Enzymes that catalyze the degradation of collagen by acting on the peptide bonds.
A metalloproteinase which degrades helical regions of native collagen to small fragments. Preferred cleavage is -Gly in the sequence -Pro-Xaa-Gly-Pro-. Six forms (or 2 classes) have been isolated from Clostridium histolyticum that are immunologically cross-reactive but possess different sequences and different specificities. Other variants have been isolated from Bacillus cereus, Empedobacter collagenolyticum, Pseudomonas marinoglutinosa, and species of Vibrio and Streptomyces. EC
A member of the MATRIX METALLOPROTEINASES that cleaves triple-helical COLLAGEN types I, II, and III.
A species of gram-positive, strongly proteolytic bacteria in the family Clostridiaceae. It contains several forms of COLLAGENASE whose action can lead to GAS GANGRENE in humans and HORSES.
A secreted matrix metalloproteinase that plays a physiological role in the degradation of extracellular matrix found in skeletal tissues. It is synthesized as an inactive precursor that is activated by the proteolytic cleavage of its N-terminal propeptide.
A member of the metalloproteinase family of enzymes that is principally responsible for cleaving FIBRILLAR COLLAGEN. It can degrade interstitial collagens, types I, II and III.
Compounds that inhibit the enzyme activity or activation of MATRIX METALLOPROTEINASES.
A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH).
A family of secreted protease inhibitory proteins that regulates the activity of SECRETED MATRIX METALLOENDOPEPTIDASES. They play an important role in modulating the proteolysis of EXTRACELLULAR MATRIX, most notably during tissue remodeling and inflammatory processes.
ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.
A class of enzymes that catalyzes the degradation of gelatin by acting on the peptide bonds. EC 3.4.24.-.
A member of the family of TISSUE INHIBITOR OF METALLOPROTEINASES. It is a 21-kDa nonglycosylated protein found in tissue fluid and is secreted as a complex with progelatinase A by human fibroblast and uncomplexed from alveolar macrophages. An overexpression of TIMP-2 has been shown to inhibit invasive and metastatic activity of tumor cells and decrease tumor growth in vivo.
A family of zinc-dependent metalloendopeptidases that is involved in the degradation of EXTRACELLULAR MATRIX components.
A product formed from skin, white connective tissue, or bone COLLAGEN. It is used as a protein food adjuvant, plasma substitute, hemostatic, suspending agent in pharmaceutical preparations, and in the manufacturing of capsules and suppositories.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
An endopeptidase that is structurally similar to MATRIX METALLOPROTEINASE 2. It degrades GELATIN types I and V; COLLAGEN TYPE IV; and COLLAGEN TYPE V.
A member of the family of TISSUE INHIBITOR OF METALLOPROTEINASES. It is a N-glycosylated protein, molecular weight 28 kD, produced by a vast range of cell types and found in a variety of tissues and body fluids. It has been shown to suppress metastasis and inhibit tumor invasion in vitro.
An extracellular endopeptidase of vertebrate tissues similar to MATRIX METALLOPROTEINASE 1. It digests PROTEOGLYCAN; FIBRONECTIN; COLLAGEN types III, IV, V, and IX, and activates procollagenase. (Enzyme Nomenclature, 1992)
A secreted endopeptidase homologous with INTERSTITIAL COLLAGENASE, but which possesses an additional fibronectin-like domain.
Matrix metalloproteinases that are associated with the CELL MEMBRANE, either through transmembrane domains or GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORS. Membrane-type matrix metalloproteinases may act within the pericellular environment to influence the process of CELL MIGRATION.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
A genus of motile or nonmotile gram-positive bacteria of the family Clostridiaceae. Many species have been identified with some being pathogenic. They occur in water, soil, and in the intestinal tract of humans and lower animals.
Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice.
Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A protective layer of firm, flexible cartilage over the articulating ends of bones. It provides a smooth surface for joint movement, protecting the ends of long bones from wear at points of contact.
The sum of the weight of all the atoms in a molecule.
A meshwork-like substance found within the extracellular space and in association with the basement membrane of the cell surface. It promotes cellular proliferation and provides a supporting structure to which cells or cell lysates in culture dishes adhere.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
The outer covering of the body that protects it from the environment. It is composed of the DERMIS and the EPIDERMIS.
Detection of RNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Granular leukocytes having a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
The rate dynamics in chemical or physical systems.
Proteins prepared by recombinant DNA technology.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed.
A variation of the PCR technique in which cDNA is made from RNA via reverse transcription. The resultant cDNA is then amplified using standard PCR protocols.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.

Bone resorption induced by parathyroid hormone is strikingly diminished in collagenase-resistant mutant mice. (1/1761)

Parathyroid hormone (PTH) stimulates bone resorption by acting directly on osteoblasts/stromal cells and then indirectly to increase differentiation and function of osteoclasts. PTH acting on osteoblasts/stromal cells increases collagenase gene transcription and synthesis. To assess the role of collagenase in the bone resorptive actions of PTH, we used mice homozygous (r/r) for a targeted mutation (r) in Col1a1 that are resistant to collagenase cleavage of type I collagen. Human PTH(1-34) was injected subcutaneously over the hemicalvariae in wild-type (+/+) or r/r mice four times daily for three days. Osteoclast numbers, the size of the bone marrow spaces and periosteal proliferation were increased in calvariae from PTH-treated +/+ mice, whereas in r/r mice, PTH-induced bone resorption responses were minimal. The r/r mice were not resistant to other skeletal effects of PTH because abundant interstitial collagenase mRNA was detected in the calvarial periosteum of PTH-treated, but not vehicle-treated, r/r and +/+ mice. Calcemic responses, 0.5-10 hours after intraperitoneal injection of PTH, were blunted in r/r mice versus +/+ mice. Thus, collagenase cleavage of type I collagen is necessary for PTH induction of osteoclastic bone resorption.  (+info)

Activation of c-Jun N-terminal kinase 1 by UV irradiation is inhibited by wortmannin without affecting c-iun expression. (2/1761)

Activation of c-Jun N-terminal kinases (JNKs)/stress-activated protein kinases is an early response of cells upon exposure to DNA-damaging agents. JNK-mediated phosphorylation of c-Jun is currently understood to stimulate the transactivating potency of AP-1 (e.g., c-Jun/c-Fos; c-Jun/ATF-2), thereby increasing the expression of AP-1 target genes. Here we show that stimulation of JNK1 activity is not a general early response of cells exposed to genotoxic agents. Treatment of NIH 3T3 cells with UV light (UV-C) as well as with methyl methanesulfonate (MMS) caused activation of JNK1 and an increase in c-Jun protein and AP-1 binding activity, whereas antineoplastic drugs such as mafosfamide, mitomycin C, N-hydroxyethyl-N-chloroethylnitrosourea, and treosulfan did not elicit this response. The phosphatidylinositol 3-kinase inhibitor wortmannin specifically blocked the UV-stimulated activation of JNK1 but did not affect UV-driven activation of extracellular regulated kinase 2 (ERK2). To investigate the significance of JNK1 for transactivation of c-jun, we analyzed the effect of UV irradiation on c-jun expression under conditions of wortmannin-mediated inhibition of UV-induced stimulation of JNK1. Neither the UV-induced increase in c-jun mRNA, c-Jun protein, and AP-1 binding nor the activation of the collagenase and c-jun promoters was affected by wortmannin. In contrast, the mitogen-activated protein kinase/ERK kinase inhibitor PD98056, which blocked ERK2 but not JNK1 activation by UV irradiation, impaired UV-driven c-Jun protein induction and AP-1 binding. Based on the data, we suggest that JNK1 stimulation is not essential for transactivation of c-jun after UV exposure, whereas activation of ERK2 is required for UV-induced signaling leading to elevated c-jun expression.  (+info)

Recruitment of the retinoblastoma protein to c-Jun enhances transcription activity mediated through the AP-1 binding site. (3/1761)

The retinoblastoma susceptibility gene product (RB) is a transcriptional modulator. One of the targets for this modulator effect is the AP-1 binding site within the c-jun and collagenase promoters. The physical interactions between RB and c-Jun were demonstrated by co-immunoprecipitation of these two proteins using anti-c-Jun or anti-RB antisera, glutathione S-transferase affinity matrix binding assays in vitro, and electrophoretic mobility shift assays. The C-terminal site of the leucine zipper of c-Jun mediated the interaction with RB. Although the B-pocket domain of RB alone bound to c-Jun, a second c-Jun binding site in the RB was also suggested. Mammalian two-hybrid-based assay provided corroborative evidence that transactivation of gene expression by RB required the C-terminal region of c-Jun. We conclude that RB enhances transcription activity mediated through the AP-1 binding site. Adenovirus E1A or human papillomavirus E7 inhibits RB-mediated transcription activity. These data reveal that the interactions between these two distinct classes of oncoproteins RB and c-Jun may be involved in controlling cell growth and differentiation mediated by transcriptional regulation.  (+info)

Murine matrix metalloproteinase 9 gene. 5'-upstream region contains cis-acting elements for expression in osteoclasts and migrating keratinocytes in transgenic mice. (4/1761)

Knowledge about the regulation of cell lineage-specific expression of extracellular matrix metalloproteinases is limited. In the present work, the murine matrix metalloproteinase 9 (MMP-9) gene was shown to contain 13 exons, and the 2.8-kilobase pair upstream region was found to contain several common promoter elements including a TATA box-like motif, three GC boxes, four AP-1-like binding sites, an AP-2 site, and three PEA3 consensus sequences that may be important for basic activity of the gene. In order to identify cell-specific regulatory elements, constructs containing varying lengths of the upstream region in front of a LacZ reporter gene were made and studied for expression in transgenic mice generated by microinjection into fertilized oocytes. Analyses of the mice revealed that the presence of sequences between -2722 and -7745 allowed for expression in osteoclasts and migrating keratinocytes, i. e. cells that have been shown to normally express the enzyme in vivo. The results represent the first in vivo demonstration of the location of cell-specific control elements in a matrix metalloproteinase gene and show that element(s) regulating most cell-specific activities of 92-kDa type collagenase are located in the -2722 to -7745 base pair region.  (+info)

Expression and tissue localization of membrane-type 1, 2, and 3 matrix metalloproteinases in human astrocytic tumors. (5/1761)

