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1دورية أكاديمية
المؤلفون: Tarangini Sathyamoorthy, Gurjinder Sandhu, Liku B. Tezera, Richard Thomas, Akul Singhania, Christopher H. Woelk, Borislav D. Dimitrov, Dan Agranoff, Carlton A. Evans, Jon S. Friedland, Paul Elkington
مصطلحات موضوعية: Tuberculosis, Infectious Diseases, FOS Health sciences, Medicine, Health Sciences, Epidemiology and Pathogenesis of Pneumocystis Pneumonia, Epidemiology, Diagnosis and Treatment of Spinal Infections, Surgery, Diagnosis, Matrilysin, Matrix metalloproteinase, Internal medicine, Pathogenesis, Body mass index, Case-control study, Gelatinase, Immunology, FOS Clinical medicine, Gelatinase A, Gastroenterology, Pathology
الوصف: Tuberculosis (TB) remains a global health pandemic and greater understanding of underlying pathogenesis is required to develop novel therapeutic and diagnostic approaches. Matrix metalloproteinases (MMPs) are emerging as key effectors of tissue destruction in TB but have not been comprehensively studied in plasma, nor have gender differences been investigated. We measured the plasma concentrations of MMPs in a carefully characterised, prospectively recruited clinical cohort of 380 individuals. The collagenases, MMP-1 and MMP-8, were elevated in plasma of patients with pulmonary TB relative to healthy controls, and MMP-7 (matrilysin) and MMP-9 (gelatinase B) were also increased. MMP-8 was TB-specific (p<0.001), not being elevated in symptomatic controls (symptoms suspicious of TB but active disease excluded). Plasma MMP-8 concentrations inversely correlated with body mass index. Plasma MMP-8 concentration was 1.51-fold higher in males than females with TB (p<0.05) and this difference was not due to ... : لا يزال السل (TB) جائحة صحية عالمية ويلزم فهم أكبر للأمراض الكامنة لتطوير مناهج علاجية وتشخيصية جديدة. تظهر البروتينات الفلزية المصفوفية (MMPs) كمؤثرات رئيسية لتدمير الأنسجة في السل ولكن لم يتم دراستها بشكل شامل في البلازما، ولم يتم التحقيق في الاختلافات بين الجنسين. قمنا بقياس تركيزات البلازما من MMPs في مجموعة سريرية محددة بعناية ومستقبلية من 380 فردًا. تم رفع إنزيمات الكولاجين، MMP -1 و MMP -8، في بلازما المرضى الذين يعانون من السل الرئوي بالنسبة للضوابط الصحية، كما تم زيادة MMP -7 (matrilysin) و MMP -9 (الجيلاتيناز B). كان MMP -8 خاصًا بالسل (p<0.001)، ولم يرتفع في ضوابط الأعراض (الأعراض المشبوهة بالسل ولكن تم استبعاد المرض النشط). ترتبط تركيزات البلازما MMP -8 عكسيًا بمؤشر كتلة الجسم. كان تركيز MMP -8 في البلازما أعلى بمقدار 1.51مرة في الذكور مقارنة بالإناث المصابات بالسل (p<0.05) ولم يكن هذا الاختلاف بسبب شدة المرض الأكبر لدى الرجال. أظهر التحليل الخاص بنوع الجنس لـ MMPs زيادة ثابتة في MMP -1 و -8 في السل، لكن MMP -8 كان تمييزًا أفضل للسل عند الرجال. ترتفع الكولاجينات البلازمية في السل الرئوي ...
