SERPINB13 293 Cell Lysate Storage: Store at -80°C

Total Page：16

File Type：pdf, Size：1020Kb

From Biology to Discovery™ SERPINB13 293 Cell Lysate Storage: Store at -80°C. Minimize freeze-thaw cycles. After addition of 2X SDS Loading Buffer, the lysates can be stored Subcategory: Cell Lysate at -20°C. Product is guaranteed 6 months from the date of Cat. No.: 407420 shipment. Unit: 0.1 mg For research use only, not for diagnostic or therapeutic Description: procedures. Antigen standard for serpin peptidase inhibitor, clade B (ovalbumin), member 13 (SERPINB13) is a lysate prepared from HEK293T cells transiently transfected with a TrueORF gene-carrying pCMV plasmid (OriGene Technologies, Inc.) and then lysed in RIPA Buffer. Protein concentration was determined using a colorimetric assay. The antigen control carries a C-terminal Myc/DDK tag for detection. Applications: ELISA, WB, IP Format: This product includes 3 vials: 1 vial of gene-specific cell lysate, 1 vial of control vector cell lysate, and 1 vial of loading buffer. Each lysate vial contains 0.1 mg lysate in 0.1 ml (1 mg/ml) of RIPA Buffer (50 mM Tris-HCl pH7.5, 250 mM NaCl, 5 mM EDTA, 50 mM NaF, 1% NP40). The loading buffer vial contains 0.5 ml 2X SDS Loading Buffer (125 mM Tris-Cl, pH6.8, 10% glycerol, 4% SDS, 0.002% Bromophenol blue, 5% beta-mercaptoethanol). Alternate Names: protease inhibitor 13 (hurpin, headpin); serine (or cysteine) proteinase inhibitor, clade B (ovalbumin), member 13; HURPIN; UV-B repressed sequence, HUR 7; PI- 13; peptidase inhibitor 13; proteinase inhibitor 13; haCaT UV- repressible serpin; SERPINB13; headpin; HSHUR7SEQ; HUR7; MGC126870; PI13 Accession No.: NP_036529 Application Notes: WB: Mix equal volume of lysates with 2X SDS Loading Buffer. Boil the mixture for 10 min before loading (for membrane protein lysates, incubate the mixture at room temperature for 30 min). Load 5 ug lysate per lane. Abbiotec, LLC • 7985 Dunbrook Rd, Ste A, San Diego, CA 92126 • USA Ph: 858.586.0500 • Fax: 858.586.6252 • Email: [email protected] • www.abbiotec.com.

Copy Link

Recommended publications

ONCOGENOMICS Through the Use of Chemotherapeutic Agents
Oncogene (2002) 21, 7749 – 7763 ª 2002 Nature Publishing Group All rights reserved 0950 – 9232/02 $25.00 www.nature.com/onc Expression profiling of primary non-small cell lung cancer for target identification Jim Heighway*,1, Teresa Knapp1, Lenetta Boyce1, Shelley Brennand1, John K Field1, Daniel C Betticher2, Daniel Ratschiller2, Mathias Gugger2, Michael Donovan3, Amy Lasek3 and Paula Rickert*,3 1Target Identification Group, Roy Castle International Centre for Lung Cancer Research, University of Liverpool, 200 London Road, Liverpool L3 9TA, UK; 2Institute of Medical Oncology, University of Bern, 3010 Bern, Switzerland; 3Incyte Genomics Inc., 3160 Porter Drive, Palo Alto, California, CA 94304, USA Using a panel of cDNA microarrays comprising 47 650 Introduction transcript elements, we have carried out a dual-channel analysis of gene expression in 39 resected primary The lack of generally effective therapies for lung cancer human non-small cell lung tumours versus normal lung leads to the high mortality rate associated with this tissue. Whilst *11 000 elements were scored as common disease. Recorded 5-year survival figures vary, differentially expressed at least twofold in at least one to some extent perhaps reflecting differences in sample, 96 transcripts were scored as over-represented ascertainment methods, but across Europe are approxi- fourfold or more in at least seven out of 39 tumours mately 10% (Bray et al., 2002). Whilst surgery is an and 30 sequences 16-fold in at least two out of 39 effective strategy for the treatment of localized lesions, tumours, including 24 transcripts in common. Tran- most patients present with overtly or covertly dissemi- scripts (178) were found under-represented fourfold in nated disease.
