The active forms of all of the matrix metalloproteinases (MMPs) are inhibited by a family of specific inhibitors, the tissue inhibitors of metalloproteinases (TIMPs). Inhibition represents a major level of control of MMP activity. A detailed knowledge of the mechanisms controlling TIMP gene expression is therefore important. We have isolated a genomic clone of the human TIMP-1 gene. A 3 kbp XbaI fragment has been sequenced; this fragment contains 1718 bp 5′ flanking sequences, exon 1, a 929 bp intron 1 and part of exon 2. Computer analysis reveals 10 consensus sequences for Sp1, six for activating protein 1 (AP-1), six for polyoma enhancer A3 (PEA3), 12 for AP-2 and five CCAAT boxes. The region hybridizing with a murine TIMP-1 promoter fragment has been subcloned and analysed further. RNase protection identifies six transcription start points, making exon 1 up to 48 bp in length. Transient transfection of promoter-chloramphenicol O-acetyltransferase reporter constructs into primary human ...
Tissue inhibitors of metalloproteinases (TIMPs) inhibit matrix metalloproteinases (MMPs) by forming a 1:1 stoichiometric complex, but the inhibition mechanism of these inhibitors is not known. Here we have investigated the reactive site of TIMP-1 by its proteinase susceptibility before and after forming a complex with MMP-3 (stromelysin 1). When TIMP-1 was allowed to react with human neutrophil elastase, its inhibitory activity was destroyed. This resulted from cleavage of the Val69-Cys70 bond. However, cleavage of this bond by neutrophil elastase was prevented when TIMP-1 formed a complex with the catalytic domain of MMP-3, and full TIMP-1 activity was restored after dissociation of the complex at pH 3.0 in the presence of EDTA. These results indicate that the region around Val69 closely associates with an active MMP. The three-dimensional structure of the N-terminal domain of TIMP-2 elucidated by NMR studies [Williamson, Martorell, Carr, Murphy, Docherty, Freedman and Feeney (1994) ...
The protocol describes a novel, rapid, and no-wash one-step immunoassay for highly sensitive and direct detection of the complexes between matrix metalloproteinases (MMPs) and their tissue inhibitor of metalloproteinases (TIMPs) based on AlphaLISA® technology. We describe two procedures: (i) one approach is used to analyze MMP-9-TIMP-1 interactions using recombinant human MMP-9 with its corresponding recombinant human TIMP-1 inhibitor and (ii) the second approach is used to analyze native or endogenous MMP-9-TIMP-1 protein interactions in samples of human plasma. Evaluating native MMP-9-TIMP-1 complexes using this approach avoids the use of indirect calculations of the MMP-9/TIMP-1 ratio for which independent MMP-9 and TIMP-1 quantifications by two conventional ELISAs are needed. The MMP-9-TIMP-1 AlphaLISA® assay is quick, highly simplified, and cost-effective and can be completed in less than 3 h. Moreover, the assay has great potential for use in basic and preclinical research as it allows direct
Badr, A. M., Interleukin-6 induces secretion of tissue inhibitors of metalloproteinases by breast carcinoma cells, Pakistan Journal of Pharmaceutical Sciences, vol. 29, issue 6, pp. 1969-1975, 2016 ...
This gene belongs to the TIMP gene family. The proteins encoded by this gene family are inhibitors of the matrix metalloproteinases, a group of peptidases involved in deg
Aneurysms are characterized by dilation, i.e. expansion and thinning of all the arterial wall layers, which is accompanied by remodeling of the connective tissue. Genes involved in the regulation of tissue remodeling are therefore candidate genes. We analyzed TIMP1 and TIMP2 coding sequences in 12 i …
IntroductionThe tissue inhibitors of metalloproteinases (TIMPs) are naturally occurring proteins that specifically inhibit matrix metalloproteinases…
MMPs and TIMPs grouped according to the MFI (low MFI: Goutallier score 0-1 (n = 10); high MFI: Goutallier score 2-4 (n = 20)). qRT-PCR was performed to anal
Main / More Pet Supplies / Prednisone make you sleepy 11 Answers - Posted in: prednisone, side effect, fatigue, sleeping - Answer: Hello, No it does not, people have trouble sleeping while on. 4 Answers - Posted in: pain, back pain, prednisone, side effect, fatigue - Answer: This should improve as time passes and your body adjusts, Does prednisone make you tired or sleepy? Prescription - Been taking prednisone for 2weeks,woke up with pain in my legs,knees down,shoud i?. The meds that are to relieve you be motivated or no prednisone make you sleepy effects occurs to that meds many us sleepy or prednisone make you sleepy sicker or drained and noticable to others that we r category or not ourselves and under the user. Weird but true i have having prednisone then others its fast but very only with the week after last dose. Im in the next of an allergic rhinitis to an unidentified graph. No new soaps, detergents, meds, etc. My obesity started on Thur night with hives. By Convocation AM my arms & ...