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2
المؤلفون: Kevin L. Dreher, Rick H. Jaskot, Wei Yi Su
المصدر: Inhalation toxicology. 12
مصطلحات موضوعية: medicine.diagnostic_test, Chemistry, Health, Toxicology and Mutagenesis, Gelatinase A, Lung injury, Tissue inhibitor of metalloproteinase, Matrix metalloproteinase, Toxicology, Molecular biology, Type IV collagen, Western blot, Biochemistry, Gene expression, medicine, Matrilysin
الوصف: Gelatinase A and gelatinase B are matrix metalloproteinases (MMPs) that are capable of degrading type IV collagen as well as other major components of basement membranes. These MMPs are also involved in modulating inflammation and tissue remodeling. Previous studies have shown the induction of pulmonary matrilysin, another MMP, following exposure to either combustion or ambient particulate matter (PM). In the present study, we examined whether gelatinase A, gelatinase B, or tissue inhibitor of metalloproteinase (TIMP) was affected following exposure to PM. Sprague-Dawley rats were exposed to a combustion PM (residual oil fly ash, ROTA, 2.5 mg/rat) or saline by intratracheal instillation and examined at 6 to 72 h postexposure. Changes in gelatinase A, gelatinase B, and TIMP-1 and -2 m RNA levels were determined using reverse transcription (RT) polymerase chain reaction (PCR). ROTA exposure increased the mRNA levels of gelatinase A and TIMP-1. However, gelatinase B mRNA, not expressed in control animals, was significantly induced from 6 to 24 h following ROFA exposure. Western blot analysis confirmed the presence of gelatinase A and B protein in lung tissue following ROFA exposure. Immunocytochemical analysis revealed that alveolar epithelial cells and inflammatory cells were major cellular sources for the pulmonary gelatinase A and B expression. To compare the effects of ambient PM with that of combustion PM and to further examine effects of ambient PM size on MMP induction, animals were treated with the same dose of the size-fractionated ambient PM [PM1.7, PM1.7-3.7, PM37.20 (size indicated in micrometers) collected from Washington, DC], Gelatinase A, gelatinase B, and TIMP gene expression and cellular distributions were assessed using RT-PCR and immunocytochemistry, respectively. Interestingly, gelatinase B was significantly induced to the same extent by all three size-fractionated ambient PM. Celatinase A and TIMP-1 expression were not changed, while TIMP-2 expression was slightly decreased by PM1.7 and PM1.7-3.7. Immunocytochemically, gelatinase A, gelatinase B, and TIMP-2 expression were localized mainly to the terminal bronchiole region and associated with inflammatory cells in ambient PM exposed animals. Thus, we have provided further evidence that MMP and TIMP expression are altered following exposure to either combustion or ambient PM supporting the hypothesis that MMP may be involved in pathogenesis of PM-induced lung injury.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1fe45fdf268e34962cfb958a6fa28accTest
https://pubmed.ncbi.nlm.nih.gov/26368525Test -
3
المؤلفون: Naohiko Koshikawa, Shouichi Higashi, Kiyohide Fujita, Kaoru Miyazaki, Kazuhiro Yamamoto, Mitomu Kioi
المصدر: Oncogene. 22:8662-8670
مصطلحات موضوعية: Cancer Research, Gelatinase A, Cell, Mice, Nude, Matrix metalloproteinase, Biology, Cell membrane, Mice, Nude mouse, Cell Line, Tumor, Cell Adhesion, Genetics, medicine, Animals, Humans, Neoplasm Metastasis, Matrilysin, Molecular Biology, Cell Aggregation, Mice, Inbred BALB C, Cadherins, biology.organism_classification, Cell aggregation, medicine.anatomical_structure, Cell culture, Matrix Metalloproteinase 7, Colonic Neoplasms, Immunology, Cancer research
الوصف: Matrilysin (MMP-7) is thought to contribute to invasive growth and metastasis of colon carcinoma and many other human cancers. The present study demonstrates that treatment of human colon carcinoma cells with active matrilysin induces cell aggregation in vitro and promotes liver metastasis in nude mice. When two kinds of colon carcinoma cell lines were incubated with active matrilysin, this enzyme efficiently bound to the cell surface and induced loose cell aggregation, which led to E-cadherin-mediated tight cell aggregation. Synthetic MMP inhibitors inhibited both the membrane binding of matrilysin and matrilysin-induced cell aggregation, while TIMP-2 inhibited only the cell aggregation. Two other active MMPs, stromelysin and gelatinase A, neither bound to cell membrane nor induced cell aggregation. Tumor cells in loose cell aggregates could reaggregate even after they were freed from matrilysin and dispersed. When injected into the spleen of nude mice, the tumor cells in the stable aggregates produced much larger metastatic nodules in the livers than control cells and those in the loose aggregates. These results suggest that matrilysin may enhance metastatic potential of tumor cells by processing a cell surface protein(s) and thereby inducing loose and then tight aggregation of tumor cells.