[Show full text]
Serpinb2 Is Involved in Cellular Response Upon UV Irradiation
www.nature.com/scientificreports OPEN SerpinB2 is involved in cellular response upon UV irradiation Hajnalka Majoros1, Zsuzsanna Ujfaludi1, Barbara Nikolett Borsos1, Viktória Vivien Hudacsek1, Zita Nagy3, Frederic Coin3, Krisztina Buzas2, Ilona Kovács4, Tamás Bíró5,6, Imre Miklós Boros1,2 1 Received: 20 August 2018 & Tibor Pankotai Accepted: 10 December 2018 Ultraviolet light induced pyrimidine dimer is a helix distortion DNA damage type, which recruits repair Published: xx xx xxxx complexes. However, proteins of these complexes that take part in both DNA damage recognition and repair have been well-described, the regulation of the downstream steps of nucleotide excision repair (NER) have not been clearly clarifed yet. In a high-throughput screen, we identifed SerpinB2 (SPB2) as one of the most dramatically upregulated gene in keratinocytes following UV irradiation. We found that both the mRNA and the protein levels of SPB2 were increased upon UV irradiation in various cell lines. Additionally, UV damage induced translocation of SPB2 from the cytoplasm to the nucleus as well as the damage induced foci formation of it. Here we show that SPB2 co-localizes with XPB involved in the NER pathway at UV-induced repair foci. Finally, we demonstrated that UV irradiation promoted the association of SPB2 with ubiquitylated proteins. In basal cell carcinoma tumour cells, we identifed changes in the subcellular localization of SPB2. Based on our results, we conclude that SPB2 protein has a novel role in UV-induced NER pathway, since it regulates the removal of the repair complex from the damaged site leading to cancerous malformation. Our genome is constantly exposed to endogenous and exogenous sources leading to DNA damage and impair- ment of genome integrity.
[Show full text]
Characterisation of Serpinb2 As a Stress Response Modulator
University of Wollongong Research Online University of Wollongong Thesis Collection 1954-2016 University of Wollongong Thesis Collections 2015 Characterisation of SerpinB2 as a stress response modulator Jodi Anne Lee University of Wollongong Follow this and additional works at: https://ro.uow.edu.au/theses University of Wollongong Copyright Warning You may print or download ONE copy of this document for the purpose of your own research or study. The University does not authorise you to copy, communicate or otherwise make available electronically to any other person any copyright material contained on this site. You are reminded of the following: This work is copyright. Apart from any use permitted under the Copyright Act 1968, no part of this work may be reproduced by any process, nor may any other exclusive right be exercised, without the permission of the author. Copyright owners are entitled to take legal action against persons who infringe their copyright. A reproduction of material that is protected by copyright may be a copyright infringement. A court may impose penalties and award damages in relation to offences and infringements relating to copyright material. Higher penalties may apply, and higher damages may be awarded, for offences and infringements involving the conversion of material into digital or electronic form. Unless otherwise indicated, the views expressed in this thesis are those of the author and do not necessarily represent the views of the University of Wollongong. Recommended Citation Lee, Jodi Anne, Characterisation of SerpinB2 as a stress response modulator, Doctor of Philosophy thesis, School of Biological Sciences, University of Wollongong, 2015. https://ro.uow.edu.au/theses/4538 Research Online is the open access institutional repository for the University of Wollongong.