Are matrix metalloproteinases and their inhibitors reliable diagnosis biomarkers and attractive therapeutic targets in endometriosis? Patrick Henriet, Khin Su Mon, Etienne Marbaix De Duve Institute, Université catholique de Louvain, Brussels, Belgium Abstract: Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) are expressed in the human endometrium during the menstrual cycle, in particular to induce substantial extracellular matrix breakdown underlying menstruation. Endometriosis (EM) is characterized by the presence of endometrial tissue at ectopic locations. Because EM is thought to often develop from retrograde menstruation followed by implantation of menstrual tissue fragments at ectopic sites, endometrial MMPs and TIMPs were rapidly suspected as contributors to EM development and progression, generating hope for their use as biomarkers to facilitate EM diagnosis and as potential targets for developing new therapies against EM. Here, we not only summarize a
Chemically and conformationally authentic active domain of human tissue inhibitor of metalloproteinases-2 refolded from bacterial inclusion ...
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.
A tissue inhibitor of metalloproteinases (TIMP)-1 was isolated from human polymorphonuclear leukocytes (PMNL) in a complex with latent 95-kDa gelatinase (matrixmetalloproteinase, MMP-9). It was separated from the enzyme by gel fitration in the presence of SDS. Using a competitive ELISA procedure, we determined that 10% of the isolated gelatinase was complexed with TIMP-1. The presence of the inhibitor in isolated PMNL could also be demonstrated by indirect immunofluorescence using a specific antibody against TIMP-1. Cellular mRNA was isolated from PMNL, which were highly purified by separation via formylMet-Leu-Pro-stimulated chemotactic migration in a Boyden chamber. Using reverse-transcription PCR and Northern blotting, TIMP-1 mRNA was shown to be present in PMNL, suggesting that these cells are also capable of synthesizing TIMP-1 ...
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.
Research Topics, Genomes and Genes, Research Grants, Scientific Experts, Publications, Species about tissue inhibitor of metalloproteinase 2
TY - JOUR. T1 - Cellular distribution of tissue inhibitor of metalloproteimases-1 and-2 transcripts in human hepatocellalar carunoma(共著). AU - Ashida, Kouzou. PY - 1995. Y1 - 1995. M3 - Article. VL - 22. SP - 192. EP - 192. JO - HEPATOLOGY. JF - HEPATOLOGY. IS - 4. ER - ...
TIMP-3 (Tissue inhibitor of metalloproteinases 3) is a secreted extracellular matrix protein, metalloprotease inhibitor. It forms complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-3 is critical to the maintenance of tissue homeostasis by suppressing the proliferation of quiescent tissues in response to angiogenic factors and by inhibiting protease activity in tissues undergoing remodelling of the extracellular matrix. Defects in TIMP-3 are the cause of Sorsby fundus dystrophy (SFD). SFD is a rare autosomal dominant macular disorder with an age of onset in the fourth decade. It is characterized by loss of central vision from subretinal neovascularization and atrophy of the ocular tissues. Generally, macular disciform degeneration develops in the patients eye within 6 months to 6 years ...
The simplest interpretation of our in vitro studies is that increased expression of the MMP-9 proenzyme leads to the formation of active enzyme, which, in turn, degrades type IV collagen, leading to amnion cell apoptosis. Alternative interpretations include the possibility that the increased proMMP-9 sequestered endogenous tissue inhibitors of me-talloproteinases, leading to increased activities of […] ...
MMPs degrade the extracellular matrix of proteins, cleave cell surface receptors, release apoptotic ligands, and support activity of chemokine/cytokines.
Secreted active proteases, from families of enzymes such as matrix metalloproteinases (MMPs) and ADAMs (a disintegrin and metalloproteinases), participate in diverse pathological processes. To simultaneously measure multiple specific protease activities, a series of parallel enzyme reactions combined with a
Tumor necrosis factor-alpha is released from cells by a proteolytic cleavage. Previous work suggested that a specific, non-matrix metalloproteinase carries out this cleavage, but matrix metalloproteinases have also been implicated. In this paper, we report that none of the matrix metalloproteinases tested cleaved peptide substrates as specifically as the non-matrix metalloproteinase. A matrix metalloproteinase did process tumor necrosis factor-alpha extracted from COS cells, but neither tissue inhibitor of metalloproteinases-1 nor -2 blocked tumor necrosis factor-alpha processing by human monocytes. Moreover, tissue inhibitor of metalloproteinases-1 had at most a partial effect on the in vivo release of the cytokine in mice. We conclude that a non-matrix metalloproteinase is the major physiological tumor necrosis factor-alpha convertase.