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bdfe6fb10afd737b171261f2ccf27fbTest
https://doi.org/10.1038/sj.onc.1207181Test -
4
المؤلفون: Pierre Vabres, Bernard Pellat, Myriam Dridi, Gaston Godeau, Mireille Bonnefoix, Pierre Yves Venencie, Bruno Gogly, Sabah Ghomrasseni
المصدر: The American Journal of Dermatopathology. 24:118-129
مصطلحات موضوعية: Adult, Male, Pathology, medicine.medical_specialty, Adolescent, Cell Survival, Biopsy, Anetoderma, Gelatinase A, Dermatology, Matrix metalloproteinase, Skin Diseases, Stromelysin 1, Pathology and Forensic Medicine, Image Processing, Computer-Assisted, medicine, Humans, Matrilysin, Child, Cells, Cultured, Tissue Inhibitor of Metalloproteinase-2, Tissue Inhibitor of Metalloproteinase-1, integumentary system, biology, Chemistry, General Medicine, Elastic Tissue, medicine.disease, Matrix Metalloproteinases, Extracellular Matrix, medicine.anatomical_structure, Collagenase, biology.protein, Electrophoresis, Polyacrylamide Gel, Female, Elastin, Elastic fiber, medicine.drug
الوصف: The amount of elastic fibers from lesional and healthy skin areas of five patients with anetoderma was determined by automated image analysis. Dermal elastic fibers were almost completely absent in anetodermic skin and preelastic fibers were undetectable or extremely rare. Organ cultures were performed using explants from affected and unaffected skin areas of the same patient. We identified and quantified proteases in the culture media of explants: MMP-1 (collagenase 1), MMP-2 and MMP-9 (gelatinases A and B), MMP-3 (stromelysin 1), MMP-7 (matrilysin 1), and tissue inhibitors of metalloproteinases, TIMP-1 and TIMP-2. The data were compared with those of two healthy donors. For the five samples of anetodermic skin, MMP-1 levels were significantly higher compared with the uninvolved cultures and the two healthy samples. A significant increase of TIMP-1 expression was also observed in the affected cultures. We demonstrated a significant increase in the production of gelatinase A in lesional skin when compared with nonlesional skin and healthy donor samples. We found no significant production of TIMP-2 in the five samples of anetodermic skin compared with the samples from the two healthy donors. There was a significant decrease in TIMP-2 expression in the five nonlesional samples compared with the control samples. These data are in favor of an altered balance in anetodermic patients between MMP-2 and TIMP-2. Levels of MMP-9, MMP-3, and MMP-7 were significantly higher in the culture-conditioned media of the anetodermic skin samples than the nonlesional skin cultures. Because MMP-3, MMP-7, MMP-9 are known to degrade elastin, and MMP-3 can activate the latent forms of MMP-7 and MMP-9, we propose that these metalloproteinases also participate in the degradation of elastic fibers in anetodermic skin.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba3314b2a52afd4c6aab14c5392d3382Test
https://doi.org/10.1097/00000372-200204000-00003Test -
5
المصدر: Journal of Orthopaedic Research. 19:642-649
مصطلحات موضوعية: Adult, Male, Pathology, medicine.medical_specialty, Anterior cruciate ligament, Gelatinase A, Biology, Matrix metalloproteinase, Gene Expression Regulation, Enzymologic, Stromelysin 1, Sex Factors, medicine, Humans, Orthopedics and Sports Medicine, RNA, Messenger, Anterior Cruciate Ligament, Matrilysin, Aged, DNA Primers, Aged, 80 and over, Metalloproteinase, Reverse Transcriptase Polymerase Chain Reaction, Anterior Cruciate Ligament Injuries, Tissue Inhibitor of Metalloproteinases, Middle Aged, musculoskeletal system, Molecular biology, Matrix Metalloproteinases, medicine.anatomical_structure, Collagenase, Ligament, Female, medicine.drug