Three different membrane-type matrix metalloproteinases (MT1-, MT2-, and MT3-MMPs) are known to activate in vitro the zymogen of MMP-2 (pro-MMP-2, progelatinase A), which is one of the key MMPs in invasion and metastasis of various cancers. In the present study, we have examined production and activation of pro-MMP-2, expression of MT1-, MT2-, and MT3-MMPs and their correlation with pro-MMP-2 activation, and localization of MMP-2, MT1-MMP, and MT2-MMP in human astrocytic tumors. The sandwich enzyme immunoassay demonstrates that the production levels of pro-MMP-2 in the anaplastic astrocytomas and glioblastomas are significantly higher than that in the low-grade astrocytomas (P<0.05 and P<0.01, respectively), metastatic brain tumors (P<0.05), or normal brains (P<0.01). Gelatin zymography indicates that the pro-MMP-2 activation ratio is significantly higher in the glioblastomas than in other astrocytic tumors (P<0.01), metastatic brain tumors (P<0.01), and normal brains (P<0.01). The quantitative reverse transcription polymerase chain reaction analyses demonstrate that MT1-MMP and MT2-MMP are expressed predominantly in glioblastoma tissues (17/17 and 12/17 cases, respectively), and their expression levels increase significantly as tumor grade increases. MT3-MMP is detectable in both astrocytic tumor and normal brain tissues, but the mean expression level is approximately 50-fold lower compared with that of MT1-MMP and MT2-MMP in the glioblastomas. The activation ratio of pro-MMP-2 correlates directly with the expression levels of MT1-MMP and MT2-MMP but not MT3-MMP. In situ hybridization indicates that neoplastic astrocytes express MT1-MMP and MT2-MMP in the glioblastoma tissues (5/5 cases and 5/5 cases, respectively). Immunohistochemically, MT1-MMP and MT2-MMP are localized to the neoplastic astrocytes in glioblastoma samples (17/17 cases and 12/17 cases, respectively), which are also positive for MMP-2. In situ zymography shows gelatinolytic activity in the glioblastoma tissues but not in the normal brain tissues. These results suggest that both MT1-MMP and MT2-MMP play a key role in the activation of pro-MMP-2 in the human malignant astrocytic tumors and that the gelatinolytic activity is involved in the astrocytic tumor invasion.  (+info)

Collagenase-3 (MMP-13) is expressed by tumor cells in invasive vulvar squamous cell carcinomas. (6/1761)

Collagenase-3 (MMP-13) is a human matrix metalloproteinase specifically expressed by invading tumor cells in squamous cell carcinomas (SCCs) of the head and neck. Here, we have further elucidated the role of MMP-13 in tumor invasion by examining its expression in invasive malignant tumors of the female genital tract. Using in situ hybridization, expression of MMP-13 mRNA was detected in 9 of 12 vulvar SCCs, primarily in tumor cells, but not in intact vulvar epithelium, in cervical SCCs (n = 12), or in endometrial (n = 11) or ovarian adenocarcinomas (n = 8). MMP-13 expression was especially abundant in vulvar carcinomas showing metastasis to lymph nodes and was associated with expression of membrane type 1 MMP by tumor cells and gelatinase-A (MMP-2) by stromal cells, as detected by immunohistochemistry. MMP-13 mRNAs were detected in 9 of 11 cell lines established from vulvar carcinomas and in 4 of 6 cell lines from cervical carcinomas, whereas endometrial (n = 10) and ovarian (n = 9) carcinoma cell lines were negative for MMP-13 mRNA. No correlation was detected between MMP-13 expression and p53 gene mutations in vulvar SCC cell lines. However, MMP-13 expression was detected in 5 of 6 vulvar and cervical SCC cell lines harboring HPV 16 or 68 DNA. These results show that MMP-13 is specifically expressed by malignantly transformed squamous epithelial cells, including vulvar SCC cells, and appears to serve as a marker for their invasive capacity.  (+info)

Oxidized low-density lipoprotein regulates matrix metalloproteinase-9 and its tissue inhibitor in human monocyte-derived macrophages. (7/1761)

BACKGROUND: Macrophages in human atherosclerotic plaques produce a family of matrix metalloproteinases (MMPs), which may influence vascular remodeling and plaque disruption. Because oxidized LDL (ox-LDL) is implicated in many proatherogenic events, we hypothesized that ox-LDL would regulate expression of MMP-9 and tissue inhibitor of metalloproteinase-1 (TIMP-1) in monocyte-derived macrophages. MWRHOSA AND RESULTS: Mononuclear cells were isolated from normal human subjects with Ficoll-Paque density gradient centrifugation, and adherent cells were allowed to differentiate into macrophages during 7 days of culture in plastic dishes. On day 7, by use of serum-free medium, the macrophages were incubated with various concentrations of native LDL (n-LDL) and copper-oxidized LDL. Exposure to ox-LDL (10 to 50 microg/mL) increased MMP-9 mRNA expression as analyzed by Northern blot, protein expression as measured by ELISA and Western blot, and gelatinolytic activity as determined by zymography. The increase in MMP-9 expression was associated with increased nuclear binding of transcription factor NF-kappaB and AP-1 complex on electromobility shift assay. In contrast, ox-LDL (10 to 50 microg/mL) decreased TIMP-1 expression. Ox-LDL-induced increase in MMP-9 expression was abrogated by HDL (100 microg/mL). n-LDL had no significant effect on MMP-9 or TIMP-1 expression. CONCLUSIONS: These data demonstrate that unlike n-LDL, ox-LDL upregulates MMP-9 expression while reducing TIMP-1 expression in monocyte-derived macrophages. Furthermore, HDL abrogates ox-LDL-induced MMP-9 expression. Thus, ox-LDL may contribute to macrophage-mediated matrix breakdown in the atherosclerotic plaques, thereby predisposing them to plaque disruption and/or vascular remodeling.  (+info)

The matrix metalloproteinase-9 regulates the insulin-like growth factor-triggered autocrine response in DU-145 carcinoma cells. (8/1761)

The androgen-independent human prostate adenocarcinoma cell line DU-145 proliferates in serum-free medium and produces insulin-like growth factors (IGF)-I, IGF-II, and the IGF type-1 receptor (IGF-1R). They also secrete three IGF-binding proteins (IGFBP), IGFBP-2, -3, and -4. Of these, immunoblot analysis revealed selective proteolysis of IGFBP-3, yielding fragments of 31 and 19 kDa. By using an anti-IGF-I-specific monoclonal antibody (mAb), we detect surface receptor-bound IGF-I on serum-starved DU-145 cells, which activates IGF-1R and triggers a mitogenic signal. Incubation of DU-145 cells with blocking anti-IGF-I, anti-IGF-II, or anti-IGF-I plus anti-IGF-II mAb does not, however, inhibit serum-free growth of DU-145. Conversely, anti-IGF-1R mAb and IGFBP-3 inhibit DNA synthesis. IGFBP-3 also modifies the DU-145 cell cycle, decreases p34(cdc2) levels, and IGF-1R autophosphorylation. The antiproliferative IGFBP-3 activity is not IGF-independent, since des-(1-3)IGF-I, which does not bind to IGFBP-3, reverses its inhibitory effect. DU-145 also secretes the matrix metalloproteinase (MMP)-9, which can be detected in both a soluble and a membrane-bound form. Matrix metalloproteinase inhibitors, but not serpins, abrogate DNA synthesis in DU-145 associated with the blocking of IGFBP-3 proteolysis. Overexpression of an antisense cDNA for MMP-9 inhibits 80% of DU-145 cell proliferation that can be reversed by IGF-I in a dose-dependent manner. Inhibition of MMP-9 expression is also associated with a decrease in IGFBP-3 proteolysis and with reduced signaling through the IGF-1R. Our data indicate an IGF autocrine loop operating in DU-145 cells, specifically modulated by IGFBP-3, whose activity may in turn be regulated by IGFBP-3 proteases such as MMP-9.  (+info)

Collagenases are a group of enzymes that have the ability to break down collagen, which is a structural protein found in connective tissues such as tendons, ligaments, and skin. Collagen is an important component of the extracellular matrix, providing strength and support to tissues throughout the body.

Collagenases are produced by various organisms, including bacteria, animals, and humans. In humans, collagenases play a crucial role in normal tissue remodeling and repair processes, such as wound healing and bone resorption. However, excessive or uncontrolled activity of collagenases can contribute to the development of various diseases, including arthritis, periodontitis, and cancer metastasis.

Bacterial collagenases are often used in research and medical applications for their ability to digest collagen quickly and efficiently. For example, they may be used to study the structure and function of collagen or to isolate cells from tissues. However, the clinical use of bacterial collagenases is limited due to concerns about their potential to cause tissue damage and inflammation.

Overall, collagenases are important enzymes that play a critical role in maintaining the health and integrity of connective tissues throughout the body.

Microbial collagenase is not a medical term per se, but it does refer to an enzyme that is used in various medical and research contexts. Collagenases are a group of enzymes that break down collagen, a structural protein found in connective tissues such as skin, tendons, and ligaments. Microbial collagenase is a type of collagenase that is produced by certain bacteria, such as Clostridium histolyticum.

In medical terms, microbial collagenase is used in various therapeutic and research applications, including:

1. Wound healing: Microbial collagenase can be used to break down and remove necrotic tissue from wounds, which can help promote healing and prevent infection.
2. Dental applications: Collagenases have been used in periodontal therapy to remove calculus and improve the effectiveness of root planing and scaling procedures.
3. Research: Microbial collagenase is a valuable tool for researchers studying the structure and function of collagen and other extracellular matrix proteins. It can be used to digest tissue samples, allowing scientists to study the individual components of the extracellular matrix.

It's important to note that while microbial collagenase has many useful applications, it must be used with care, as excessive or improper use can damage healthy tissues and cause adverse effects.

Matrix Metalloproteinase 8 (MMP-8), also known as Collagenase-2 or Neutrophil Collagenase, is an enzyme that belongs to the Matrix Metalloproteinases family. MMP-8 is primarily produced by neutrophils and has the ability to degrade various components of the extracellular matrix (ECM), including collagens, gelatin, and elastin. It plays a crucial role in tissue remodeling, wound healing, and inflammatory responses. MMP-8 is also involved in the pathogenesis of several diseases, such as periodontitis, rheumatoid arthritis, and cancer, where it contributes to the breakdown of the ECM and promotes tissue destruction and invasion.

'Clostridium histolyticum' is a gram-positive, anaerobic, spore-forming bacterium that is known to produce several exoenzymes, including collagenases and gelatinases. This organism is commonly found in soil and the intestinal tracts of humans and animals. It can cause severe soft tissue infections, including gas gangrene, due to its ability to produce powerful toxins that can cause tissue necrosis. 'Clostridium histolyticum' is also used in medical treatments for conditions such as chronic wounds and urinary tract disorders due to its collagenase production.