The proteoglycan aggrecan is an important major component of cartilage matrix that gives articular cartilage the ability to withstand compression. Increased breakdown of aggrecan is associated with the development of arthritis and is considered to be catalyzed by aggrecanases, members of the ADAM-TS family of metalloproteinases. Four endogenous tissue inhibitors of metalloproteinases (TIMPs) regulate the activities of functional matrix metalloproteinases (MMPs), enzymes that degrade most components of connective tissue, but no endogenous factors responsible for the regulation of aggrecanases have been found. We show here that the N-terminal inhibitory domain of TIMP-3, a member of the TIMP family that has functional properties distinct from other TIMPs, is a strong inhibitor of human aggrecanases 1 and 2, with K(i) values in the subnanomolar range. This truncated inhibitor, which lacks the C-terminal domain that is responsible for interactions with molecules other than active metalloproteinases, is
Balanced expression of proteases and their inhibitors is one prerequisite of tissue homeostasis. Metastatic spread of tumor cells through the organism depends on proteolytic activity and is the death determinant for cancer patients. Paradoxically, increased expression of tissue inhibitor of metalloproteinases-1 (TIMP-1), a natural inhibitor of several endometalloproteinases, including matrix metalloproteinases and a disintegrin and metalloproteinase-10 (ADAM-10), in cancer patients is negatively correlated with their survival, although TIMP-1 itself inhibits invasion of some tumor cells. Here, we show that elevated stromal expression of TIMP-1 promotes liver metastasis in two independent tumor models by inducing the hepatocyte growth factor (HGF) signaling pathway and expression of several metastasis-associated genes, including HGF and HGF-activating proteases, in the liver. We also found in an in vitro assay that suppression of ADAM-10 is in principle able to prevent shedding of cMet, which may be one
Matrix metalloproteinases in impaired wound healing Fabio Sabino, Ulrich auf dem Keller Institute of Molecular Health Sciences, Eidgenössische Technische Hochschule (ETH) Zürich, Zürich, Switzerland Abstract: Cutaneous wound healing is a complex tissue response that requires a coordinated interplay of multiple cells in orchestrated biological processes to finally re-establish the skin's barrier function upon injury. Proteolytic enzymes and in particular matrix metalloproteinases (MMPs) contribute to all phases of the healing process by regulating immune cell influx, facilitating migration of fibroblasts and keratinocytes, and remodeling of the scar tissue. As a result of these pleiotropic functions in the healing skin wound, uncontrolled activities of MMPs are associated with impaired wound healing, a growing health problem in Western countries due to increased life expectancies and rising rates of underlying diseases, such as diabetes. However, detailed mechanisms have been only
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 ...
Tissue inhibitors of metalloproteinases (TIMPs) are a family of closely related proteins that inhibit matrix metalloproteinases (MMPs). In the central nervous system (CNS), TIMPs 2, 3, and 4 are constitutively expressed at high levels, whereas TIMP1 can be induced by various stimuli. Here, we studied the effects of constitutive expression of TIMP1 in the CNS in transgenic mice. Transgene expression started prenatally and persisted throughout lifetime at high levels. Since MMP activity has been implicated in CNS development, in proper function of the adult CNS, and in inflammatory disorders, we investigated Timp1-induced CNS alterations. Despite sufficient MMP inhibition, high expressor transgenic mice had a normal phenotype. The absence of compensatory up-regulation of MMP genes in the CNS of Timp1 transgenic mice indicates that development, learning, and memory functions do not require the entire MMP arsenal. To elucidate the effects of strong Timp1 expression in CNS inflammation, we induced ...
To the Editor:. It was with great interest that I read the article by Tuomainen et al1 recently published in this journal on the association of matrix metalloproteinase (MMP)-8 and tissue inhibitor of MMP-1 (TIMP-1) with cardiovascular diseases. The authors measured both analytes in serum and concluded from their results that serum MMP-8 and the ratio of MMP-8 to TIMP-1 were useful biomarkers with prognostic and diagnostic significances in men with cardiovascular disease, especially in those with prevalent or subclinical arteriosclerosis.1 Although I am not experienced in this clinical field, I believe it might be meaningful to make the readership of this journal aware of an important issue that was obviously not considered by Tuomainen et al in their study design. It refers to the influence of blood sample processing as essential precondition for the correct determination of circulating MMPs and TIMPs in peripheral blood. The effect of the type of blood sample, either collected as serum with or ...
