The pathological destruction of collagen plays a key role in the development of inflammatory disease states affecting every organ system in the human body. Neutrophils localized at inflammatory sites can potentially degrade collagen by releasing a metalloenzyme, collagenase, which is stored in a latent inactive form. Triggered human neutrophils were shown to release and simultaneously activate their latent collagenase. The activation of the latent enzyme was coupled to an oxidative process that required the generation of a highly reactive oxygen metabolite, hypochlorous acid. Oxidative regulation of latent collagenase activity may be important in the pathogenesis of connective tissue damage in vivo.. ...
The human tissue inhibitor of metalloproteinases (TIMP) is a glycoprotein with a molecular weight of 28,000. It appears to be ubiquitous in human mesoderm tissues and has previously been shown to be identical to the collagenase inhibitor isolated from human skin fibroblasts. TIMP inhibits type I- and IV-specific collagenases and other neutral metalloen-doproteinases that may be responsible for the degradation of extracellular matrix in tumor cell metastasis. In this work we have utilized recombinant human TIMP (rTIMP) obtained by expression of its cDNA gene (Carmichael et al., Proc. Natl. Acad. Sci. USA, 83: 2407, 1986). The rTIMP is shown to have similar inhibition properties as natural TIMP against human skin fibroblast collagenase. In an in vitro amnion invasion assay system, rTIMP inhibited the invasion of B16-F10 murine melanoma cells through the human amniotic membrane at an identical concentration to that reported previously for natural TIMP. The mechanism by which rTIMP inhibits amniotic ...
Collagenase Inhibitor I - Calbiochem The Collagenase Inhibitor I controls the biological activity of Collagenase. This small molecule/inhibitor is primarily used for Protease Inhibitors applications. - Find MSDS or SDS, a COA, data sheets and more information.
TY - JOUR. T1 - Antitumor effect of pingyangmycin in combination with monoclonal antibody 3G11 directed against type IV collagenase. AU - Liu, Xiu Jun. AU - Ouyang, Zhi Gang. AU - Dai, Yao. AU - Liu, Xiao Yun. AU - Zhen, Yong Su. PY - 2007/2. Y1 - 2007/2. N2 - Objective: To study the antitumor effects of the combination of pingyangmycin (PYM) and monoclonal antibody(mAb) 3G11 directed against type IV collagenase. Methods: Immunoreactivity of mAb 3G11 to type IV collagenase and various tumor cells was determined by ELISA and the cytotoxicity of PYM and PYM plus 3G11 was examined by MTT assay. Antitumor effects in vivo were evaluated by using subcutaneously transplanted hepatoma 22 tumor model in mice. Results: mAb 3G11 showed immunoreactivity to type IV collagenase, mouse hepatoma 22 (H22) cells, human hepatoma HepG2 cells, and human prostatic carcinoma DU145 cells. As compared with free PYM, PYM plus 3G11 showed stronger cytotoxicity to these tumor cells. Synergetic effect was found at a certain ...
The mechanisms involved in retinoic acid (RA)-mediated regulation of the collagenase gene in a rabbit synovial fibroblast cell line (HIG82) were investigated. When HIG82 cells are cotransfected with expression vectors containing cDNAs for retinoic acid receptor (RAR) α1, β2, or γ1 and collagenase promoter-driven CAT reporter constructs, only RAR-γ1 represses basal CAT expression upon RA treatment, while RAR-α1, β2, and γ1 all suppress phorbol-induced CAT expression. Thus, transcriptional regulation of collagenase by RA is mediated by RARs in an RAR-type specific manner. Using mutatlonal and deletional analysis, we find that interaction between elements within 182 bp collagenase promoter plays an important role in this process. In addition, cotreatment with RA results in a decrease of phorbol-induced mRNA levels of fos and jun, and binding of nuclear proteins to an AP-1 oligonucleotide. Furthermore, RA-induced nuclear protein(s) specifically bind to a 22 bp sequence (−182 to −161) of the
72 kDa Type IV Collagenase (Matrix Metalloproteinase 2 or Gelatinase A or Neutrophil Gelatinase or 72 kDa Gelatinase or TBE 1 or MMP2 or EC 3.4.24.24) - Pipeline Review, H2 2017 with 46 pages available at USD 3500 for single User PDF at ReportsWeb research database.