Medical Definition:

Matrix Metalloproteinase 13 (MMP-13), also known as collagenase 3, is an enzyme belonging to the family of Matrix Metalloproteinases. These enzymes are involved in the degradation of extracellular matrix components, playing crucial roles in various physiological and pathological processes such as tissue remodeling, wound healing, and cancer progression.

MMP-13 has a specific affinity for cleaving type II collagen, one of the major structural proteins found in articular cartilage. It is also capable of degrading other extracellular matrix components like proteoglycans, elastin, and gelatin. This enzyme is primarily produced by chondrocytes, synovial fibroblasts, and osteoblasts.

Increased expression and activity of MMP-13 have been implicated in the pathogenesis of several diseases, most notably osteoarthritis (OA) and cancer. In OA, overexpression of MMP-13 leads to excessive degradation of articular cartilage, contributing to joint damage and degeneration. In cancer, MMP-13 facilitates tumor cell invasion and metastasis by breaking down the surrounding extracellular matrix.

Regulation of MMP-13 activity is essential for maintaining tissue homeostasis and preventing disease progression. Various therapeutic strategies aiming to inhibit MMP-13 activity are being explored as potential treatments for osteoarthritis and cancer.

Medical Definition of Matrix Metalloproteinase 1 (MMP-1):

Matrix metalloproteinase 1, also known as collagenase-1 or fibroblast collagenase, is a member of the matrix metalloproteinase family of enzymes. These enzymes are involved in degrading and remodeling extracellular matrix components, such as collagens, gelatins, and other proteins. MMP-1 specifically targets interstitial collagens (types I, II, III, VII, and X) and plays a crucial role in tissue repair, wound healing, and pathological processes like tumor invasion and metastasis. It is secreted as an inactive proenzyme and requires activation before it can carry out its proteolytic functions. MMP-1 activity is regulated at various levels, including transcription, activation, and inhibition by endogenous tissue inhibitors of metalloproteinases (TIMPs). Dysregulation of MMP-1 has been implicated in several diseases, such as arthritis, cancer, and fibrosis.

Matrix metalloproteinase inhibitors (MMPIs) are a class of pharmaceutical compounds that work by inhibiting the activity of matrix metalloproteinases (MMPs), which are a family of enzymes involved in the breakdown and remodeling of extracellular matrix (ECM) proteins. MMPs play important roles in various physiological processes, including tissue repair, wound healing, and angiogenesis, but they can also contribute to the pathogenesis of several diseases, such as cancer, arthritis, and cardiovascular disease.

MMPIs are designed to block the activity of MMPs by binding to their active site or zinc-binding domain, thereby preventing them from degrading ECM proteins. These inhibitors can be broad-spectrum, targeting multiple MMPs, or selective, targeting specific MMP isoforms.

MMPIs have been studied as potential therapeutic agents for various diseases, including cancer, where they have shown promise in reducing tumor growth, invasion, and metastasis by inhibiting the activity of MMPs that promote these processes. However, clinical trials with MMPIs have yielded mixed results, and some studies have suggested that broad-spectrum MMPIs may have off-target effects that can lead to adverse side effects. Therefore, there is ongoing research into developing more selective MMPIs that target specific MMP isoforms involved in disease pathogenesis while minimizing off-target effects.

Collagen is the most abundant protein in the human body, and it is a major component of connective tissues such as tendons, ligaments, skin, and bones. Collagen provides structure and strength to these tissues and helps them to withstand stretching and tension. It is made up of long chains of amino acids, primarily glycine, proline, and hydroxyproline, which are arranged in a triple helix structure. There are at least 16 different types of collagen found in the body, each with slightly different structures and functions. Collagen is important for maintaining the integrity and health of tissues throughout the body, and it has been studied for its potential therapeutic uses in various medical conditions.

A Tissue Inhibitor of Metalloproteinases (TIMPs) is a group of four naturally occurring proteins that play a crucial role in the regulation of extracellular matrix (ECM) remodeling. They function by inhibiting Matrix Metalloproteinases (MMPs), which are a family of enzymes responsible for degrading various components of the ECM, such as collagen and elastin.

By controlling MMP activity, TIMPs help maintain the balance between ECM synthesis and degradation, thereby ensuring proper tissue structure and function. An imbalance in TIMPs and MMPs has been implicated in various pathological conditions, including fibrosis, cancer, and inflammatory diseases.

There are four known TIMPs: TIMP1, TIMP2, TIMP3, and TIMP4, each with distinct expression patterns and substrate specificities. They not only inhibit MMPs but also have other functions, such as promoting cell survival, modulating cell growth and differentiation, and regulating angiogenesis.

Metalloendopeptidases are a type of enzymes that cleave peptide bonds in proteins, specifically at interior positions within the polypeptide chain. They require metal ions as cofactors for their catalytic activity, typically zinc (Zn2+) or cobalt (Co2+). These enzymes play important roles in various biological processes such as protein degradation, processing, and signaling. Examples of metalloendopeptidases include thermolysin, matrix metalloproteinases (MMPs), and neutrophil elastase.

Gelatinases are a group of matrix metalloproteinases (MMPs) that have the ability to degrade gelatin, which is denatured collagen. There are two main types of gelatinases: MMP-2 (gelatinase A) and MMP-9 (gelatinase B). These enzymes play important roles in various physiological processes such as tissue remodeling and wound healing, but they have also been implicated in several pathological conditions, including cancer, cardiovascular diseases, and neurological disorders.

MMP-2 is produced by a variety of cells, including fibroblasts, endothelial cells, and immune cells. It plays a crucial role in angiogenesis (the formation of new blood vessels) and tumor cell invasion and metastasis. MMP-9 is primarily produced by inflammatory cells such as neutrophils and macrophages, and it has been associated with the degradation of the extracellular matrix during inflammation and tissue injury.

Both MMP-2 and MMP-9 are synthesized as inactive zymogens and require activation by other proteases or physicochemical factors before they can exert their enzymatic activity. The regulation of gelatinase activity is tightly controlled at multiple levels, including gene expression, protein synthesis, secretion, activation, and inhibition. Dysregulation of gelatinase activity has been linked to various diseases, making them attractive targets for therapeutic intervention.

Tissue Inhibitor of Metalloproteinase-2 (TIMP-2) is a protein that inhibits the activity of matrix metalloproteinases (MMPs), which are enzymes involved in breaking down and remodeling extracellular matrix (ECM) components. TIMP-2 specifically inhibits MMP-2, also known as gelatinase A, by forming a 1:1 complex with it.

TIMP-2 is produced by various cell types, including fibroblasts, endothelial cells, and smooth muscle cells. It plays important roles in regulating ECM turnover, tissue remodeling, and wound healing. Imbalances between MMPs and TIMPs have been implicated in several pathological conditions, such as cancer, fibrosis, and cardiovascular diseases.

In the context of cancer, increased MMP-2 activity has been associated with tumor invasion and metastasis. TIMP-2 can counteract this effect by inhibiting MMP-2, thus potentially reducing tumor progression. However, the precise role of TIMP-2 in cancer is complex and may depend on various factors, including the type of cancer and the stage of disease progression.

Matrix metalloproteinases (MMPs) are a group of enzymes responsible for the degradation and remodeling of the extracellular matrix, the structural framework of most tissues in the body. These enzymes play crucial roles in various physiological processes such as tissue repair, wound healing, and embryonic development. They also participate in pathological conditions like tumor invasion, metastasis, and inflammatory diseases by breaking down the components of the extracellular matrix, including collagens, elastins, proteoglycans, and gelatins. MMPs are zinc-dependent endopeptidases that require activation from their proenzyme form to become fully functional. Their activity is tightly regulated at various levels, including gene expression, protein synthesis, and enzyme inhibition by tissue inhibitors of metalloproteinases (TIMPs). Dysregulation of MMPs has been implicated in several diseases, making them potential therapeutic targets for various clinical interventions.

Gelatin is not strictly a medical term, but it is often used in medical contexts. Medically, gelatin is recognized as a protein-rich substance that is derived from collagen, which is found in the skin, bones, and connective tissue of animals. It is commonly used in the production of various medical and pharmaceutical products such as capsules, wound dressings, and drug delivery systems due to its biocompatibility and ability to form gels.

In a broader sense, gelatin is a translucent, colorless, flavorless food ingredient that is derived from collagen through a process called hydrolysis. It is widely used in the food industry as a gelling agent, thickener, stabilizer, and texturizer in various foods such as candies, desserts, marshmallows, and yogurts.

It's worth noting that while gelatin has many uses, it may not be suitable for vegetarians or those with dietary restrictions since it is derived from animal products.

Protease inhibitors are a class of antiviral drugs that are used to treat infections caused by retroviruses, such as the human immunodeficiency virus (HIV), which is responsible for causing AIDS. These drugs work by blocking the activity of protease enzymes, which are necessary for the replication and multiplication of the virus within infected cells.

Protease enzymes play a crucial role in the life cycle of retroviruses by cleaving viral polyproteins into functional units that are required for the assembly of new viral particles. By inhibiting the activity of these enzymes, protease inhibitors prevent the virus from replicating and spreading to other cells, thereby slowing down the progression of the infection.

Protease inhibitors are often used in combination with other antiretroviral drugs as part of highly active antiretroviral therapy (HAART) for the treatment of HIV/AIDS. Common examples of protease inhibitors include saquinavir, ritonavir, indinavir, and atazanavir. While these drugs have been successful in improving the outcomes of people living with HIV/AIDS, they can also cause side effects such as nausea, diarrhea, headaches, and lipodystrophy (changes in body fat distribution).

Medical Definition:

Matrix metalloproteinase 9 (MMP-9), also known as gelatinase B or 92 kDa type IV collagenase, is a member of the matrix metalloproteinase family. These enzymes are involved in degrading and remodeling the extracellular matrix (ECM) components, playing crucial roles in various physiological and pathological processes such as wound healing, tissue repair, and tumor metastasis.

MMP-9 is secreted as an inactive zymogen and activated upon removal of its propeptide domain. It can degrade several ECM proteins, including type IV collagen, elastin, fibronectin, and gelatin. MMP-9 has been implicated in numerous diseases, such as cancer, rheumatoid arthritis, neurological disorders, and cardiovascular diseases. Its expression is regulated at the transcriptional, translational, and post-translational levels, and its activity can be controlled by endogenous inhibitors called tissue inhibitors of metalloproteinases (TIMPs).

Tissue Inhibitor of Metalloproteinase-1 (TIMP-1) is a protein that inhibits the activity of matrix metalloproteinases (MMPs), which are enzymes responsible for breaking down extracellular matrix proteins. TIMP-1 plays a crucial role in regulating the balance between the synthesis and degradation of the extracellular matrix, thereby maintaining tissue homeostasis. It is involved in various biological processes, including cell growth, differentiation, and apoptosis (programmed cell death). An imbalance between MMPs and TIMPs has been implicated in several pathological conditions, such as cancer, fibrosis, and inflammatory diseases.