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Extracellular matrix provides the microenvironment for the cells and serves as a tissue scaffold, guiding cell migration during embryonic development and wound repair. Beyond that, it also functions as the repository and modulator of growth factors and cytokines, and therefore is responsible for transmitting environmental signals to the cells.. Among proteases, the matrix metalloproteinases (MMPs) and a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) family are often associated with ECM degradation and remodeling. The inhibitors of MMPs are called tissue inhibitors of metalloproteinases (TIMPs), which are comprised of TIMP-1, TIMP-2, TIMP-3, and TIMP-4. The interactions between these proteases and their inhibitors play important roles in cell morphogenesis, angiogenesis, tissue remodeling, tissue repair, tumor metastasis, cirrhosis, and arthritis. The features of the ECM are determined both by the cells that produce the matrix and by the cells growing in it. QIAGENs ...
Substrate cleavage by metalloproteinases involves nucleophilic attack on the scissile peptide bond by a water molecule that is polarized by a catalytic metal, usually a zinc ion, and a general base, usually the carboxyl group of a glutamic acid side chain
Catalog No :RS01Ab0134Organism- HumanClonality :MonoclonalHost :MouseConcentration :500ug/mlApplication :WB, ICC, IHC-P, IHC-F, ELISA Immunoglobulin Type: IgGPurification: Affinity ChromatographyConjugate: No Conjugate IMMUNOGEN INFORMATIONImmunogen: Recombinant TIMP1 (Thr25~Ala207) expressed in E.coli.ANTIBODY SPECIFI
Lung development is a highly orchestrated process characterized by timed expression and activation of growth factor and protease/antiprotease systems. This interplay is essential in regulating vasculogenesis, alveolarization, and epithelial to mesenchymal transition during lung development. Alterati …
Sigma-Aldrich offers abstracts and full-text articles by [Eyal Zcharia, Juan Jia, Xiao Zhang, Lea Baraz, Ulf Lindahl, Tamar Peretz, Israel Vlodavsky, Jin-Ping Li].
Reaktivität: Fledermaus, Huhn, Schimpanse and more. 328 verschiedene TIMP2 Antikörper vergleichen. Alle direkt auf antikörper-online bestellbar!
Tabelul periodic - Sistemul periodic al elementelor - Nu credeam ca voi reusi sa-mi fac timp, sa mai pun vreo caramida la...Page 1 of 2 -
Tissue inhibitor of metalloproteinase-3 (TIMP-3) is a dual inhibitor of the matrix metalloproteinases (MMPs) and some adamalysins, two families of extracellular and cell surface metalloproteinases that function in extracellular matrix turnover and the shedding of cell surface proteins. The mechanism of inhibition of MMPs by TIMPs has been well characterized, and since the catalytic domains of MMPs and adamalysins are homologous, it was assumed that the interaction of TIMP-3 with adamalysins is closely similar. Here we report that the inhibition of the extracellular region of ADAM-17 (tumor necrosis factor alpha-converting enzyme (TACE)) by the inhibitory domain of TIMP-3 (N-TIMP-3) shows positive cooperativity. Also, mutations in the core of the MMP interaction surface of N-TIMP-3 dramatically reduce the binding affinity for MMPs but have little effect on the inhibitory activity for TACE. These results suggest that the mechanism of inhibition of ADAM-17 by TIMP-3 may be distinct from that for MMPs. The
TY - JOUR. T1 - Tissue inhibitor of metalloproteinases-3 promoter methylation is an independent prognostic factor for bladder cancer. AU - Hoque, Mohammad Obaidul. AU - Begum, Shahnaz. AU - Brait, Mariana. AU - Jeronimo, Carmen. AU - Zahurak, Marianna. AU - Ostrow, Kimberly Laskie. AU - Rosenbaum, Eli. AU - Trock, Bruce. AU - Westra, William H.. AU - Schoenberg, Mark. AU - Goodman, Steven N.. AU - Sidransky, David. PY - 2008/2. Y1 - 2008/2. N2 - Purpose: TIMP-3 (tissue inhibitor of metalloproteinases-3) is 1 of 4 members of a family of proteins that were originally classified according to their ability to inhibit matrix metalloproteinases. We analyzed TIMP-3 methylation in 175 urine sediment DNA samples from patients with bladder cancer with well characterized clinicopathological parameters, including patient outcome. Materials and Methods: We examined urine sediment DNA for aberrant methylation of 9 genes, including TIMP-3, by quantitative fluorogenic real-time polymerase chain reaction. ...