الوصف: Women are more susceptible to anterior cruciate ligament (ACL) injuries than men performing similar athletic activities. Because tissue remodeling may affect ligament strength, we assessed expression of tissue remodeling effector genes in the human ACL. Specifically, we surveyed ACL for RNAs encoding all known matrix metalloproteases (MMPs) and tissue inhibitors of metalloproteases (TIMPs) by reverse transcription/polymerase chain reaction (RT-PCR). These experiments revealed that mRNAs encoding nine of sixteen MMPs and all four TIMPs are present in the normal ACL. The nine expressed proteases were MMPs 1-3, 7, 9, 11, 14, and 17 (collagenase 1, gelatinase A, stromelysin 1, matrilysin, gelatinase B, stromelysin 3, and membrane types 1 and 4, respectively), and MMP-18. Genes for MMPs 8, 10, 12, 13, 15, and 16 appeared not to be expressed in ACL, as their mRNAs were not detected using RT-PCR conditions that did yield positive signals from other tissues (testis or bone). We conclude that numerous genes encoding tissue remodeling effector proteins are expressedin the human ACL.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7afbb96dd065b49342c2a69f4fad471eTest
https://doi.org/10.1016/s0736-0266Test(00)00071-1 -
6
المؤلفون: Zhiwen Liu, Anna Ivanoff, Julius Klominek
المصدر: International Journal of Cancer. 91:638-643
مصطلحات موضوعية: Mesothelioma, Cancer Research, Pathology, medicine.medical_specialty, DNA, Complementary, Blotting, Western, Gelatinase A, Matrix metalloproteinase, Culture Media, Serum-Free, Substrate Specificity, Extracellular matrix, Matrix Metalloproteinase 10, Matrix Metalloproteinase 11, Laminin, Tumor Cells, Cultured, medicine, Humans, Neoplasm Invasiveness, Protease Inhibitors, Vitronectin, Matrilysin, Tissue Inhibitor of Metalloproteinase-3, Tissue Inhibitor of Metalloproteinase-2, Tissue Inhibitor of Metalloproteinase-1, biology, Reverse Transcriptase Polymerase Chain Reaction, Metalloendopeptidases, Molecular biology, Matrix Metalloproteinases, Fibronectins, Fibronectin, Matrix Metalloproteinase 9, Oncology, Cell culture, Matrix Metalloproteinase 7, biology.protein, Matrix Metalloproteinase 2, RNA, Matrix Metalloproteinase 3, Matrix Metalloproteinase 1
الوصف: The extracellular matrix metalloproteases (MMPs) secreted by various human tumor cells play a crucial role in tumor cell invasion and metastasis, but their expression in malignant mesothelioma (MM) cells has not been examined. In this study, we have investigated the spectrum of MMPs and tissue inhibitors of metalloproteases (TIMPs) produced by 8 MM cell lines. Using RT-PCR, we found that all investigated MM cell lines expressed genes encoding mRNA for MMP-1 (interstitial collagenase), MMP-2 (gelatinase A), MMP-3 (stromelysin-1), MMP-9 (gelatinase B) and TIMPs 1, 2 and 3. We also found that 6/8 MM cell lines expressed MMP-7 (matrilysin) and 3/8 MM cell lines expressed MMP-10 (stromelysin-2). MMP-11 (stromelysin-3) was not detected in any of the MM cell lines. Production of MMP-2 and MMP-9 was confirmed using gelatin zymography. In addition, all MM cell lines secreted a 66 kDa metalloprotease, while 3/8 MM cell lines secreted 46, 48, 51 and 63 kDa metalloproteases which specifically degraded the extracellular matrix components fibronectin, vitronectin and laminin. The 66 kDa protease was identified as MMP-3 by Western blot. Our results reveal a broad spectrum of MMPs and TIMPs produced by MM cells and indicate that different substrate specificities of MMPs may play a role in MM cell invasion.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b961b6e83695d16949e6fe128d2db12Test
https://doi.org/10.1002/1097-0215Test(200002)9999:9999<::aid-ijc1102>3.0.co;2-y -
7
المؤلفون: Donna E. Haynes-Johnson, Lekha Patel, Judy A. Lenhart, Stephen S. Palmer, Patricia Kraft, Zivin Robert
المصدر: Connective Tissue Research. 42:149-163
مصطلحات موضوعية: Collagen Type IV, medicine.medical_treatment, Proteolysis, Gelatinase A, Fluorescence Polarization, Peptide, Biochemistry, Substrate Specificity, Rheumatology, Cricetinae, medicine, Animals, Humans, Orthopedics and Sports Medicine, Matrilysin, Molecular Biology, chemistry.chemical_classification, Protease, medicine.diagnostic_test, biology, Cell Biology, Molecular biology, In vitro, Fibronectins, Fibronectin, Animals, Newborn, chemistry, Matrix Metalloproteinase 7, biology.protein, Matrix Metalloproteinase 2, Electrophoresis, Polyacrylamide Gel, Fluorescence anisotropy