Matrix metalloproteinase 3 (MMP-3), also known as stromelysin-1, is a member of the matrix metalloproteinase family. These are a group of enzymes involved in the degradation of the extracellular matrix, the network of proteins and other molecules that provides structural and biochemical support to surrounding cells. MMP-3 is secreted by various cell types, including fibroblasts, synovial cells, and chondrocytes, in response to inflammatory cytokines.

MMP-3 has the ability to degrade several extracellular matrix components, such as proteoglycans, laminin, fibronectin, and various types of collagen. It also plays a role in processing and activating other MMPs, thereby contributing to the overall breakdown of the extracellular matrix. This activity is crucial during processes like tissue remodeling, wound healing, and embryonic development; however, uncontrolled or excessive MMP-3 activation can lead to pathological conditions, including arthritis, cancer, and cardiovascular diseases.

In summary, Matrix metalloproteinase 3 (MMP-3) is a proteolytic enzyme involved in the degradation of the extracellular matrix and the activation of other MMPs. Its dysregulation has been implicated in several diseases.

Matrix metalloproteinase 2 (MMP-2), also known as gelatinase A, is an enzyme that belongs to the matrix metalloproteinase family. MMPs are involved in the breakdown of extracellular matrix components, and MMP-2 is responsible for degrading type IV collagen, a major component of the basement membrane. This enzyme plays a crucial role in various physiological processes, including tissue remodeling, wound healing, and angiogenesis. However, its dysregulation has been implicated in several pathological conditions, such as cancer, arthritis, and cardiovascular diseases. MMP-2 is synthesized as an inactive proenzyme and requires activation by other proteases or chemical modifications before it can exert its proteolytic activity.

Matrix metalloproteinases (MMPs) are a group of enzymes that can degrade various components of the extracellular matrix (ECM). Membrane-associated matrix metalloproteinases (MT-MMPs) are a subgroup of MMPs that are bound to the cell membrane through a transmembrane domain. They play important roles in ECM remodeling, tissue repair and regeneration, as well as in various pathological processes such as cancer invasion and metastasis.

MT-MMPs can activate other MMPs and convert pro-MMPs into their active forms. They also have the ability to cleave cell surface receptors, adhesion molecules, and growth factors, thereby regulating various cellular processes such as cell migration, proliferation, and apoptosis.

The membrane-associated matrix metalloproteinases include MMP-14 (MT1-MMP), MMP-15 (MT2-MMP), MMP-16 (MT3-MMP), MMP-17 (MT4-MMP), and MMP-24 (MT5-MMP). Dysregulation of MT-MMPs has been implicated in various diseases, including cancer, fibrosis, and neurodegenerative disorders.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

'Clostridium' is a genus of gram-positive, rod-shaped bacteria that are widely distributed in nature, including in soil, water, and the gastrointestinal tracts of animals and humans. Many species of Clostridium are anaerobic, meaning they can grow and reproduce in environments with little or no oxygen. Some species of Clostridium are capable of producing toxins that can cause serious and sometimes life-threatening illnesses in humans and animals.

Some notable species of Clostridium include:

* Clostridium tetani, which causes tetanus (also known as lockjaw)
* Clostridium botulinum, which produces botulinum toxin, the most potent neurotoxin known and the cause of botulism
* Clostridium difficile, which can cause severe diarrhea and colitis, particularly in people who have recently taken antibiotics
* Clostridium perfringens, which can cause food poisoning and gas gangrene.

It is important to note that not all species of Clostridium are harmful, and some are even beneficial, such as those used in the production of certain fermented foods like sauerkraut and natto. However, due to their ability to produce toxins and cause illness, it is important to handle and dispose of materials contaminated with Clostridium species carefully, especially in healthcare settings.

Pepsin A is defined as a digestive enzyme that is primarily secreted by the chief cells in the stomach's fundic glands. It plays a crucial role in protein catabolism, helping to break down food proteins into smaller peptides during the digestive process. Pepsin A has an optimal pH range of 1.5-2.5 for its enzymatic activity and is activated from its inactive precursor, pepsinogen, upon exposure to acidic conditions in the stomach.

Fibroblasts are specialized cells that play a critical role in the body's immune response and wound healing process. They are responsible for producing and maintaining the extracellular matrix (ECM), which is the non-cellular component present within all tissues and organs, providing structural support and biochemical signals for surrounding cells.

Fibroblasts produce various ECM proteins such as collagens, elastin, fibronectin, and laminins, forming a complex network of fibers that give tissues their strength and flexibility. They also help in the regulation of tissue homeostasis by controlling the turnover of ECM components through the process of remodeling.

In response to injury or infection, fibroblasts become activated and start to proliferate rapidly, migrating towards the site of damage. Here, they participate in the inflammatory response, releasing cytokines and chemokines that attract immune cells to the area. Additionally, they deposit new ECM components to help repair the damaged tissue and restore its functionality.

Dysregulation of fibroblast activity has been implicated in several pathological conditions, including fibrosis (excessive scarring), cancer (where they can contribute to tumor growth and progression), and autoimmune diseases (such as rheumatoid arthritis).

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Articular cartilage is the smooth, white tissue that covers the ends of bones where they come together to form joints. It provides a cushion between bones and allows for smooth movement by reducing friction. Articular cartilage also absorbs shock and distributes loads evenly across the joint, protecting the bones from damage. It is avascular, meaning it does not have its own blood supply, and relies on the surrounding synovial fluid for nutrients. Over time, articular cartilage can wear down or become damaged due to injury or disease, leading to conditions such as osteoarthritis.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

The extracellular matrix (ECM) is a complex network of biomolecules that provides structural and biochemical support to cells in tissues and organs. It is composed of various proteins, glycoproteins, and polysaccharides, such as collagens, elastin, fibronectin, laminin, and proteoglycans. The ECM plays crucial roles in maintaining tissue architecture, regulating cell behavior, and facilitating communication between cells. It provides a scaffold for cell attachment, migration, and differentiation, and helps to maintain the structural integrity of tissues by resisting mechanical stresses. Additionally, the ECM contains various growth factors, cytokines, and chemokines that can influence cellular processes such as proliferation, survival, and differentiation. Overall, the extracellular matrix is essential for the normal functioning of tissues and organs, and its dysregulation can contribute to various pathological conditions, including fibrosis, cancer, and degenerative diseases.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Endopeptidases are a type of enzyme that breaks down proteins by cleaving peptide bonds inside the polypeptide chain. They are also known as proteinases or endoproteinases. These enzymes work within the interior of the protein molecule, cutting it at specific points along its length, as opposed to exopeptidases, which remove individual amino acids from the ends of the protein chain.

Endopeptidases play a crucial role in various biological processes, such as digestion, blood coagulation, and programmed cell death (apoptosis). They are classified based on their catalytic mechanism and the structure of their active site. Some examples of endopeptidase families include serine proteases, cysteine proteases, aspartic proteases, and metalloproteases.

It is important to note that while endopeptidases are essential for normal physiological functions, they can also contribute to disease processes when their activity is unregulated or misdirected. For instance, excessive endopeptidase activity has been implicated in the pathogenesis of neurodegenerative disorders, cancer, and inflammatory conditions.

Gene expression regulation, enzymologic refers to the biochemical processes and mechanisms that control the transcription and translation of specific genes into functional proteins or enzymes. This regulation is achieved through various enzymatic activities that can either activate or repress gene expression at different levels, such as chromatin remodeling, transcription factor activation, mRNA processing, and protein degradation.

Enzymologic regulation of gene expression involves the action of specific enzymes that catalyze chemical reactions involved in these processes. For example, histone-modifying enzymes can alter the structure of chromatin to make genes more or less accessible for transcription, while RNA polymerase and its associated factors are responsible for transcribing DNA into mRNA. Additionally, various enzymes are involved in post-transcriptional modifications of mRNA, such as splicing, capping, and tailing, which can affect the stability and translation of the transcript.

Overall, the enzymologic regulation of gene expression is a complex and dynamic process that allows cells to respond to changes in their environment and maintain proper physiological function.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

In medical terms, the skin is the largest organ of the human body. It consists of two main layers: the epidermis (outer layer) and dermis (inner layer), as well as accessory structures like hair follicles, sweat glands, and oil glands. The skin plays a crucial role in protecting us from external factors such as bacteria, viruses, and environmental hazards, while also regulating body temperature and enabling the sense of touch.

Northern blotting is a laboratory technique used in molecular biology to detect and analyze specific RNA molecules (such as mRNA) in a mixture of total RNA extracted from cells or tissues. This technique is called "Northern" blotting because it is analogous to the Southern blotting method, which is used for DNA detection.

The Northern blotting procedure involves several steps:

1. Electrophoresis: The total RNA mixture is first separated based on size by running it through an agarose gel using electrical current. This separates the RNA molecules according to their length, with smaller RNA fragments migrating faster than larger ones.

2. Transfer: After electrophoresis, the RNA bands are denatured (made single-stranded) and transferred from the gel onto a nitrocellulose or nylon membrane using a technique called capillary transfer or vacuum blotting. This step ensures that the order and relative positions of the RNA fragments are preserved on the membrane, similar to how they appear in the gel.

3. Cross-linking: The RNA is then chemically cross-linked to the membrane using UV light or heat treatment, which helps to immobilize the RNA onto the membrane and prevent it from washing off during subsequent steps.

4. Prehybridization: Before adding the labeled probe, the membrane is prehybridized in a solution containing blocking agents (such as salmon sperm DNA or yeast tRNA) to minimize non-specific binding of the probe to the membrane.

5. Hybridization: A labeled nucleic acid probe, specific to the RNA of interest, is added to the prehybridization solution and allowed to hybridize (form base pairs) with its complementary RNA sequence on the membrane. The probe can be either a DNA or an RNA molecule, and it is typically labeled with a radioactive isotope (such as ³²P) or a non-radioactive label (such as digoxigenin).

6. Washing: After hybridization, the membrane is washed to remove unbound probe and reduce background noise. The washing conditions (temperature, salt concentration, and detergent concentration) are optimized based on the stringency required for specific hybridization.

7. Detection: The presence of the labeled probe is then detected using an appropriate method, depending on the type of label used. For radioactive probes, this typically involves exposing the membrane to X-ray film or a phosphorimager screen and analyzing the resulting image. For non-radioactive probes, detection can be performed using colorimetric, chemiluminescent, or fluorescent methods.

