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Biological-Derived Biomaterials for Stem Cell Culture and Differentiation
Published in Gilson Khang, Handbook of Intelligent Scaffolds for Tissue Engineering and Regenerative Medicine, 2017
Collagen biocompatibility and possible degradation by human collagenases are responsible for the widespread use of this material in many biomedical applications. On the other hand, the rate of the degradation process often needs to be regulated using diverse methods such as crosslinking techniques19,20 or a structural modification agent like epigallocatechin-3-gallate (EGCG).21 Therefore, biodegradation of collagen-based biomaterials for applications such as tissue engineering could potentially lead to the restoration of tissue structure and functionality.22 Collagenases such as matrix metalloproteinase (MMP) are responsible for most collagen degradation in vivo. It is also important to know that all collagenases have a different rate of collagen hydrolysis.
Intrinsic Fluorescence Spectroscopy of Biological Tissue
Published in Mary-Ann Mycek, Brian W. Pogue, Handbook of Biomedical Fluorescence, 2003
Irene Georgakoudi, Michael S. Feld, Markus G. Müller
Note that there is a substantial increase in the relative NAD(P)H contribution for the dysplastic sites compared with the non-dysplastic sites for Barrett’s esophagus and cervical tissues. This change could be the result of an increased number of cells and/or increased levels of metabolic activity in the epithelial cells [5]. A significant decrease in the relative contribution of collagen to the overall tissue fluorescence spectra characterizes the dysplastic Barrett’s esophagus sites and the cervical sites of the transformation zone. The transformation zone consists of tissue that undergoes constant change as the squamous epithelium gradually replaces the columnar epithelium. Collagenases (enzymes that break down collagen) are known to play an important role in processes that take place during significant tissue architectural changes, as in the case of wound healing and tissue regeneration [30]. Changes in the expression of matrix metalloproteinases (MMPs), which are types of collagenases, have been reported in dysplastic lesions in the cervix [31], bronchus [32], and oral cavity [33]. In addition, it has been shown that an increased level of cysteine and serine proteases, which are known to be MMP activators [34], is found in gastric and colorectal cancerous and precancerous lesions [35]. Furthermore, the presence of MMPs is essential during tumor invasion and metastasis [36]. It is possible that the decrease in collagen fluorescence observed within sites of dysplasia or of the dynamically changing transformation zone of the cervix can be attributed to the presence of collagenases degrading the fluorescing collagen crosslinks.
Protein-Based Hydrogels
Published in Claudio Migliaresi, Antonella Motta, Scaffolds for Tissue Engineering, 2014
Claudio Migliaresi, Antonella Motta
for implantation since only few persons possess specific immunity against it, that can be easily revealed by serologic allergenic tests. Collagen is degraded by collagenase, an enzyme present in our body, which breaks the peptide bonds in collagen.
Extracellular collagenase isolated from Streptomyces antibioticus UFPEDA 3421: purification and biochemical characterization
Published in Preparative Biochemistry & Biotechnology, 2023
Elizianne Pereira Costa, Romero Marcos Pedrosa Brandão-Costa, Wendell Wagner Campos Albuquerque, Thiago Pajeú Nascimento, Amanda Emmanuelle Sales Conniff, Kethylen Barbara Barbosa Cardoso, Anna Gabrielly Duarte Neves, Juanize Matias da Silva Batista, Ana Lúcia Figueiredo Porto
Microbial collagenases [E.C. 3.4.24.3] are metalloproteinases (MMPs) that belong to M9 family of metallopeptidases, but it may also include some serine proteases from the S1, S8, and S53 families.[1,2] The S8 family proteases, characterized by an Asp-His-Ser catalytic triad (DHS triad), are often accompanied, on either side, by other domains. A similar His-Asp-Ser catalytic triad is present in S1 protease family, what is described as a clear example of convergent evolution. Collagenases are responsible for degrading the triple-helix structure of native collagen. Microbial collagenases are less specific than animal collagenases and cleave several types of collagens, including insoluble collagen and denatured collagen.[3] These enzymes are widely used in industrial processes and in therapeutic procedures as: meat softening, leather tanning, production of beer, transplants, treatment of skin disease, of glaucoma, treatment of fibrosis, Dupuytren’s disease, Peyronie’s disease, treatment of scars and burns.[4–10] Despite of having enormous applications, the use of collagen is predominantly limited because of its high cost. Moreover, collagen degradation produces fragments of peptides with potential antimicrobial and antioxidant activities, which also result in increases in skin firmness and osteoblasts proliferation.[11–14]
Production and characterization of collagenase from a new Amazonian Bacillus cereus strain
Published in Preparative Biochemistry & Biotechnology, 2019
Alexsandra C. L. Pequeno, Aline A. Arruda, Douglas F. Silva, José M. W. Duarte Neto, Vladimir M. Silveira Filho, Attilio Converti, Daniela A. V. Marques, Ana L. F. Porto, Carolina A. Lima
Collagenases have several industrial, biotechnological, pharmacological, and medicinal applications. They are used to tenderize meat in the food industry,[11] improve dye exhaustion in fur and hide tanning,[12] isolate and cultivate mammalian cells,[13] clean blood for improved screening in medical diagnostics,[14] and enhance semen rheological characteristics.[15] Their therapeutic applications include treatments of burns and ulcers,[16,17] elimination of scar tissue,[18,19] prevention of complications during organ transplantation,[20,21] wound healing,[16] treatment of Peyronie’s disease,[22] and various types of destructive fibrosis such as liver cirrhosis.[23] Peptides formed by enzymatic hydrolysis of collagen and gelatin find wide applications, among which are cosmetic moisturizers, dietary materials, immunotherapeutic agents, agents for treating osteoporosis, gastric ulceration, and hypertension.[24]
Devices for penile traction: the long and winding road to treating Peyronie’s disease
Published in Expert Review of Medical Devices, 2018
Shaan A Setia, Laurence A Levine
Most oral therapies (e.g. pentoxifylline, vitamin E, Potaba, colchicine) are thought to reduce inflammation and/or decrease fibrotic activity [29–33]. However, multiple studies have shown a lack of efficacy, particularly as monotherapy. A literature review from 2012 reports that there is no oral therapy that reliably reduces the signs and symptoms of PD in a clinically meaningful way [34]. ILI, on the other hand, represents an option more likely to provide meaningful benefit. Multiple different medications have been used with varying success. Calcium channel blockers such as verapamil or nicardipine have been shown to decrease fibroblast proliferation, increase collagenase activity, and decrease fibroblast ECM production in vitro [35]. Clinically, there are no large-scale, randomized placebo-controlled trials for calcium channel blockers. However, multiple small trials have shown some benefit [36–39]. Similar to calcium channel blockers, interferon injections have also demonstrated an ability to reduce fibroblast proliferation, increase collagenase activity, and decrease ECM production in vitro [40]. However, clinical outcomes have been more mixed [41–43]. The only US Food and Drug Administration approved nonsurgical treatment option for PD is collagenase Clostridium histolyticum (CCH). Its approval was largely based on the outcomes of phase 3 randomized, double-blind, placebo-controlled trials in 2013 (IMPRESS I and II) [44]. Collagenase is an enzyme which breaks down collagen. The IMPRESS trials demonstrated a statistically significant decrease in penile curvature, symptom bother, and low serious adverse events in men using CCH injections versus placebo.