الوصف: Matrilysin and gelatinase A are hypothesized to have significant roles in uterine and ovarian function. However, proteolytic activity assays for these enzymes are limited. We describe the development of simple and rapid assays for the proteolysis of fluorescein-labeled full-length substrates, collagen IV (Col-IV) and fibronectin (FN), and demonstrate the selectivity of matrilysin (MMP-7) compared to gelatinase A (MMP-2) for fibronectin. Changes in fluorescence intensity (FIU) and fluorescence polarization (mP) resulting from the protease activity of matrilysin and gelatinase A were measured. These studies show that the fluorescently labeled substrates, Col-IV and FN, are as reliable and amenable to rapid in vitro assay as peptide substrates. In addition, they are easier to use than previously described, non-fluorescent methods. The results demonstrate that assays using full-length, biological matrix proteins are more sensitive indicators of MMP-specific substrate activity than peptide based assays.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7d7bc6a7efd341309c3f5f5054f653aTest
https://doi.org/10.3109/03008200109014256Test -
8
المؤلفون: Hans-Peter Hartung, Hans-Walter Pfister, Uwe Koedel, Bernd C. Kieseier, Andrew J. H. Gearing, Robert Paul, T. Seifert, John M. Clements
المصدر: Brain. 122:1579-1587
مصطلحات موضوعية: Male, Pathology, medicine.medical_specialty, Transcription, Genetic, Gelatinase A, Meningitis, Meningococcal, Biology, Matrix metalloproteinase, medicine.disease_cause, Blood–brain barrier, Gene Expression Regulation, Enzymologic, Pathogenesis, chemistry.chemical_compound, Reference Values, Matrix Metalloproteinase 13, medicine, Animals, Humans, Collagenases, RNA, Messenger, Rats, Wistar, Matrilysin, Cerebrospinal Fluid, Evans Blue, Neisseria meningitidis, Metalloendopeptidases, medicine.disease, Rats, medicine.anatomical_structure, Matrix Metalloproteinase 9, chemistry, Blood-Brain Barrier, Gelatinases, Matrix Metalloproteinase 2, Matrix Metalloproteinase 3, Neurology (clinical), Meningitis
الوصف: Matrix metalloproteinases (MMPs) are implicated in the pathogenesis of various inflammatory diseases of the central nervous system. Evidence is accumulating that gelatinase B (MMP-9) might be involved in the pathogenesis of meningitis, but the spectrum of different MMPs involved in the inflammatory reaction of this disease has not been determined. We investigated the temporal and spatial mRNA expression pattern of gelatinase B in experimental meningococcal meningitis in rats. In contrast to controls, increased mRNA levels with peak values 6 h after injection with menigococci were found in brain specimens of the animals. Elevated MMP-9 mRNA expression was accompanied by enhanced proteolytic activity, as demonstrated by gelatin zymography, and positive immunoreactivity. The mRNA expression pattern of six other MMPs was investigated. Collagenase-3 and stromelysin-1 mRNAs were also found to be upregulated. In contrast, mRNA levels for gelatinase A, matrilysin, stromelysin-2 and stromelysin-3 remained unchanged. As evidenced by significantly increased intracranial pressure and by leakage of intravenously injected Evans blue through the blood vessel walls into the brain parenchyma, the animals injected with meningococci revealed signs of blood-brain barrier disruption. Augmented proteolytic activity of MMP-9 could also be demonstrated in CSF samples obtained from patients with bacterial meningitis, underlining the clinical relevance of our experimental findings. Our data indicate that gelatinase B, collagenase-3 and stromelysin-1 are selectively upregulated in bacterial meningitis and thus may contribute to the pathogenesis of this infectious disease of the central nervous system.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b7ac6d68e87ee0ba822490f3848ec30Test
https://doi.org/10.1093/brain/122.8.1579Test -
9
المؤلفون: Marlys H. Witte, Dennis Way, Linda C. Meade-Tollin
المصدر: Acta Histochemica. 101:305-316