[Show full text]
Supplementary Methods
Supplementary methods Human lung tissues and tissue microarray (TMA) All human tissues were obtained from the Lung Cancer Specialized Program of Research Excellence (SPORE) Tissue Bank at the M.D. Anderson Cancer Center (Houston, TX). A collection of 26 lung adenocarcinomas and 24 non-tumoral paired tissues were snap-frozen and preserved in liquid nitrogen for total RNA extraction. For each tissue sample, the percentage of malignant tissue was calculated and the cellular composition of specimens was determined by histological examination (I.I.W.) following Hematoxylin-Eosin (H&E) staining. All malignant samples retained contained more than 50% tumor cells. Specimens resected from NSCLC stages I-IV patients who had no prior chemotherapy or radiotherapy were used for TMA analysis by immunohistochemistry. Patients who had smoked at least 100 cigarettes in their lifetime were defined as smokers. Samples were fixed in formalin, embedded in paraffin, stained with H&E, and reviewed by an experienced pathologist (I.I.W.). The 413 tissue specimens collected from 283 patients included 62 normal bronchial epithelia, 61 bronchial hyperplasias (Hyp), 15 squamous metaplasias (SqM), 9 squamous dysplasias (Dys), 26 carcinomas in situ (CIS), as well as 98 squamous cell carcinomas (SCC) and 141 adenocarcinomas. Normal bronchial epithelia, hyperplasia, squamous metaplasia, dysplasia, CIS, and SCC were considered to represent different steps in the development of SCCs. All tumors and lesions were classified according to the World Health Organization (WHO) 2004 criteria. The TMAs were prepared with a manual tissue arrayer (Advanced Tissue Arrayer ATA100, Chemicon International, Temecula, CA) using 1-mm-diameter cores in triplicate for tumors and 1.5 to 2-mm cores for normal epithelial and premalignant lesions.
[Show full text]
Serpins—From Trap to Treatment
MINI REVIEW published: 12 February 2019 doi: 10.3389/fmed.2019.00025 SERPINs—From Trap to Treatment Wariya Sanrattana, Coen Maas and Steven de Maat* Department of Clinical Chemistry and Haematology, University Medical Center Utrecht, Utrecht University, Utrecht, Netherlands Excessive enzyme activity often has pathological consequences. This for example is the case in thrombosis and hereditary angioedema, where serine proteases of the coagulation system and kallikrein-kinin system are excessively active. Serine proteases are controlled by SERPINs (serine protease inhibitors). We here describe the basic biochemical mechanisms behind SERPIN activity and identify key determinants that influence their function. We explore the clinical phenotypes of several SERPIN deficiencies and review studies where SERPINs are being used beyond replacement therapy. Excitingly, rare human SERPIN mutations have led us and others to believe that it is possible to refine SERPINs toward desired behavior for the treatment of enzyme-driven pathology. Keywords: SERPIN (serine proteinase inhibitor), protein engineering, bradykinin (BK), hemostasis, therapy Edited by: Marvin T. Nieman, Case Western Reserve University, United States INTRODUCTION Reviewed by: Serine proteases are the “workhorses” of the human body. This enzyme family is conserved Daniel A. Lawrence, throughout evolution. There are 1,121 putative proteases in the human body, and about 180 of University of Michigan, United States Thomas Renne, these are serine proteases (1, 2). They are involved in diverse physiological processes, ranging from University Medical Center blood coagulation, fibrinolysis, and inflammation to immunity (Figure 1A). The activity of serine Hamburg-Eppendorf, Germany proteases is amongst others regulated by a dedicated class of inhibitory proteins called SERPINs Paulo Antonio De Souza Mourão, (serine protease inhibitors).
[Show full text]
Serpinb10, a Serine Protease Inhibitor, Is Implicated in UV-Induced Cellular Response
International Journal of Molecular Sciences Article SerpinB10, a Serine Protease Inhibitor, Is Implicated in UV-Induced Cellular Response Hajnalka Majoros 1, Barbara N. Borsos 1, Zsuzsanna Ujfaludi 1 , Zoltán G. Páhi 1,Mónika Mórocz 2, Lajos Haracska 2, Imre Miklós Boros 3,4 and Tibor Pankotai 1,* 1 Institute of Pathology, Faculty of Medicine, University of Szeged, 1 Állomás utca, H-6725 Szeged, Hungary; [email protected] (H.M.); [email protected] (B.N.B.); [email protected] (Z.U.); [email protected] (Z.G.P.) 2 HCEMM-BRC Mutagenesis and Carcinogenesis Research Group, Institute of Genetics, Biological Research Centre, H-6726 Szeged, Hungary; [email protected] (M.M.); [email protected] (L.H.) 3 Department of Biochemistry and Molecular Biology, Faculty of Science and Informatics, University of Szeged, H-6726 Szeged, Hungary; [email protected] 4 Institute of Biochemistry, Biological Research Centre, H-6726 Szeged, Hungary * Correspondence: [email protected]; Tel.: +36-62-546-164 Abstract: UV-induced DNA damage response and repair are extensively studied processes, as any malfunction in these pathways contributes to the activation of tumorigenesis. Although several proteins involved in these cellular mechanisms have been described, the entire repair cascade has remained unexplored. To identify new players in UV-induced repair, we performed a microarray screen, in which we found SerpinB10 (SPB10, Bomapin) as one of the most dramatically upregulated SPB10 genes following UV irradiation. Here, we demonstrated that an increased mRNA level of is a general cellular response following UV irradiation regardless of the cell type.