1FBL: Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller.
Collagenase, Lyophilized Powder, 50 mg [BM-5030-50MG] - Collagenase consists of a blend of enzymes including collagenase, caseinase, clostripain and trypsin designed to effectively hydrolyze collagen and dissociate tissues. Various collagenase products have been evaluated specifically for use with Advanced BioMatrix s collagen products. This product is offered to improve the viability and functionality of isolated cells from the
[Video] Subculture of hESCs by Collagenase IV - posted in Stem Cell: Name: Subculture of hESCs by Collagenase IV Category: Stem CellsDate Added: 24 July 2013 - 10:23 PMSubmitter: bioforumShort Description: None ProvidedView Video
Worthington Collagenase Vial, NCIS [WLK003245-5VI] - UNSPSC Code(s):12352204≥500 units per mg dry weightA component of the NCIS kit. This material is 0.22 micron membrane filtered and lyophilized in autoclaved vials. A vial reconstituted with 5 ml of HBSS or equivalent yields a solution of 300 units/ml of collagenase, Code: CLSPA. Suitable for cell
Protease capable of digesting collagen fibrils. Contains high levels of collagenase and caseinase activity. Produced using animal component-free materials.
Table of Contents. Table of Contents 2. List of Tables 5. List of Figures 5. Introduction 6. Global Markets Direct Report Coverage 6. Matrix Metalloproteinase 9 (Gelatinase B or 92 kDa Type IV Collagenase or 92 kDa Gelatinase or MMP9 or EC 3.4.24.35) Overview 7. Therapeutics Development 8. Matrix Metalloproteinase 9 (Gelatinase B or 92 kDa Type IV Collagenase or 92 kDa Gelatinase or MMP9 or EC 3.4.24.35)-Products under Development by Stage of Development 8. Matrix Metalloproteinase 9 (Gelatinase B or 92 kDa Type IV Collagenase or 92 kDa Gelatinase or MMP9 or EC 3.4.24.35)-Products under Development by Therapy Area 9. Matrix Metalloproteinase 9 (Gelatinase B or 92 kDa Type IV Collagenase or 92 kDa Gelatinase or MMP9 or EC 3.4.24.35)-Products under Development by Indication 10. Matrix Metalloproteinase 9 (Gelatinase B or 92 kDa Type IV Collagenase or 92 kDa Gelatinase or MMP9 or EC 3.4.24.35)-Pipeline Products Glance 12. Late Stage Products 12. Early Stage Products 13. Matrix Metalloproteinase 9 ...
TY - JOUR. T1 - Enhancement of the structural stability of full-length clostridial collagenase by calcium ions. AU - Ohbayashi, Naomi. AU - Yamagata, Noriko. AU - Goto, Masafumi. AU - Watanabe, Kimiko. AU - Yamagata, Youhei. AU - Murayama, Kazutaka. PY - 2012/8. Y1 - 2012/8. N2 - The clostridial collagenases G and H are multidomain proteins. For collagen digestion, the domain arrangement is likely to play an important role in collagen binding and hydrolysis. In this study, the full-length collagenase H protein from Clostridium histolyticum was expressed in Escherichia coli and purified. The N-terminal amino acid of the purified protein was Ala31. The expressed protein showed enzymatic activity against azocoll as a substrate. To investigate the role of Ca2+ in providing structural stability to the full-length collagenase H, biophysical measurements were conducted using the recombinant protein. Size exclusion chromatography revealed that the Ca2+ chelation by EGTA induced interdomain ...
Neutrophil collagenase (EC 3.4.24.34, matrix metalloproteinase 8, PMNL collagenase, MMP-8) is an enzyme. This enzyme catalyses the following chemical reaction Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, interstitial collagenase, this enzyme cleaves type III collagen more slowly than type I This enzyme belongs to the peptidase family M10. Collagenase Hasty, K. (1987). "A., Jeffrey, J. J., Hibbs, M. S. and Welgus, H. G. The collagen substrate specificity of human neutrophil collagenase". J. Biol. Chem. 262 (21): 10048-10052. PMID 3038863. Hasty, K. (1990). "A., Pourmotabbed, T. F., Goldberg, G. I., Thompson, J. P., Spinella, D. G., Stevens, R. M. and Mainardi, C. L. Human Neutrophil Collagenase. A distinct gene product with homology to other matrix metalloproteinases". J. Biol. Chem. 265 (20): 11421-11424. PMID 2164002. Knäuper, V.; Krämer, S.; Reinke, H.; Tschesche, H. (1990). "Characterization and activation of procollagenase from human ...