8. Data analysis: The intensity of the signal is quantified and compared to controls (such as housekeeping genes) to determine the relative expression level of the RNA of interest. This information can be used for various purposes, such as identifying differentially expressed genes in response to a specific treatment or comparing gene expression levels across different samples or conditions.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Neutrophils are a type of white blood cell that are part of the immune system's response to infection. They are produced in the bone marrow and released into the bloodstream where they circulate and are able to move quickly to sites of infection or inflammation in the body. Neutrophils are capable of engulfing and destroying bacteria, viruses, and other foreign substances through a process called phagocytosis. They are also involved in the release of inflammatory mediators, which can contribute to tissue damage in some cases. Neutrophils are characterized by the presence of granules in their cytoplasm, which contain enzymes and other proteins that help them carry out their immune functions.

"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

A peptide fragment is a short chain of amino acids that is derived from a larger peptide or protein through various biological or chemical processes. These fragments can result from the natural breakdown of proteins in the body during regular physiological processes, such as digestion, or they can be produced experimentally in a laboratory setting for research or therapeutic purposes.

Peptide fragments are often used in research to map the structure and function of larger peptides and proteins, as well as to study their interactions with other molecules. In some cases, peptide fragments may also have biological activity of their own and can be developed into drugs or diagnostic tools. For example, certain peptide fragments derived from hormones or neurotransmitters may bind to receptors in the body and mimic or block the effects of the full-length molecule.

Enzyme activation refers to the process by which an enzyme becomes biologically active and capable of carrying out its specific chemical or biological reaction. This is often achieved through various post-translational modifications, such as proteolytic cleavage, phosphorylation, or addition of cofactors or prosthetic groups to the enzyme molecule. These modifications can change the conformation or structure of the enzyme, exposing or creating a binding site for the substrate and allowing the enzymatic reaction to occur.

For example, in the case of proteolytic cleavage, an inactive precursor enzyme, known as a zymogen, is cleaved into its active form by a specific protease. This is seen in enzymes such as trypsin and chymotrypsin, which are initially produced in the pancreas as inactive precursors called trypsinogen and chymotrypsinogen, respectively. Once they reach the small intestine, they are activated by enteropeptidase, a protease that cleaves a specific peptide bond, releasing the active enzyme.

Phosphorylation is another common mechanism of enzyme activation, where a phosphate group is added to a specific serine, threonine, or tyrosine residue on the enzyme by a protein kinase. This modification can alter the conformation of the enzyme and create a binding site for the substrate, allowing the enzymatic reaction to occur.

Enzyme activation is a crucial process in many biological pathways, as it allows for precise control over when and where specific reactions take place. It also provides a mechanism for regulating enzyme activity in response to various signals and stimuli, such as hormones, neurotransmitters, or changes in the intracellular environment.

An Enzyme-Linked Immunosorbent Assay (ELISA) is a type of analytical biochemistry assay used to detect and quantify the presence of a substance, typically a protein or peptide, in a liquid sample. It takes its name from the enzyme-linked antibodies used in the assay.

In an ELISA, the sample is added to a well containing a surface that has been treated to capture the target substance. If the target substance is present in the sample, it will bind to the surface. Next, an enzyme-linked antibody specific to the target substance is added. This antibody will bind to the captured target substance if it is present. After washing away any unbound material, a substrate for the enzyme is added. If the enzyme is present due to its linkage to the antibody, it will catalyze a reaction that produces a detectable signal, such as a color change or fluorescence. The intensity of this signal is proportional to the amount of target substance present in the sample, allowing for quantification.

ELISAs are widely used in research and clinical settings to detect and measure various substances, including hormones, viruses, and bacteria. They offer high sensitivity, specificity, and reproducibility, making them a reliable choice for many applications.

Reverse Transcriptase Polymerase Chain Reaction (RT-PCR) is a laboratory technique used in molecular biology to amplify and detect specific DNA sequences. This technique is particularly useful for the detection and quantification of RNA viruses, as well as for the analysis of gene expression.

The process involves two main steps: reverse transcription and polymerase chain reaction (PCR). In the first step, reverse transcriptase enzyme is used to convert RNA into complementary DNA (cDNA) by reading the template provided by the RNA molecule. This cDNA then serves as a template for the PCR amplification step.

In the second step, the PCR reaction uses two primers that flank the target DNA sequence and a thermostable polymerase enzyme to repeatedly copy the targeted cDNA sequence. The reaction mixture is heated and cooled in cycles, allowing the primers to anneal to the template, and the polymerase to extend the new strand. This results in exponential amplification of the target DNA sequence, making it possible to detect even small amounts of RNA or cDNA.

RT-PCR is a sensitive and specific technique that has many applications in medical research and diagnostics, including the detection of viruses such as HIV, hepatitis C virus, and SARS-CoV-2 (the virus that causes COVID-19). It can also be used to study gene expression, identify genetic mutations, and diagnose genetic disorders.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Electron microscopy (EM) is a type of microscopy that uses a beam of electrons to create an image of the sample being examined, resulting in much higher magnification and resolution than light microscopy. There are several types of electron microscopy, including transmission electron microscopy (TEM), scanning electron microscopy (SEM), and reflection electron microscopy (REM).

In TEM, a beam of electrons is transmitted through a thin slice of the sample, and the electrons that pass through the sample are focused to form an image. This technique can provide detailed information about the internal structure of cells, viruses, and other biological specimens, as well as the composition and structure of materials at the atomic level.

In SEM, a beam of electrons is scanned across the surface of the sample, and the electrons that are scattered back from the surface are detected to create an image. This technique can provide information about the topography and composition of surfaces, as well as the structure of materials at the microscopic level.

REM is a variation of SEM in which the beam of electrons is reflected off the surface of the sample, rather than scattered back from it. This technique can provide information about the surface chemistry and composition of materials.

Electron microscopy has a wide range of applications in biology, medicine, and materials science, including the study of cellular structure and function, disease diagnosis, and the development of new materials and technologies.