[Show full text]
Suppression of the Invasion and Migration of Cancer Cells by SERPINB Family Genes and Their Derived Peptides
238 ONCOLOGY REPORTS 27: 238-245, 2012 Suppression of the invasion and migration of cancer cells by SERPINB family genes and their derived peptides RUEY-HWANG CHOU1-4, HUI-CHIN WEN1,7, WEI-GUANG LIANG1,5, SHENG-CHIEH LIN1,5, HSIAO-WEI YUAN1, CHENG-WEN WU1,5,6 and WUN-SHAING WAYNE CHANG1 1National Institute of Cancer Research, National Health Research Institutes, Miaoli 35053; 2Center for Molecular Medicine, China Medical University Hospital, Taichung 40402; 3China Medical University, Taichung 40402; 4Department of Biotechnology, Asia University, Taichung 41354; 5College of Life Science, National Tsing Hua University, Hsinchu 30013; 6Institute of Biochemistry and Molecular Biology, National Yang Ming University, Taipei 11221, Taiwan, R.O.C. Received June 28, 2011; Accepted August 17, 2011 DOI: 10.3892/or.2011.1497 Abstract. Apart from SERPINB2 and SERPINB5, the roles SERPINB RCL-peptides may provide a reasonable strategy of the remaining 13 members of the human SERPINB family against lethal cancer metastasis. in cancer metastasis are still unknown. In the present study, we demonstrated that most of these genes are differentially Introduction expressed in tumor tissues compared to matched normal tissues from lung or breast cancer patients. Overexpression of Cancer metastasis is the leading cause of morbidity and each SERPINB gene effectively suppressed the invasiveness mortality in cancer patients. It is a highly complex process, and motility of malignant cancer cells. Among all of the genes, including cell detachment, migration, invasion, circulation in the SERPINB1, SERPINB5 and SERPINB7 genes were more blood vessels, adhesion, colonization at other sites and forma- potent, and the inhibitory effect was further enhanced by tion of secondary tumors (1).
[Show full text]
Serpin Inhibition Mechanism: a Delicate Balance Between Native Metastable State and Polymerization
SAGE-Hindawi Access to Research Journal of Amino Acids Volume 2011, Article ID 606797, 10 pages doi:10.4061/2011/606797 Review Article Serpin Inhibition Mechanism: A Delicate Balance between Native Metastable State and Polymerization Mohammad Sazzad Khan,1 Poonam Singh,1 Asim Azhar,1 Asma Naseem,1 Qudsia Rashid,1 Mohammad Anaul Kabir,2 and Mohamad Aman Jairajpuri1 1 Department of Biosciences, Jamia Millia Islamia University, Jamia Nagar, New Delhi 110025, India 2 Department of Biotechnology, National Institute of Technology Calicut (NITC), NIT Campus P.O., Calicut, Kerala 673601, India Correspondence should be addressed to Mohamad Aman Jairajpuri, m [email protected] Received 14 February 2011; Accepted 7 March 2011 Academic Editor: Zulfiqar Ahmad Copyright © 2011 Mohammad Sazzad Khan et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The serpins (serine proteinase inhibitors) are structurally similar but functionally diverse proteins that fold into a conserved structure and employ a unique suicide substrate-like inhibitory mechanism. Serpins play absolutely critical role in the control of proteases involved in the inflammatory, complement, coagulation and fibrinolytic pathways and are associated with many conformational diseases. Serpin’s native state is a metastable state which transforms to a more stable state during its inhibitory mechanism. Serpin in the native form is in the stressed (S) conformation that undergoes a transition to a relaxed (R) conformation for the protease inhibition. During this transition the region called as reactive center loop which interacts with target proteases, inserts itself into the center of β-sheet A to form an extra strand.