Our most active crude collagenase, type XI, contains significant activities of other proteolytic enzymes, including clostripain, caseinase, and a tryptic activity. While this product is highly suited for preparation of pancreatic islets and islet cells, the tryptic activity of the collagenase medium can activate the zymogens of the digestive enzymes produced by pancreatic acinar cells. The addition of trypsin inhibitor to the culture medium from Clostridium histolyticum prevents or greatly reduces the activation of the protease proenzymes stored in the pancreas.
Using SANTYL COLLAGENASE OINTMENT 250UNITS/GM during pregnancy may raise the risk of children developing some disorder (commpon for some such kind of drugs), however it depends upon how SANTYL COLLAGENASE OINTMENT 250UNITS/GM ingredients pass through placenta and may have effect on baby - Strength of SANTYL COLLAGENASE OINTMENT 250UNITS/GM is major factor in determination of such side effects, The possible danger in pregnancy are under research. BIOMED, S.L. Canada publish leaflet about SANTYL COLLAGENASE OINTMENT 250UNITS/GM every update to describe possible risks of using SANTYL COLLAGENASE OINTMENT 250UNITS/GM side effect in pregnancy and pregnant women. You may download BIOMED, S.L. issued leaflet regarding side effects of SANTYL COLLAGENASE OINTMENT 250UNITS/GM - COLLAGENASE. Pregnancy Side Effects can be easily know by Atc code of SANTYL COLLAGENASE OINTMENT 250UNITS/GM ATC CODE.. ...
Purpose: Collagenase could be considered as a method for generating animal model of keratoconus. The authors aimed to evaluate the impact of collagenase on the interlamellar cohesive force of rabbit corneas.. Methods: 20 post mortem New Zealand white rabbit corneas were divided into 4 groups: group 1(15 mg/ml collagenase type II with 15% dextran, N=5), group 2(10 mg/ml collagenase type II with 15% dextran, N=5),group 3(5 mg/ml collagenase type II with 15% dextran, N=5) and group 4(the control group,15% dextran, N=5). After removing epithelium and measuring the corneal thickness, 9*4mm corneal strips were incised and interlamellar cohesive force at 50% depth of stroma was measured with a microcomputer-controlled biomaterial testing machine.. Results: The mean interlamellar cohesive force of group 1,group 2,group 3 and group 4 was 0.225 N/mm,0.217 N/mm,0.199 N/mm,and 0.211 N/mm respectively; without statistically significant differences. Light microscopy showed stromal tissue became less tight ...
The early stages of degradation of native collagen by two bacterial collagenases were studied by electron microscopy and by automatic Edman degradation. The purified collagenase from Clostridium histolyticum was shown to cleave native collagen at several sites, but not progressively from the N-terminus, as had been previously suggested. The homogeneous collagenase from Achromobacter iophagus cleaves native collagen preferentially at two sites corresponding to the interbands 33-34 and 41-42. The latter lies within the region cleaved by the eukaryotic collagenases. ...
H-ras transformed human bronchial epithelial cells (TBE-1) secrete a single major extracellular matrix metalloprotease which is not found in the normal parental cells. The enzyme is secreted in a latent form which can be activated to catalyze the cleavage of the basement membrane macromolecule type IV collagen. The substrates in their order of preference are: gelatin, type IV collagen, type V collagen, fibronectin, and type VII collagen; but the enzyme does not cleave the interstitial collagens or laminin. This protease is identical to gelatinase isolated from normal human skin explants, normal human skin fibroblasts, and SV40-transformed human lung fibroblasts. Based on this ability to initiate the degradation of type IV collagen in a pepsin-resistant portion of the molecule, it will be referred to as type IV collagenase. This enzyme is most likely the human analog of type IV collagenase detected in several rodent tumors. Type IV collagenase consists of three domains. Type IV collagenase ...
