selected submucosal ECMs, such as the submucosal ECM of the urinary bladder; a location in which less rigid structure is required for appropriate function than is required in a tendinous or ligamentous location. Type IV collagen is present within the basement membrane of all vascular structures and is an important ligand for endothelial cells. Type VI collagen functions as a “connector” of glycosaminoglycan and functional proteins to larger structural proteins such as type I collagen, thus helping to provide a gel like consistency to the ECM. Type VII collagen is an essential component of the anchoring fibrils of keratinocytes to the underlying basement membrane of the epidermis. Each of these collagen types is of course the result of specific gene expression patterns as cells differentiate and tissues and organs develop and spatially organize.
Angiogenesis Treatment with CD13 Targeting Nanomedicines
Published in Sarwar Beg, Mahfoozur Rahman, Md. Abul Barkat, Farhan J. Ahmad, Nanomedicine for the Treatment of Disease, 2019
Madhu Gupta, Ramesh K. Goyal, Vikas Sharma
Angiogenesis is the formation of new blood vessels, and tumor growth depends on a steady blood supply with nutrients and oxygen for survival and tumor growth and ultimately for spreading the tumor cells into other tissue or site. These tumor blood vessels over-expressed certain markers that are either present at very low levels or are entirely absent in normal blood vessels like APN or CD13 marker. In tumor pathophysiology, APN levels raised due to hypoxia, angiogenic growth factors and others signals regulating capillary tube formation during angiogenesis (Bhagwat et al., 2001). Indeed, vascular endothelial growth factor (VEGF), a key angiogenesis regulator, induced the increased expression of APN at an early stage of tumor growth, which is crucial for sustained growth of most solid tumors. The endothelial cells produced several enzymes that are responsible for degradation of basement membrane components. These enzymes are type IV collagenases, matrix metalloproteases, and aminopeptidases. The studies supported that type IV collagen is substrate of the APN/CD13 and enhance the migration of endothelial cells into the surrounding tissue and contribute to the mechanism of tumor metastasis (Pasqualini et al., 2000). Finally, all the addressing issue turned the benign tumor to malignant tumor with raising the severity of the disease. Hence, the level of APN expression is inhibited then the angiogenesis and metastasis of the tumor can be inhibited, and growth of a tumor can be inhibited.
Tissue engineering and regenerative medicine
Published in Ronald L. Fournier, Basic Transport Phenomena in Biomedical Engineering, 2017
Although more than twenty types of collagen molecules have been identified, there are four that are most important. These are the fibrillar collagens (type I, type II, and type III) and type IV collagen. The first three types of collagen molecules assemble themselves into much larger structures called collagen fibrils that aggregate further to form collagen fibers. Type I collagen makes up about 90% of the collagen found in the body. It is found mostly in the skin, tendons, ligaments, various internal organs, and bone. Type II collagen is primarily found in cartilage, and type III collagen is found in blood vessels, as well as the skin. Type IV collagen organizes itself to form sheets within the basal lamina of the basement membrane. Fibroblasts have the ability to organize the collagen fibrils they secrete forming sheets or rope-like structures; therefore, they can affect the spatial organization of the matrix they produce.
Thioredoxin-1 and MMP-9 as biomarkers in breast cancer metastasis in Egyptian female patients
Published in Egyptian Journal of Basic and Applied Sciences, 2018
Al Shaima G. Abd El Salam, Mohamed A. Ebrahim, Laila A. Eissa, Mamdouh M. El-Shishtawy
MMP-9, also known as gelatinase B, is a 92-kDa endopeptidase that is strongly associated with aggressiveness and metastatic spread in breast cancer [14]. During tumor angiogenesis, MMP-9 degrades type IV collagen, the main component of vascular basement membrane surrounding tumor cells which is an essential process in initiation of metastasis. Furthermore, stroma-derived MMP-9 can facilitate the liberation of extracellular matrix (ECM)-sequestered VEGF that leads to metastasis [15].
Exploration of type II and III collagen binding interactions with short peptide-phenyl pyrazole conjugates via docking, molecular dynamics and laboratory experiments
Published in Soft Materials, 2023
Lucy R. Hart, Charlotta G. Lebedenko, Beatriz G. Goncalves, Mia I. Rico, Dominic J. Lambo, Diego S. Perez, Ipsita A. Banerjee
Of particular interest in tissue growth is the role of collagen, as it is the most abundant protein in the human body and plays a critical role.[6] Depending upon the type of tissue, the nature of collagen varies. Thus far, it has been reported that 28 different types of collagen exist and the distribution of various types of collagen depends upon the tissue type and location in the body.[7] While Type I collagen accounts for over 90% of collagen in the body, and has been studied in depth, comparatively lesser studies have focused on other types of collagen, and particularly their interactions with scaffolds. Interestingly, it has been reported that Type IV collagen is the primary constituent of basement membrane, particularly in skin tissue.[8] While all collagens share the triple-helix motif, Type IV collagen lacks a glycine in every third amino acid residue which leads to its relatively kinked structure. Type III collagen, on the other hand, makes up a significant part of connective tissue including in skin, lung, and the vascular endothelial systems. An interesting aspect of Type III collagen is the occurrence of cystine knots at the C-terminal, which is necessary for its stabilization.[9] In the articular cartilage of joints, type III collagen is present in different amounts as a part of the collagen fibrillar complex, cross-linked with collagen Type II.[10] Furthermore, Type III collagen is mostly formed in mature articular cartilage, and plays a critical role in wound healing and chondrocyte behavioral changes upon tissue damage by aiding in binding interactions with the collagen network. Additionally, Type III collagen aids in the fibrillogenesis of Type I collagen and in cardiovascular development,[11] and its mutation or abnormality leads to Type IV Ehlers–Danlos syndrome.[12] Type II collagen is a major constituent of cartilage, intervertebral discs, and the vitreous humor of the eye. It is essential for the proper development of bone and teeth.[13] It has been reported that Type II collagen has three identical α1-polypeptide chains, with significant triple-helical regions and relatively short, non-helical regions that do not contain the typical Gly-Pro-Hyp repeats that are generally found in the triple-helices of collagen.[14] Furthermore, proteoglycans bind to Type II collagen fibrils and stabilize its structure.[15] More importantly, Type II collagen is the main constituent of articular cartilage in mammals[16] and reduces articular chondrocyte hypertrophy and osteoarthritis.[17]