Microbial collagenases have been identified from bacteria of both the Vibrio and Clostridium genera. Collagenase is used during ... Collagenases may be used for tenderizing meat in a manner similar to widely used tenderizers papain, bromelain and ficain. ... Collagenases at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (Protein pages needing a ... Collagenases are enzymes that break the peptide bonds in collagen. They assist in destroying extracellular structures in the ...
... (EC, matrix metalloproteinase 8, PMNL collagenase, MMP-8) is an enzyme. This enzyme catalyses ... Neutrophil+collagenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.24). ... Collagenase Hasty KA, Jeffrey JJ, Hibbs MS, Welgus HG (July 1987). "The collagen substrate specificity of human neutrophil ... Unlike EC, interstitial collagenase, this enzyme cleaves type III collagen more slowly than type I This enzyme belongs ...
... (EC, Clostridium histolyticum collagenase, clostridiopeptidase A, collagenase A, collagenase I, ... Collagenase Hanada, K.; Mizutani, T.; Yamagishi, M.; Tsuji, H.; Misaki, T.; Sawada, J. (1973). "The isolation of collagenase ... Achromobacter iophagus collagenase, collagenase, aspergillopeptidase C, nucleolysin, azocollase, metallocollagenase, ... Microbial+collagenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (Citation ...
... , also known as fibroblast collagenase, and matrix metalloproteinase-1 (MMP-1) is an enzyme that in ... MMP-1 was the first vertebrate collagenase both purified to homogeneity as a protein, and cloned as a cDNA. MMP-1 has an ... Dumin JA, Dickeson SK, Stricker TP, Bhattacharyya-Pakrasi M, Roby JD, Santoro SA, Parks WC (August 2001). "Pro-collagenase-1 ( ... Goldberg GI, Wilhelm SM, Kronberger A, Bauer EA, Grant GA, Eisen AZ (May 1986). "Human fibroblast collagenase. Complete primary ...
... may refer to one of two enzymes: Gelatinase A Gelatinase B This disambiguation page lists articles associated ... with the title Collagenase IV. If an internal link led you here, you may wish to change the link to point directly to the ...
Xiapex: collagenase clostridium histolyticum, European Medicines Agency, Undated.Accessed: 20 March 2011. Xiapex (Collagenase ... could reduce the efficacy of the collagenases, but no clinical evidence for such an interaction has been observed. "Collagenase ... Collagenase is no longer available on the National Health System except as part of a small clinical trial. On November 7, 2012 ... The substance is a constant mixture of two collagenases (AUX-I and AUX-II) with known amino acid sequences and a length of ...
... collagenases such as cathepsin B1; and hyaluronidase. PSGAG inhibits the synthesis of prostaglandin E2, which is released upon ...
Neutrophil collagenase, also known as matrix metalloproteinase-8 (MMP-8) or PMNL collagenase (MNL-CL), is a collagen cleaving ... 1991). "Characterization of 58-kilodalton human neutrophil collagenase: comparison with human fibroblast collagenase". ... 1995). "Neutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage ... 1990). "Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases". J. Biol. Chem ...
Collagenase No. 14 is present in MeSH but not listed as a collagenase, while No. 18 is absent from MeSH. The main substrates of ... These groups are the collagenases, the gelatinases, the stromelysins, and the membrane-type MMPs (MT-MMPs). The collagenases ... The collagenases are No. 1, No. 8, No. 13, and No. 18. In addition, No. 14 has also been shown to cleave fibrillar collagen, ... Eisen A, Jeffrey J, Gross J (1968). "Human skin collagenase. Isolation and mechanism of attack on the collagen molecule". ...
These collagenases break down protein into peptides. The peptides are subsequently reduced to their constituent amino acids, ... The first step in the process involves the elimination of the organic collagen fraction by the action of bacterial collagenases ...
The treatment with collagenase is different for the MCP joint and the PIP joint. In a MCP joint contracture the needle must be ... The collagenase is distributed across three injection points. For the PIP joint the needle must be placed not more than 4 mm ... Collagenase injection is likewise most effective for Stages I and II. However, it is also used at other stages.[citation needed ... Among those who worsen, clostridial collagenase injections or surgery may be tried. Radiation therapy may be used to treat this ...
Collagenase clostridium histolyticum is reported to help by breaking down the excess collagen in the penis. It was approved for ... Giorgio Pajardi, Marie A. Badalamente, Lawrence C. Hurst (2018). Collagenase in Dupuytren Disease. Springer. ISBN 9783319658223 ...
APMA is known to activate matrix metalloproteinase enzymes and collagenase. APMA activates proteolytic enzymes by reacting with ... Sellers, Anthony; Cartwright, Elizabeth; Murphy, Gillian; Reynolds, John (1977). "Evidence that Latent Collagenases are Enzyme- ... and thiol-blocking reagent used in experimental biology and chemistry to activate matrix metalloproteinases and collagenase ...
Examples are hyaluronidase and collagenase. These molecules, however, are enzymes that are secreted by a variety of organisms ...
Suppression of collagenase-1 expression". Arthritis and Rheumatism. 39 (9): 1535-1544. doi:10.1002/art.1780390914. PMID 8814066 ...
Bode W (June 1995). "A helping hand for collagenases: the haemopexin-like domain". Structure. 3 (6): 527-30. doi:10.1016/s0969- ...
"A helping hand for collagenases: the haemopexin-like domain". Structure. 3 (6): 527-30. doi:10.1016/s0969-2126(01)00185-x. PMID ...
These infectious agents produce proteases and collagenases which break down the corneal stroma. Complete loss of the stroma can ... Contains macroglobulins with anti-collagenase effects. A combination of the above may be necessary early in the disease course ... Treatment includes antibiotics and collagenase inhibitors such as acetylcysteine and homologous blood serum. Surgery may be ...
"Prostaglandin regulation of macrophage collagenase production". Proceedings of the National Academy of Sciences. 74 (11): 4955- ...
In recent decades, collagenase has begun to find various practical medical applications. The Ines Mandl Medical Foundation of ... Ines Mandl, Collagenase (Gordon and Breach 1972). "Ines Mandl". Legacy. Retrieved 11 August 2016. "Pioneering Biochemist's NYU- ... In 1950, she became the first scientist to extract collagenase from the bacterium Clostridium histolyticum. Other work involved ... was an Austrian-born American biochemist who was awarded the Garvan-Olin Medal in 1983 for her work on the enzyme collagenase. ...
Kabadjova, P.; Vlahov, S. (15 April 2014). "Regulation of Extracellular Collagenase Production in 91". Biotechnology & ...
The collagenases digest Types I, II, III, VII and X collagen. The gelatinases exist in two forms; one digesting Type-IV ... The extracellular matrix is degraded by metalloproteinases such as collagenases, gelatinases and matrix metalloproteinases, and ...
72 kDa type IV collagenase also known as matrix metalloproteinase-2 (MMP-2) and gelatinase A is an enzyme that in humans is ... Hrabec E, Naduk J, Strek M, Hrabec Z (2007). "[Type IV collagenases (MMP-2 and MMP-9) and their substrates--intracellular ... Identity with type IV collagenase from HT1080 cells". J. Biol. Chem. 267 (35): 25228-32. doi:10.1016/S0021-9258(19)74029-0. ... "Entrez Gene: MMP2 matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase)". Martignetti JA, Aqeel ...
Collagenase 3 is an enzyme that in humans is encoded by the MMP13 gene. It is a member of the matrix metalloproteinase (MMP) ... Gomis-Rüth FX, Gohlke U, Betz M, Knäuper V, Murphy G, López-Otín C, Bode W (December 1996). "The helping hand of collagenase-3 ... Barmina OY, Walling HW, Fiacco GJ, Freije JM, López-Otín C, Jeffrey JJ, Partridge NC (October 1999). "Collagenase-3 binds to a ... Deguchi JO, Aikawa E, Libby P, Vachon JR, Inada M, Krane SM, Whittaker P, Aikawa M (October 2005). "MMP-13/collagenase-3 ...
... K is the most potent mammalian collagenase. Cathepsin K is involved in osteoporosis, a disease in which a decrease in ...
... is made of hyaluronic acid and lubricin, proteinases, and collagenases. Synovial fluid exhibits non-Newtonian ...
Collagenases are zinc metalloproteases that cleave collagen and gelatin into small fragments. The seven collagenases are alpha ... Collagenase clostridium histolyticum is manufactured and marketed by Endo Pharmaceuticals in the US, and marketed by SOBI in ... This collagenase has been used to treat Dupuytren's contracture, a disease of pathological collagen production and deposition ... Collagenase clostridium histolyticum is secreted by the bacterium and can destroy connective tissue of muscles. ...
H. (1973). "A Collagenase in extracts of the invertebrate Bipalium kewense". Biochemical Journal. 133 (2): 329-334. doi:10.1042 ...
Wu H, Wu T, Xu X, Wang J, Wang J (May 2011). "Iron toxicity in mice with collagenase-induced intracerebral hemorrhage". J Cereb ...
Wu H, Wu T, Xu X, Wang J, Wang J (May 2011). "Iron toxicity in mice with collagenase-induced intracerebral hemorrhage". Journal ...
Microbial collagenases have been identified from bacteria of both the Vibrio and Clostridium genera. Collagenase is used during ... Collagenases may be used for tenderizing meat in a manner similar to widely used tenderizers papain, bromelain and ficain. ... Collagenases at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (Protein pages needing a ... Collagenases are enzymes that break the peptide bonds in collagen. They assist in destroying extracellular structures in the ...
Collagenase Clostridium histolyticum Injection: learn about side effects, dosage, special precautions, and more on MedlinePlus ... tell your doctor and pharmacist if you are allergic to collagenase Clostridium histolyticum injection, collagenase ointment ( ... 7 days prior to receiving collagenase injection. Also, tell your doctor if you have previously received collagenase Clostridium ... Collagenase Clostridium histolyticum injection comes as a powder to be mixed with a liquid and injected by a doctor. If you are ...
CLS-5 Collagenase, Type 5 Lot Number. u/mg dw Collagenase. u/mg dw Caseinase. u/mg dw Clostripain. u/mg dw Tryptic. A280nm @ 1 ... Prepared to contain 4-5X more collagenase, FALGPA and Caseinase activities than Collagenase 1-4 and with moderate clostripain ... The original AF grade collagenase with similar collagenase and secondary proteases to CLS-1 and CLS-2. ... Collagenase Sampling Program * Lot Selection Tool * Lot Survey * Sample Request * Distributors * About Us * Overview * Company ...
STRUCTURE OF ASTACIN AND IMPLICATIONS FOR ACTIVATION OF ASTACINS AND ZINC-LIGATION OF COLLAGENASES ... Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases.. Bode, W., Gomis-Ruth, F.X. ... such as vertebrate collagenases. It may therefore represent the elusive third zinc ligand in these enzymes. The amino ... STRUCTURE OF ASTACIN AND IMPLICATIONS FOR ACTIVATION OF ASTACINS AND ZINC-LIGATION OF COLLAGENASES. *PDB DOI: https://doi.org/ ...
Glibenclamide (10 μg/kg loading dose, 200 ng/h continuous infusion) was administered 2 hours post-ICH induced by collagenase ... Collagenases Is the Subject Area "Collagenases" applicable to this article? Yes. No. ...
BioAssay record AID 107858 submitted by ChEMBL: Inhibition of Matrix metalloprotease-8 (Human neutrophil collagenase, MMP-8).
are allergic to collagenase clostridium histolyticum, or any of the ingredients in Xiaflex, or to any other collagenase product ... Xiaflex (collagenase clostridium histolyticum): Dosage, Side Effects & Pregnancy Safety. March 3, 2020. ... Homebreast cancerXiaflex (collagenase clostridium histolyticum): Dosage, Side Effects & Pregnancy Safety ...
... collagenase clostridium histolyticum), frequency-based adverse effects, comprehensive interactions, contraindications, ... collagenase clostridium histolyticum topical COLLAGENASE OINTMENT - TOPICAL (coal-ADGE-ih-naze) COMMON BRAND NAME(S): Santyl ... collagenase clostridium histolyticum (Rx). Brand and Other Names:Xiaflex, Qwo, more...collagenase clostridium histolyticum-aaes ... encoded search term (collagenase clostridium histolyticum (Xiaflex%2C Qwo)) and collagenase clostridium histolyticum (Xiaflex, ...