[Show full text]
Garvan Institute for Medical Research
Supplementary figure 1 Fold Change 2510 Fold change Gene Symbol Probe Set Name Expt. A Expt. B Expt. C TNFAIP6 206025_s_at 9.6 8.5 7.4 CCL26 223710_at 7.9 7.6 6.8 TNFAIP6 206026_s_at 6.9 7.4 7.4 SERPINB4 211906_s_at 7.5 7.1 7.3 aP2 203980_at 6.5 6.7 4.7 CAPN14 1557321_a_at 6.9 5.8 5.6 TMEM71 238429_at 6.3 5.8 5.3 SERPINB4 210413_x_at 5.5 5 5.1 RASGRP1 205590_at 8 4.9 3.3 SERPINB13 211361_s_at 4.3 4.9 4.9 SLC7A2 225516_at 5.5 4.9 2.8 SERPINB13 217272_s_at 4 4.7 5 IL13RA2 206172_at 4 4.6 3.8 SERPINB3 209720_s_at 5.7 4.5 4.5 TNC 216005_at 6.4 4.5 4.4 SERPINB3 209719_x_at 4.8 4.2 4.3 KAL1 205206_at 4.7 4.1 4.1 TNC 237169_at 5.8 4 4.2 CXCL6 206336_at 2.8 3.8 3.2 PMP22 210139_s_at 5.9 3.8 2.6 NTRK1 208605_s_at 3.8 3.6 5.3 --- 236198_at 5.1 3.6 4 LRRC31 220622_at 5.1 3.5 3.9 CTSC 225647_s_at 3.4 3.5 3.1 CTSC 231234_at 3.8 3.5 3.4 SERPINB13 211362_s_at 2.8 3.4 5.2 DPP4 203716_s_at 2.9 3.3 3.9 ADAM28 205997_at 4.3 3 3.8 ADAM28 208268_at 2.7 3 2.5 SIDT1 219734_at 2.8 3 2.4 CDH26 232306_at 3.4 2.9 2.2 HAS2 230372_at 3.4 2.8 2 TNC 241272_at 4.5 2.8 2.9 CXCL10 204533_at 2.3 2.7 3.1 CXCL11 210163_at 2.1 2.7 2.9 LEPREL1 218717_s_at 2.2 2.7 2.2 CHST9 224400_s_at 3.1 2.7 2 CTSC 225646_at 3.1 2.7 2.7 C21orf34 239999_at 2.5 2.7 4.1 CYP1A1 205749_at 2.2 2.5 2.9 CPM 206100_at 2.7 2.5 2.1 MME 203434_s_at 2.7 2.4 2.6 TA-LRRP 212978_at 2.2 2.4 2 ST8SIA1 210073_at 2.4 2.3 2.3 PPFIBP2 212841_s_at 2.2 2.3 3 FLJ22833 219334_s_at 2.3 2.3 2.3 CHST9 223737_x_at 3 2.3 2.4 SERPINB13 216258_s_at 2.4 2.2 4.4 LOC129607 226702_at 3.8 2.2 2.9 --- 231925_at 2.6 2.2 2.2 CPM
[Show full text]
Headpin: a Serpin with Endogenous and Exogenous Suppression of Angiogenesis
Research Article Headpin: A Serpin with Endogenous and Exogenous Suppression of Angiogenesis Thomas D. Shellenberger,1 Abhijit Mazumdar,1 Ying Henderson,1 Katrina Briggs,1 Mary Wang,1 Chandrani Chattopadhyay,1 Arumugam Jayakumar,1 Mitchell Frederick,1 and Gary L. Clayman1,2 Department of 1Head and Neck Surgery and 2Cancer Biology, The University of Texas M.D. Anderson Cancer Center, Houston, Texas Abstract range of cancers. Several highly conserved serpin genes, including Headpin is a novel serine proteinase inhibitor (serpin) with plasminogen activator inhibitor 1 and 2 (PAI-1 and PAI-2), constitutive mRNA expression in histologically normal oral squamous cell carcinoma antigen 1 and 2 (SCCA-1 and SCCA-2), mucosa but with lost or down-regulated expression in head maspin, and headpin, cluster to chromosome 18q21.3 to q23 (1). and neck squamous cell carcinoma. Several serpin family This locus is a site of frequent loss in multiple cancer types (2–5). members are similarly lost in multiple cancer types and Moreover, the loss of serpin expression has been correlated with hold tumor suppressor functions including the inhibition advanced tumor progression (6–9). of angiogenesis. However, the functional significance for We initially identified headpin as a head and neck serpin that the loss of headpin expression in cancer is not known. Using shows strong constitutive expression in histologically normal oral immunohistochemical analysis of invasive squamous cell mucosa but profoundly reduced mRNA expression in head and carcinoma and matched normal squamous mucosa of neck squamous cell carcinoma (HNSCC; ref. 10). The gene was patient specimens, headpin expression was lost or down- independently discovered by Abts et al.