Aims: To test whether the immersion of the pancreas in solutions of 1 or 2 mg/mL of collagenase in 4°C for 24 hours, for the isolation of Langerhans islets, rises the yield of islets/grams of pancreatic tissue. Methods: Experimental study with mouses, performed in the Laboratory of Nephrology of the Instituto de Pesquisas Biológicas do Hospital São Lucas da PUCRS, Porto Alegre, RS. After the animals have been sacrified under anesthesia, the pancreas were removed and divided in four groups, according the technique used for isolating the islets. A) collagenase 1mg/mL, in 4ºC for 24 hours and heating for 39ºC for 15 minutes. B) collagenase 2mg/mL with the same previous described steps. C) collagenase 1mg/mL and heating of the solution in the same day, in 39ºC for 15 minutes. D) collagenase 2mg/mL and heating of the solution in the same day, in 39ºC for 15 minutes. We verified the viability of the islet through the trypan blue test. Results: The median numbers of isolated islets in the groups ...
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Effect of topical application of the collagenase IV inhibitor, SB-3CT, on hair regrowth.Notes: After 5, 15, and 25 days treatment, typical photos of dorsal skin
The trial aims to investigate the safety and tolerability of acute intracoronary injected collagenase in patients with chronic total coronary artery occlusions
1JAQ: X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design.
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MATRIX DEGRADING PROTEINASES FROM HUMAN-GRANULOCYTES - TYPE-I, TYPE-II, TYPE-III COLLAGENASE, GELATINASE AND TYPE-IV, TYPE-V-COLLAGENASE - A SURVEY OF RECENT FINDINGS AND INHIBITION BY GAMMA-ANTICOLLAGENASE ...
We examined the effects of IGF 1 around the collagenolytic action of DU145 cells utilizing gelatin MAPK 阻害剤 zymography that is an incredibly delicate technique
XIAFLEX (Collagenase clostridium histolyticum) drug information & product resources from MPR including dosage information, educational materials, & patient assistance.
Learn about Xiaflex (Collagenase Clostridium Histolyticum) may treat, uses, dosage, side effects, drug interactions, warnings, patient labeling, reviews, and related medications.
This pilot study evaluates the safety and tolerability of a single injection of collagenase enzyme directly into a uterine fibroid in subjects already selected
We previously advanced the hypothesis that a highly regulated balance of synthesis and degradation determines collagen content in the fibrous cap of atherosclerotic plaques.1,2 In turn, collagen levels critically influence the integrity of the plaques cap, a structure whose biomechanical failure may cause most myocardial infarctions. Earlier indirect evidence suggested that collagenases of the MMP family can regulate collagen content in the plaque.5-12 We initially demonstrated overexpression of the prototypical interstitial collagenase MMP-1 in human atheromata5 and later showed colocalization of MMP-1/collagenase-1 and MMP-13/collagenase-3 with degraded collagen in these lesions as detected by an antibody specific for the collagenase cleavage site of collagen.9 Recently, our group showed that human atheromata contain a third interstitial collagenase, MMP-8/collagenase-2,11 also present in mouse atheromata, as shown here (Figure 2C). Shah et al32 reported that conditioned media of cultured ...
OBJECTIVES: I. Compare the safety and efficacy of clostridial collagenase vs placebo in terms of improving the degree of flexion deformity, range of finger motion, and grip strength in patients with residual stage Dupuytrens disease.. II. Compare the overall clinical success rate, time to return to normal finger contracture to within 0-5 degrees of normal (zero degrees), and frequency of cord rupture in the joint of patients treated with these regimens.. III. Compare the baseline change in degree of finger flexion deformity, range of motion of the treated finger, and strength of hand grip (in pounds) in patients treated with these regimens.. IV. Compare the frequency distribution of the number of patients with reduction in finger contracture to within 0-5 degrees of normal (zero degrees) and the number who require re-treatment with open-label collagenase after treatment with these regimens. ...
[119 Pages Report] Check for Discount on Global (North America, Europe and Asia-Pacific, South America, Middle East and Africa) Collagenase Market 2017 Forecast to 2022 report by Global Info Research. Collagenase, obtained from Clostridium histolyticum, is an enzyme used for...
WASHINGTON -- The FDA has approved the first drug for the progressive hand disease known as Dupuytrens contracture -- the injectable collagenase clostridium histolyticum (Xiaflex).