Ønsker du mer informasjon om våre produkter eller tjenester ...
Neutrophil Collagenase) ELISA Kit from Innovative Research is intended for quantitative detection of rat MMP-8 in cell culture ... Neutrophil collagenase, a member of the family of matrix metalloproteinases, is distinct from the collagenase of skin ... Neutrophil collagenase has been found to possess 57% identity with the deduced protein sequence for fibroblast collagenase with ... When compared with the published sequence for fibroblast collagenase, neutrophil collagenase contains four additional sites for ...
Indonesian Purple Rice Ferulic Acid as a Candidate for Anti-aging through the Inhibition of Collagenase and Tyrosinase ... 11] Vijayakumar, R., Abd Gani, S.S., and Mokhtar, N.F., 2017, Anti-elastase, anti-collagenase and antimicrobial activities of ... Indonesian Purple Rice Ferulic Acid as a Candidate for Anti-aging through the Inhibition of Collagenase and Tyrosinase ... and moderate anti-collagenase activities (IC50 74.18 ± 3.11 µg/mL). This study supports the use of Indonesian purple rice as a ...
BACKGROUND: To determine the safety and efficacy of collagenase clostridium histolyticum (CCH) injection for the treatment of ... Efficacy and safety of collagenase clostridium histolyticum for Dupuytren disease nodules: a randomized controlled trial.. ...
Collagenase. Collagenase ENZIM - the enzyme breaks down collagen with the release of the free amino acid oxyproline. An ... Collagenase is used in various areas where it is necessary to break down collagen fibers: biomedicine, dermatology and ... important property of collagenase is its ability to biodegrade the main protein of the extracellular matrix, collagen. The ...
Nordmark Collagenase NB 5 Sterile Grade, Nordmark Collagenase NB 4G Proved Grade, Nordmark Collagenase NB 4 Standard Grade ... Nordmark Collagenase NB 1 Premium Grade, Nordmark Neutral Protease NB, ... Collagenase N, Anti Collagenase, Collagenase Calculator, Drug Master File (DMF) and Frequently asked questions (FAQ): ... Home , Nordmark Collagenase NB Nordmark Collagenase NB Crescent Chemical Co., Inc. supplies Nordmark Collagenase NB obtained ...
Collagenase. The collagenase activity was determined using the synthetic peptide N-(3-(2-furyl)acryloyl)-Leu-Gly-Pro-Ala ( ... 1 The sample concentration used for tyrosinase was 0.0125 mg/mL and for collagenase was 0.0023 mg/mL, to overcome samples ... To study the use of OIBPE as potential anti-ageing and anti-inflammatory agents, the effects in elastase, collagenase, ... Table 4. Enzymatic inhibition assays of elastase, collagenase, hyaluronidase, and tyrosinase by olive by-products extracts. ...
Collagenase. Collagenase injection currently has limited evidence. The initial evaluation yielded unsatisfactory results, as an ... Compression and collagenase therapy may be especially helpful in combination, as both help to break down aberrant collagen ... Kang N, Sivakumar B, Sanders R, Nduka C, Gault D. Intra-lesional injections of collagenase are ineffective in the treatment of ... Collagenase followed by compression for the treatment of earlobe keloids. Dermatol Surg. 2014;40(5):519-24. ...
Supplier for Enzymes, Tissue Dissociation - Benefit from a regular stock of 10000 or more products and a shipping time of 24 hours.
Anti-Collagenase HRP polyclonal antibody is produced in sheep against clostridial Collagenase NB. Clostridial collagenase ... Produced in sheep against clostridial Collagenase NB. Recognizes several collagenase isoforms. Composition. IgG in PBS buffer ... Nordmark also offers an unconjugated antibody called Anti-Collagenase Antibody.. Ordering Information Product Name. Cat. No. ... immunostaining of tissue and analysis of residual collagenase impurities in cell preparations. ...
What does a collagenase do?. COLLAGENASE (kohl LAH jen ace) is an enzyme that breaks down collagen in damaged tissue and helps ... What causes collagenase?. In addition to being produced by some bacteria, collagenase can be made by the body as part of its ... What is a collagenase inhibitor?. Thiols are thought to inhibit corneal collagenases by binding to or removing an intrinsic ... Does collagenase require a prescription?. What is Collagenase SANTYL◊ Ointment? SANTYL Ointment is an FDA-approved prescription ...
Recombinant Mouse Collagenase 3 Protein. Synthesized in e. coli. Protein Tag: His. Purity: Greater than 90% as determined by ... Mouse Collagenase 3 Recombinant Protein Product Attributes. Product Type: Recombinant Protein. Recombinant Collagenase 3 based ... Be the first to review "Recombinant Mouse Collagenase 3 Protein" Cancel reply. Your email address will not be published. ... Protein Construction: A DNA sequence encoding the Mus musculus (Mouse) Collagenase 3, was expressed in the hosts and tags ...
Copyright and disclaimer for the Collagenase SANTYL◊ Ointment HCP website. See complete Safety and Prescribing Information on ... Collagenase ointment for the treatment of venous leg ulcers in outpatient care settings. Presented at: ISPOR 20th Annual ... Collagenase promotes the cellular responses to injury and wound healing in vivo. J Burns Wounds. 2005; 4:112-124. ... Indication: Collagenase SANTYL Ointment ("SANTYL") is indicated for debriding chronic dermal ulcers and severely burned areas. ...
How should I store my purified collagenase?. This product is stable for at least two years from date of manufacture if stored ... Recombinant vs Natural Collagenase, a Future Entry into the Human Islet Yield Table ... Additional studies have shown the reconstituted collagenase was successfully frozen and thawed three times as a concentrated or ...
Collagenase is an enzyme used in plastic surgery to break down collagen, allowing for the removal of scar tissue and the ... Learn about Collagenase from Dr. Karan Chopra, a board-certified plastic surgeon known for natural-looking results and ... FAQs about Collagenase. What is collagenase?. Collagenase is an enzyme that breaks down collagen, a protein found in connective ... How is collagenase used in plastic surgery?. Collagenase is used in plastic surgery to help break down and remove scar tissue, ...
Collagenase) online. Ordering Santyl Ointment online from Canada Med Pharmacy is quick and affordable. Save on your medication ... Buy Santyl Ointment (Collagenase). Canadian Pharmacy Meds / Santyl Ointment .showOnMobile { height: 10px; } .strengthWrapper { ... If the dressing becomes soiled, collagenase may be applied more frequently.. To apply Santyl ointment, wash your hands first. ...
Collagenase SANTYL® Ointment is an FDA-approved prescription ointment that cleans wounds to clear the way for healthy tissue. ... Collagenase SANTYL Ointment , Collagenase SANTYL Ointment 250 units/g - Collagenase SANTYL® Ointment is an FDA-approved ...
Collagenase Enzymes / ES INFINI COLLAGENBOOSTER. Infini Aquaboost + C CollagenStimulate / IT JALUPRO + PLASMATHERAPY. Jalupro ...
Watson Bio Ltd develops Recombinant Collagenase I CAS 9001-12-1 Three-dimensional helical structure for the specific hydrolysis ... Recombinant Collagenase I CAS 9001-12-1 2022年6月28日. /in Enzymes, First Page, Key Products /by Janice Zhang. *Identification ... Recombinant Collagenase I. SMILES. CCCCCCCC[C@H]1CC[C@@]2([C@@]1(CC[C@]3(C2CC[C@@]4([C@@]3(Cc5c(nc6c(n5)C[C@@]7(CCC8[C@@]9(CC[C ... You are here: Home1 / Enzymes2 / Recombinant Collagenase I CAS 9001-12-1 ...
  • Collagenases are enzymes that break the peptide bonds in collagen. (wikipedia.org)
  • Collagen, a key component of the animal extracellular matrix, is made through cleavage of pro-collagen by collagenase once it has been secreted from the cell. (wikipedia.org)
  • Collagenase is used during bacterial attack to degrade the collagen barrier of the host during invasion. (wikipedia.org)
  • Collagen cleavage occurs at an Xaa+Got in Vibrio bacteria and at Yaa+Gly bonds in Clostridium collagenases. (wikipedia.org)
  • Collagenase ENZIM - the enzyme breaks down collagen with the release of the free amino acid oxyproline. (enzim.ua)
  • An important property of collagenase is its ability to biodegrade the main protein of the extracellular matrix, collagen. (enzim.ua)
  • Collagenase is used in various areas where it is necessary to break down collagen fibers: biomedicine, dermatology and cosmetology. (enzim.ua)
  • Collagenases obtained from Clostridium histolyticum are enzymes that break the peptide bond in collagen. (creschem.com)
  • COLLAGENASE (kohl LAH jen ace) is an enzyme that breaks down collagen in damaged tissue and helps healthy tissue to grow. (durrell2012.com)
  • This enzyme, called collagenase, dissolves collagen and is harvested from a bacterium, clostridium histolyticum. (durrell2012.com)
  • Degradation of human collagen isoforms by Clostridium collagenase and the effects of degradation products on cell migration. (santyl.com)
  • Collagenase is an enzyme that breaks down collagen , a protein found in the skin, tendons, and other connective tissues. (chopraplasticsurgery.com)
  • Collagenase is an enzyme that breaks down collagen , a protein found in connective tissues such as skin, tendons, and ligaments. (chopraplasticsurgery.com)
  • Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis. (ox.ac.uk)
  • The three-dimensional structure of a prototypic collagenase, MMP-1, indicates that the substrate-binding site of the enzyme is too narrow to accommodate triple-helical collagen. (ox.ac.uk)
  • CCH is composed of two purified collagenases that work to break down collagen when injected into fibrous tissue. (endo.com)
  • Collagenase clostridium histolyticum (CCH) is composed of 2 purified collagenases (AUX-I and AUX-II) that hydrolyze collagen under physiologic conditions, resulting in disruption of collagen containing structures. (endo.com)
  • Using Northern blot analysis and in situ hybridization on parallel sections of murine embryos and bones of newborn mice we compared the expression pattern of the recently cloned Itm2a and MMP-13 (collagenase-3) genes with that of established marker genes for bone formation, such as alkaline phosphatase (ALP), osteocalcin (OC), and collagen type X, during endochondral and intramembranous ossification. (nyu.edu)
  • This Rat Matrix Metalloproteinease-8 (Neutrophil Collagenase) ELISA Kit from Innovative Research is intended for quantitative detection of rat MMP-8 in cell culture supernates, serum and plasma (heparin). (innov-research.com)
  • Expression system for standard: Matrix metalloproteinase 8(MMP8) also called neutrophil collagenase. (innov-research.com)
  • Neutrophil collagenase, a member of the family of matrix metalloproteinases, is distinct from the collagenase of skin fibroblasts and synovial cells in substrate specificity and immunologic crossreactivity. (innov-research.com)
  • The human neutrophil collagenase(HNC) cDNA clone has been sequenced and shown to encode a 467-residue protein. (innov-research.com)
  • Neutrophil collagenase has been found to possess 57% identity with the deduced protein sequence for fibroblast collagenase with 72% chemical similarity. (innov-research.com)
  • When compared with the published sequence for fibroblast collagenase, neutrophil collagenase contains four additional sites for glycosylation. (innov-research.com)
  • What is Collagenase SANTYL◊ Ointment? (durrell2012.com)
  • Sheets AR, Demidova-Rice TN, Shi L, Ronfard V, Grover KV, Herman IM (2016) Identification and Characterization of Novel Matrix-Derived Bioactive Peptides: A Role for Collagenase from Santyl® Ointment in Post-Debridement Wound Healing? (santyl.com)
  • Clinical outcomes associated with serial sharp debridement of diabetic foot ulcers with and without clostridial collagenase ointment. (santyl.com)
  • Collagenase SANTYL® Ointment is an FDA-approved prescription ointment that cleans wounds to clear the way for healthy tissue. (spendlessformedicine.com)
  • The purpose of this study was to evaluate the effect of collagenase ointment on the epithelial healing of an abrasive wound induced by a radiofrequency system. (uchile.cl)
  • Results: The animals treated with collagenase ointment presented accelerated healing process and less inflammatory cell infiltration than the saline solution treated animals from one to fifteen postoperative days. (uchile.cl)
  • Conclusion: According to our results the use of collagenase ointment may accelerate the healing process of a radiofrequency induced abrasive wound. (uchile.cl)