مصطلحات موضوعية: Histology, Blotting, Western, Gelatinase A, Matrix metalloproteinase, Cell Line, Extracellular matrix, Western blot, Tumor Cells, Cultured, medicine, Animals, Humans, Collagenases, Matrilysin, Sarcoma, Kaposi, medicine.diagnostic_test, Chemistry, Caseins, Metalloendopeptidases, Cell Biology, General Medicine, Fibroblasts, Urokinase-Type Plasminogen Activator, Molecular biology, Rats, Molecular Weight, Matrix Metalloproteinase 9, Biochemistry, Gelatinases, Cell culture, Culture Media, Conditioned, Matrix Metalloproteinase 2, Interstitial collagenase, Matrix Metalloproteinase 3, Endothelium, Vascular, Matrix Metalloproteinase 1, Plasminogen activator
الوصف: Summary Kaposi's sarcoma (KS) cells are considered to be of endothelial origin. KS lesions are characterized by hyperproliferation and an invasive phenotype. We have determined that KS cell cultures constitutively secrete multiple forms of several matrix metalloproteinases (MMPs) and an altered form of urokinase plasminogen activator (u PA) by zymogram and Western analysis of the culture media. MMPs are a family of secreted endoproteinases which degrade components of the extracellular matrix. Their enhanced expression and activity are strongly correlated with cellular processes involving tissue remodeling and invasion. The KS cells secrete increased levels of gelatinase A and B and a high molecular weight u PA in vitro when compared with non- KS endothelial or epithelial cells. Multiple forms of gelatinases A and B were observed on gelatin zymograms. Caseinolytic bands observed were confirmed by Western blot analysis to be due to stromelysin activity, whereas matrilysin was not detected by casein zymography. Western blot analysis also detected secretion of interstitial collagenase and high molecular weight u PA. Gelatinolytic activity with the mobility of gelatinase B was detected on gelatin zymograms, but not by Western analysis. This unusual constitutive expression pattern of MMPs and u PA by KS cells in vitro is characterized by elevated levels of gelatinase A, gelatinase B, interstitial collagenase, stromelysin and a high molecular weight form of u PA, and the lack of expression of matrilysin. These secreted MMPs, taken together, are capable of digesting a broad range of components of the extracellular matrix. This unusual pattern is likely to contribute to the characteristic hyperproliferative and invasive phenotype of KS lesions.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fa059c28bce7a1d6dfc91f35c523ecaTest
https://doi.org/10.1016/s0065-1281Test(99)80031-2 -
10
المؤلفون: Charles L. Chaffin, Richard L. Stouffer
المصدر: Biology of Reproduction. 61:14-21
مصطلحات موضوعية: endocrine system, medicine.medical_specialty, media_common.quotation_subject, Gelatinase A, Trilostane, Cell Biology, General Medicine, Matrix metalloproteinase, Biology, Follicle, Endocrinology, medicine.anatomical_structure, Reproductive Medicine, Internal medicine, medicine, Interstitial collagenase, Matrilysin, Ovarian follicle, Ovulation, medicine.drug, media_common
الوصف: Progesterone appears essential for ovulation and luteinization of the primate follicle, but specific gene targets of progesterone action remain elusive. Limited evidence supports a role for progesterone in the induction of collagenolytic activity in the periovulatory follicle of primate and nonprimate species. This study was designed to elucidate the pattern of expression and progesterone regulation of mRNAs for the matrix metalloproteinases (MMPs) and their tissue inhibitors (TIMPs) in macaque granulosa cells during controlled ovarian stimulation cycles before (0 h) and after (up to 36 h) administration of an ovulatory hCG bolus. Levels of mRNAs for interstitial collagenase, gelatinase A, matrilysin, TIMP-1 and TIMP-2 increased (p < 0.05) within 12 h of hCG, while gelatinase B mRNA increased later, by 36 h after hCG. Administration of a 3beta-hydroxysteroid dehydrogenase inhibitor (Trilostane [TRL]) during hCG treatment decreased (p < 0.05) mRNA levels for interstitial collagenase, gelatinase B, matrilysin, TIMP-1, and TIMP-2. Progestin (R5020) replacement during hCG+TRL treatment returned interstitial collagenase and TIMP-1 mRNAs to control levels. These data suggest that one action of progesterone, and possibly other steroids, in the cascade of events leading to ovulation and luteinization of the primate follicle is to regulate the expression of specific ovarian proteases and protease inhibitors.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_________::9cca54615201936da113dfe4d4423148Test
https://doi.org/10.1095/biolreprod61.1.14Test