Auxilium Pharmaceutical, manufacturer of Xiaflex collagenase injections, boasts that in a two-year study Xiaflex had a recurrence rate of 19.3 percent, a considerably lower rate of return than those who used surgical procedures to treat their hand problem.. The answer to the question "Is the Xiaflex recurrence rate for Dupuytren low?" is a qualified yes and no.. Yes, Xiaflex or collagenase treatment results in a considerably lower Dupuytren recurrence rate than hand surgery. However, this does not necessarily mean that the rate of recurrence is actually low; it only means the problem will come back slower than what happens after invasive hand surgery. The reality is that hand surgery has a tremendously high recurrence rate, so a non-surgical therapy option by comparison will look favorable.. Every child learns that pointing to someone who has done something worse than you does not diminish his crime. When you told your mother that the child next door stole 25 cents from his mother, you were ...
A soft agarose clonogenic assay is presented which has been optimized for the growth of human gastrointestinal adenocarcinomas. Samples from 15 gastric and colonic solid tumors and from 2 noncancerous stomachs (control cultures) were disaggregated by treatment with collagenase at 37° overnight. Colonies appeared 10 to 15 days after plating, with a cloning efficiency between 0 and 0.82%, which was markedly improved by a fibroblastic feeder layer. The results suggest a correlation between cloning efficiency and the degree of differentiation of the initial tumor. Histochemistry, electron microscopy, and a carcinoembryonic antigen immunofluorescence assay showed that the colonies consisted of cells with the same characteristics as those of the original tumor. This colony formation assay appears to be potentially useful for assessing the stem cell pool of gastrointestinal tumors. It will be valuable for studying their response to chemotherapeutic agents in vitro. This clonogenic assay may also ...
An extracellular endopeptidase of vertebrate tissues homologous with interstitial collagenase. Digests proteoglycan, fibronectin, collagen types III, IV, V, IX, and activates procollagenase. In peptidase family M10 (interstitial collagenase family ...
Santyl Collagenase is an enzymatic debrider. CLAIMED BENEFITS: It actively and selectively removes necrotic tissue without harming granulation tissue. INTENDED USE: indicated for ...
Neutrophil collagenase, also known as matrix metalloproteinase-8 (MMP-8) or PMNL collagenase (MNL-CL), is a collagen cleaving enzyme which is present in the connective tissue of most mammals. In humans, the MMP-8 protein is encoded by the MMP8 gene. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is stored in secondary granules within neutrophils and is activated by autolytic cleavage. Its function is degradation of type I, II and III collagens. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. GRCh38: Ensembl release 89: ENSG00000118113 - Ensembl, May 2017 GRCm38: Ensembl release 89: ...
The Secondary Outcome Measure for participants who were enrolled at Step1 through Step2 and treated with AK160 is the time to first achieve and maintain clinical success after the last injection where clinical success was defined as reduction in the contracture of the first treated joint to 5° or less. The injection was allowed up to 3 times ...
This enzyme is synthesized as a proenzyme of 53 kDa that is converted to an active form of 22 kDa. cDNA sequences have been obtained for the mouse [3] and human [4] enzymes. In peptidase family M10 (interstitial collagenase family ...
Optimum Nutrition Amino Energy Plus UC-II Collagen offers a combination of 5g of Amino Acids, 100 mg of Caffeine, and UC-II Collagen. Joint Support.
We studied the in vivo effect of long-term doxycycline treatment combined with NSAID on human interstitial collagenases, other matrix metalloproteinases, serine proteinases, tissue inhibitor of matrix metalloproteinase-l (TIMP-1) and lactoferrin from saliva and serum during the course of acute reactive arthritis (ReA). Collagenase activity and serine proteases (elastase-like, cathepsin G-like and trypsin-like activities) of saliva (n = 10) and gelatinase, lactoferrin and TIMP-1 of saliva (E = 10) and serum (n = 10) samples before and after 2 months doxycycline treatment, combined with NSAID, were studied by quantitative SDS-PAGE assay, ELISA assay and by spectrophotometric assay. The cellular source and molecular forms of salivary collagenase were characterized by immunoblotting using specific antisera. We found that activities of total and endogenously active interstitial collagenase reduced significantly. The salivary collagenase was found to originate from neutrophils. No fragmentation of ...