  • DUBLIN , May 5, 2022 /PRNewswire/ -- Endo International plc (NASDAQ: ENDP) today announced the upcoming launch of a new clinical study relevant to the use of Qwo ® (collagenase clostridium histolyticum-aaes) for the treatment of moderate to severe cellulite in the buttocks of adult women. (endo.com)
  • The poster presentation, titled "APHRODITE-1: A Phase 2 Study of Different Interventions to Reduce Bruising Following Collagenase Clostridium Histolyticum-aaes Treatment for Cellulite of the Buttocks in Women," will share the objectives and unique design of this multi-cohort study which will test different interventions to assess their potential impact on reduction of bruising. (endo.com)
  • wound healing (Santyl) cellulite (Qwo) This group of metallopeptidases constitutes the MEROPS peptidase family M9, subfamilies M9A and M9B (microbial collagenase, clan MA(E)). The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA and the predicted active site residues for members of this family and thermolysin occur in the motif HEXXH. (wikipedia.org)
  • How do you use Santyl collagenase? (durrell2012.com)
  • Anti-Collagenase HRP polyclonal antibody is produced in sheep against clostridial Collagenase NB. (nordmark-pharma.de)
  • Clostridial collagenase consists of several collagenase isoforms which are recognized by the antibody. (nordmark-pharma.de)
  • Identification of clostridium histolyticum collagenase hyperreactive sites in type I, II, III collagens: lack of correlation with local triple helical stability. (santyl.com)
  • Enzyme vial of HIS kit that contains 20,000 units of collagenase (Code: CLS-1) and 30 units of elastase (Code: ESL), filtered through 0.22 micron membrane and lyophilized. (worthington-biochem.com)
  • Wounds with sufficient moisture will naturally activate collagenase enzyme. (durrell2012.com)
  • Calculation of Collagenase activity Units/mg = µmoles L-leucine (equivalent liberated) / mg enzyme in digestion mixture The 3 typical intrinsic activities of collagenase: Clostripain Clostripain activity is measured by the ability to hydrolyse N-benzoyl-L-arginine ethyl ester (BAEE) in the presence of the activator dithiothreitol (DTT). (durrell2012.com)
  • EZ-LiFT does not suffer from the drawbacks of other enzyme-based dissociation reagents such as Dispase, Collagenase IV and Accutase. (thomassci.com)
  • Collagenase Clostridium histolyticum injection is in a class of medications called enzymes. (medlineplus.gov)
  • citation needed] Collagenases have been approved for medical uses for: treatment of Dupuytren's contracture and Peyronie's disease (Xiaflex). (wikipedia.org)
  • Your doctor or pharmacist will give you the manufacturer's patient information sheet (Medication Guide) when you begin treatment with collagenase Clostridium histolyticum (Xiaflex) and each time you receive the medication. (medlineplus.gov)
  • Talk to your doctor about the risks of receiving collagenase Clostridium histolyticum injection (Xiaflex). (medlineplus.gov)
  • Collagenase Clostridium histolyticum injection (Xiaflex) is used to treat Dupuytren's contracture (a painless thickening and tightening of tissue [cord] beneath the skin in the palm of the hand, which may make it difficult to straighten one or more fingers) when a cord of tissue can be felt upon examination. (medlineplus.gov)
  • Collagenase Clostridium histolyticum injection (Xiaflex) is also used to treat Peyronie's disease (a thickening of tissue [plaque] inside the penis that causes the penis to curve). (medlineplus.gov)
  • If you are receiving collagenase Clostridium histolyticum injection (Xiaflex) to treat Dupuytren's contracture, your doctor will inject the medicine into a cord just under the skin in the affected hand. (medlineplus.gov)
  • If you are receiving collagenase Clostridium histolyticum injection (Xiaflex) to treat Peyronie's disease, your doctor will inject the medicine into the plaque that is causing your penis to curve. (medlineplus.gov)
  • are allergic to collagenase clostridium histolyticum , or any of the ingredients in Xiaflex, or to any other collagenase product. (hdkino.org)
  • Each lot assayed for collagenase, caseinase, clostripain and tryptic activities. (worthington-biochem.com)
  • Clostridium histolyticum secretes Collagenase Class I and II, Neutral Protease and Clostripain. (creschem.com)
  • Here, we describe a novel Salmonella typhimurium (ST) vector expressing the bacterial collagenase Streptomyces omiyaensis trypsin (SOT), a serine protease known to hydrolyze collagens I and IV, which are predominantly found in PDAC. (preprints.org)
  • Within this stretch is found PLGP, an amino acid sequence typical of collagenase substrates. (wikipedia.org)
  • This sequence may thus be implicated in self-processing of the collagenase. (wikipedia.org)
  • The third histidine (His 102) forms part of a consensus sequence, shared not only by the members of the astacin family, but also by otherwise sequentially unrelated proteinases, such as vertebrate collagenases. (rcsb.org)
  • A DNA sequence encoding the Mus musculus (Mouse) Collagenase 3, was expressed in the hosts and tags indicated. (enquirebio.com)
  • Efficacy and safety of collagenase clostridium histolyticum for Dupuytren disease nodules: a randomized controlled trial. (qxmd.com)
  • To determine the safety and efficacy of collagenase clostridium histolyticum (CCH) injection for the treatment of palmar Dupuytren disease nodules. (qxmd.com)
  • Collagenase Clostridium histolyticum injection (QWO) is also used to treat cellulite (fat deposit beneath the skin) in the buttocks of adult women. (medlineplus.gov)
  • Collagenase Clostridium histolyticum injection comes as a powder to be mixed with a liquid and injected by a doctor. (medlineplus.gov)
  • We sought to establish the in-vivo immune response in collagenase-induced OA and investigate the ability of human mesenchymal stem cells (hMSCs) overexpressing viral interleukin 10 (vIL-10) to modulate immune populations and delay/prevent disease progression. (nuigalway.ie)
  • In the present study, we investigated whether early treatment with a single dose of IL-1 ß blocking antibodies could prevent Western diet (WD) induced changes to systemic monocyte populations and their cytokine secretion profile and herewith modulate collagenase induced osteoarthritis (CiOA) pathology . (bvsalud.org)
  • A single dose of anti-IL-1ß antibodies prevents Western diet-induced immune activation during early stage collagenase-induced osteoarthritis, but does not ameliorate end-stage pathology. (bvsalud.org)
  • The use of collagenase minimizes trauma to the tissues, leading to faster healing and reduced downtime for patients. (chopraplasticsurgery.com)
  • however, pro-inflammatory cytokines, increased collagenase activity and advanced glycation end products (AGEs) may be responsible for destructive properties of DM affecting both oral soft and hard tissues [4]. (who.int)
  • are allergic to collagenase or to any of the ingredients in QWO, or have an active infection at the treatment area. (endo.com)
  • Manuel, E.R. Collagenase-Expressing Salmonella Targets Major Collagens in Pancreatic Cancer Leading to Reductions in Immunosuppressive Subsets and Tumor Growth. (preprints.org)
  • Endo International plc (NASDAQ:ENDP) announced today initial results from a Phase I study (EN3835-105) evaluating collagenase clostridium histolyticum (CCH) for the treatment of plantar fibromatosis. (endo.com)
  • Kim M, Hamilton S, Guddat L, Overall C. Plant collagenase: unique collagenolytic activity of cysteine proteases from ginger. (santyl.com)
  • Indonesian purple rice has a lower concentration of ferulic acid (4.114 ± 0.013 mg/L) than black rice but shows strong reducing power (IC 50 9.35 ± 1.95 µg/mL), high anti-tyrosinase (IC 50 59.57 ± 3.60 µg/mL), and moderate anti-collagenase activities (IC 50 74.18 ± 3.11 µg/mL). (ugm.ac.id)
  • Collagenase topical may also be used for other purposes not listed in this medication guide. (durrell2012.com)
  • This study correlates nuclear bone scan findings and measurements of type IV collagenases for the evaluation of bony metastasis in patients with proven breast cancer. (korea.ac.kr)
  • The authors retrospectively evaluated the final diagnosis of a bone scan and the results of an immunohistochemical staining for 92 kDa and 72 kDa type IV collagenases in, respectively, 30 and 30 patients with metastatic breast cancer, and, respectively, 27 and 26 patients with primary breast cancer. (korea.ac.kr)
  • The aim of this study was to comparatively evaluate the effects of the four main paradigms of tES, including tDCS, transcranial alternating (tACS), pulsed (tPCS), and random noise (tRNS) stimulations on collagenase-induced sensorimotor impairments and striatum tissue damage in male rats. (biomedcentral.com)
  • In vertebrates, it is initiated by collagenases belonging to the matrix metalloproteinase (MMP) family. (ox.ac.uk)
  • It is important to consult with a qualified plastic surgeon to discuss the potential risks and benefits of collagenase treatment. (chopraplasticsurgery.com)
  • Treatment of Dupuytren's Contracture With Collagenase: A Systematic Re" by Alexis B. Sandler, John P. Scanaliato et al. (gwu.edu)
  • To induce ICH, 0.5 μl of collagenase was injected into the right striatum of male Sprague Dawley rats. (biomedcentral.com)
  • This antibody can be used in ELISA and Western blot experiments, immunostaining of tissue and analysis of residual collagenase impurities in cell preparations. (nordmark-pharma.de)
  • In addition to being produced by some bacteria, collagenase can be made by the body as part of its normal immune response. (wikipedia.org)
  • Collagenase is used to soften and reshape scar tissue from previous pregnancies, allowing for a smoother and more aesthetically pleasing outcome. (chopraplasticsurgery.com)
  • A separate experiment was conducted to investigate resistance to collagenase digestion. (durrell2012.com)
  • Collagenase topical (for the skin) is used to treat severe burns or skin ulcers in adults. (durrell2012.com)
  • Collagenase topical (for the skin) is applied to severe burns or skin ulcers to help remove dead skin tissue and aid in wound healing. (durrell2012.com)
  • The results indicated that the application of the four tES paradigms (tDCS, tACS, tRNS, and tPCS) significantly reversed motor disorders in collagenase-induced ICH groups. (biomedcentral.com)
  • 170 92 kDa (26 of 27), 72 kDa (26 of 26) type IV collagenase, showed no active bony, lung, or liver metastases. (korea.ac.kr)
  • Methods: Eight-week-old male C57BL/6 mice were injected with 1 U type VII collagenase over two consecutive days. (nuigalway.ie)
  • Thiols are thought to inhibit corneal collagenases by binding to or removing an intrinsic metal cofactor (Zn), and/or possibly by reducing one or more disulfide bonds. (durrell2012.com)
  • Here we report that collagenases bind and locally unwind the triple-helical structure before hydrolyzing the peptide bonds. (ox.ac.uk)
  • antithrombin alfa increases toxicity of collagenase clostridium histolyticum by anticoagulation. (medscape.com)
  • Scroll down for Crescent's line of Nordmark Collagenase NB and Product Notes. (creschem.com)
  • Collagenase is used to break down scar tissue and promote the natural healing process, resulting in a more youthful and rejuvenated appearance. (chopraplasticsurgery.com)
  • Collagenase is used in plastic surgery to help break down and remove scar tissue, particularly in cases of contracture or tightness. (chopraplasticsurgery.com)
  • Dr. Karan Chopra, a board-certified plastic and reconstructive surgeon, is known for his expertise in utilizing collagenase to achieve natural-looking results for his patients. (chopraplasticsurgery.com)
  • Dr. Karan Chopra's patients have reported high levels of satisfaction with the results achieved through the use of collagenase, contributing to his exceptional reputation in the field. (chopraplasticsurgery.com)
  • His artistic hand, combined with the use of collagenase, allows him to achieve results that are tailored to each patient's unique needs and desires. (chopraplasticsurgery.com)
  • Experience the benefits of collagenase and discover the natural-looking results you've always desired. (chopraplasticsurgery.com)