Using a competitive PCR technique we have established a system for rapid and simultaneous measurement of multiple genes involved in the metabolism of the ECM within a single colonic biopsy. To gain further insight into their biological function in inflammatory bowel disease we analysed relative mRNA expression of collagen type III, matrix metalloproteinases MMP-1 and MMP-2, their respective major activators MMP-3 and MMP-14, as well as their physiological inhibitors TIMP-1 and TIMP-2 in endoscopic biopsies from inflamed and non-inflamed colon of IBD patients.. We observed that mRNA expression of all MMPs was significantly increased in inflamed compared with non-inflamed colonic mucosa of these patients. This increase was most pronounced in ulcerated colonic mucosa. By performing westerns blots, increased expression of MMP-1, MMP-2, and MMP-3 was also demonstrated at the protein level, which supports previous in vitro studies showing a close correlation between mRNA and protein expression of ...
TY - JOUR. T1 - Progression of mycosis fungoides is associated with changes in angiogenesis and expression of the matrix metalloproteinases 2 and 9. AU - Vacca, A.. AU - Moretti, S.. AU - Ribatti, D.. AU - Pellegrino, A.. AU - Pimpinelli, N.. AU - Bianchi, B.. AU - Bonifazi, E.. AU - Ria, R.. AU - Serio, G.. AU - Dammacco, F.. PY - 1997/9. Y1 - 1997/9. N2 - Changes in angiogenesis and expression of extracellular matrix-degrading enzymes have been substantiated during progression of solid tumours, whereas information on haematological tumours remains circumstantial. In this study, 57 biopsies of mycosis fungoides (MF), a haematological tumour of T-cell lineage, were investigated immunohistochemically for the extent of angiogenesis, and by in situ hybridisation for the expression of matrix metalloproteinases 2 (MMP-2, collagenase A) and 9 (MMP-9, collagenase B). The biopsies we grouped according to the stage of progression: patch → plaque → nodular (most advanced). The extent of angiogenesis, ...
Purpose: While antiretroviral therapy (ART) has improved the quality of life and survival of HIV-1-infected patients, HIV-1-associated neurocognitive disorders (HAND) remain a major problem in over 30% of cases. All forms of HAND are associated with CNS inflammation. Astrocytes, the principal type of glial cells, are involved in signaling, homeostasis, and repair during CNS pathology. Some astrocytes become non-productively infected by HIV-1. The balance between matrix metalloproteinases (MMP) and their inhibitors must be tightly regulated during CNS inflammation. In the brain, tissue inhibitor of MMPs (TIMP)-1 protects human neurons from HIV-1-induced apoptosis and is mainly produced by astrocytes. Further, astrocyte TIMP-1 is differentially regulated during acute and chronic IL-1β-activation. However, the direct or indirect effects of astrocyte HIV-1 protein expression on TIMP-1 regulation are not well studied. Here, we investigated downstream effects of HIV-1 Tat and gp120 expression in astrocytes
ANGIOGENESIS, CYCLOOXYGENASE-2 AND MATRIX METALLOPROTEINASES IN MALIGNANT MESOTHELIOMA A thesis presented for the degree of DOCTOR OF PHILOSOPHY at The University o f Leicester Mr. John G. Edwards M.B.
Published in Trends in Cardiovascular Medicine, Volume 14, Issue 3, 2004, pages 105-111. © Trends in Cardiovascular Medicine, 2004, Elsevier Publishing. Lessner, S.M., Galis, Z.S. (2004). Matrix Metalloproteinases and Vascular Endothelium-Mononuclear Cell Close Encounters. Trends in Cardiovascular Medicine, 14(3), 105-111.. http://dx.doi.org/10.1016/j.tcm.2003.12.009. ...
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Based on automated MP annotations supported by experiments on knockout mouse models. Click on icons to go to all Timp3 data for that phenotype. ...
TIMP1, 0.1 mg. Tissue Inhibitors of Metalloproteinases (TIMPs) inhibit the proteolytic invasiveness of tumor cells and normal placental trophoblast cells.
TIMP1, 0.1 mg. Tissue Inhibitors of Metalloproteinases (TIMPs) inhibit the proteolytic invasiveness of tumor cells and normal placental trophoblast cells.
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Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7 and MMP-9.
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Vranka, Janice A., "The characterization of gelatinase inhibition and the involvement of the matrix metalloproteinases and their inhibitors in glaucoma and a retinal degeneration" (1997). Scholar Archive. 2639 ...