BACKGROUND: 72 Kilodalton (kd) type IV collagenase is a matrix metalloproteinase that specifically cleaves type IV collagen molecules. The enzyme has been postulated to have an important role in the invasion and spread of malignant tumors. EXPERIMENTAL DESIGN: In situ hybridization was used to study the expression of the 72 kd type IV collagenase mRNA in 24 benign, 2 semimalignant, and 15 malignant ovarian tumors and in 5 metastases of ovarian serous adenocarcinomas. The results were correlated with the expression of the mRNA for the alpha 1(IV) chain of type IV collagen and with the corresponding immunohistochemical distribution of the enzyme. RESULTS: The results showed that the more malignant an ovarian tumor was, the more clearly mRNA expressions for both 72 kd type IV collagenase and the alpha 1(IV) chain could be detected in tumor cells. The expression of both types of mRNAs was localized within the cells of tumor stroma and occurred mainly in fibroblasts and vascular endothelial cells. ...
DupuytrEn Treatment EffeCtiveness Trial (DETECT): a protocol for prospective, randomised, controlled, outcome assessor-blinded, three-armed parallel 1:1:1, multicentre trial comparing the effectiveness and cost of collagenase clostridium histolyticum, percutaneous needle fasciotomy and limited fasciectomy as short-term and long-term treatment strategies in Dupuytrens ...
Interactions between C1q and collagen are thought to be due to the similarity in the structure of collagen and part of C1q. In the present paper immunological and biochemical aspects of this similarity were explored. It was found that one of nine rabbit anticollagen sera studied showed a clearcut reactivity with C1q, while anticollagenantibody-positive sera and synovial fluids of patients with rheumatoid arthritis did not display any cross-reactivity with C1q. Eleven of twenty collagen-immunized guinea pigs, however, demonstrated cellular cross-reactivity with CLF, the collagen-like fragment of C1q. Gel filtration studies indicated the formation of complexes between CLF and collagen, simulating immunological inhibition of anti-C1q-antibody by collagen. Human RA synovial collagenase was found capable of splitting C1q at a position within its collagen-like fragment. The importance of the interactions between collagen and C1q for the pathological events characterizing RA is discussed.
Results were expressed as amplitude of peak cur rents evoked by ,meATP or as current density, defined as the ratio of peak amplitude over membrane capacitance. For measuring recovery, the amplitude of the third P2X3 response was compared to the first and expressed as a percentage. they The results obtained after 2 h drug incubation Inhibitors,Modulators,Libraries were always compared to those obtained after 2 h incubation in culturing media containing DMSO. Membrane capacitance and series resistance were measured through the peak amplitude and decay constant of transients induced by repetitive depolarizing pulses of 10 mV. Voltage clamp and macropatch recordings in Xenopus oocytes Oocytes were surgically removed from Tricaine anesthe tized female Xenopus laevis frogs and were incubated in OR2 solution containing 1 2 mgml type IA collagenase at room temperature for 2 h under agitation.. Stage V and VI oocytes were then manually defolliculated before nuclear or cytoplasmic microinjection of ...
Heptachlor, a chlorinated hydrocarbon pesticide, suppresses the production of progesterone and estradiol in the female rat in vivo or in isolated ovaries in vitro. In this study the effect of heptachlor on steroid hormone production by isolated rat luteal and follicular cells, in the presence of two precursor hormones was investigated. Ovaries were isolated from anesthetized mature normocyclic virgin rats (3 to 4 months old), under sterile conditions. Corpora lutea and follicles were microscopically dissected out and separately enzymatically dispersed with collagenase at 37 degrees C. Viable cells collected after centrifugation were used at a concentration of approximately 2.5 x 10(5) cells/10 mL. Both luteal and follicular cell preparations were separately incubated overnight (15 h) at 37 degrees C in the presence of pregnenolone (P5) and androstenedione (A4) at a concentration of 6.0 nmol/L each, and heptachlor at either 0.12 microg/mL (low dose) or 1.20 microg/mL (high dose) (test cells) or ...
BioAssay record AID 208335 submitted by ChEMBL: Tested for inhibition of stromelysin using [3H]transferrin, following pre-incubation with prostromelysin for 0 hr prior to activation by plasmin.