[Show full text]
SERPINB13 Mouse Monoclonal Antibody [Clone ID: OTI2F5] Product Data
OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for TA503673 SERPINB13 Mouse Monoclonal Antibody [Clone ID: OTI2F5] Product data: Product Type: Primary Antibodies Clone Name: OTI2F5 Applications: FC, WB Recommend Dilution: WB 1:2000, FLOW 1:100 Reactivity: Human Host: Mouse Isotype: IgG2a Clonality: Monoclonal Immunogen: Full length human recombinant protein of human SERPINB13(NP_036529) produced in HEK293T cell. Formulation: PBS (PH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide. Concentration: 0.87 mg/ml Purification: Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G) Predicted Protein Size: 44.1 kDa Gene Name: serpin family B member 13 Database Link: NP_036529 Entrez Gene 5275 Human Synonyms: headpin; HSHUR7SEQ; HUR7; PI13 Protein Families: Druggable Genome, Transmembrane This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2020 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 1 / 2 SERPINB13 Mouse Monoclonal Antibody [Clone ID: OTI2F5] – TA503673 Product images: HEK293T cells were transfected with the pCMV6- ENTRY control (Left lane) or pCMV6-ENTRY SERPINB13 ([RC211032], Right lane) cDNA for 48 hrs and lysed. Equivalent amounts of cell lysates (5 ug per lane) were separated by SDS-PAGE and immunoblotted with anti-SERPINB13. Positive lysates [LY415794] (100ug) and [LC415794] (20ug) can be purchased separately from OriGene. HEK293T cells transfected with either [RC211032] overexpress plasmid (Red) or empty vector control plasmid (Blue) were immunostained by anti-SERPINB13 antibody (TA503673), and then analyzed by flow cytometry.
[Show full text]
Role of Protease-Inhibitors in Ocular Diseases
Molecules 2014, 19, 20557-20569; doi:10.3390/molecules191220557 OPEN ACCESS molecules ISSN 1420-3049 www.mdpi.com/journal/molecules Review Role of Protease-Inhibitors in Ocular Diseases Nicola Pescosolido 1, Andrea Barbato 2, Antonia Pascarella 3, Rossella Giannotti 2, Martina Genzano 2 and Marcella Nebbioso 2,* 1 Department of Cardiovascular, Respiratory, Nephrologic, Anesthesiologic and Geriatric Sciences, Policlinico Umberto I, Faculty of Medicine and Odontology, Sapienza University of Rome, piazzale Aldo Moro 5, Rome 00185, Italy 2 Department of Sense Organs, Ocular Electrophysiology Center, Policlinico Umberto I, Faculty of Medicine and Odontology, Sapienza University of Rome, piazzale Aldo Moro 5, Rome 00185, Italy 3 Department of Biology and Biotechnology Charles Darwin, Sapienza University of Rome, piazzale Aldo Moro 5, Rome 00185, Italy * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel.: +39-06-4997-5422; Fax: +39-06-4997-5425. External Editor: Isabel C. F. R. Ferreira Received: 19 October 2014; in revised form: 2 December 2014 / Accepted: 2 December 2014 / Published: 8 December 2014 Abstract: It has been demonstrated that the balance between proteases and protease-inhibitors system plays a key role in maintaining cellular and tissue homeostasis. Indeed, its alteration has been involved in many ocular and systemic diseases. In particular, research has focused on keratoconus, corneal wounds and ulcers, keratitis, endophthalmitis, age-related macular degeneration, Sorsby fundus dystrophy, loss of nerve cells and photoreceptors during optic neuritis both in vivo and in vitro models. Protease-inhibitors have been extensively studied, rather than proteases, because they may represent a therapeutic approach for some ocular diseases.
[Show full text]