Probe Set Name Symbol 1598 G at Growth Arres
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Figure 2S 4 7 A - C 080125 CSCs 080418 CSCs - + IFN-a 48 h + IFN-a 48 h + IFN-a 72 h 6 + IFN-a 72 h 3 5 MRFI 4 2 3 2 1 1 0 0 MHC I MHC II MICA MICB ULBP-1 ULBP-2 ULBP-3 ULBP-4 MHC I MHC II MICA MICB ULBP-1 ULBP-2 ULBP-3 ULBP-4 7 B 13 080125 FBS - D 080418 FBS - + IFN-a 48 h 12 + IFN-a 48 h + IFN-a 72 h + IFN-a 72 h 6 080125 FBS 11 10 5 9 8 4 7 6 3 MRFI 5 4 2 3 2 1 1 0 0 MHC I MHC II MICA MICB ULBP-1 ULBP-2 ULBP-3 ULBP-4 MHC I MHC II MICA MICB ULBP-1 ULBP-2 ULBP-3 ULBP-4 Molecule Molecule FIGURE 4S FIGURE 5S Panel A Panel B FIGURE 6S A B C D Supplemental Results Table 1S. Modulation by IFN-α of APM in GBM CSC and FBS tumor cell lines. Molecule * Cell line IFN-α‡ HLA β2-m# HLA LMP TAP1 TAP2 class II A A HC§ 2 7 10 080125 CSCs - 1∞ (1) 3 (65) 2 (91) 1 (2) 6 (47) 2 (61) 1 (3) 1 (2) 1 (3) + 2 (81) 11 (80) 13 (99) 1 (3) 8 (88) 4 (91) 1 (2) 1 (3) 2 (68) 080125 FBS - 2 (81) 4 (63) 4 (83) 1 (3) 6 (80) 3 (67) 2 (86) 1 (3) 2 (75) + 2 (99) 14 (90) 7 (97) 5 (75) 7 (100) 6 (98) 2 (90) 1 (4) 3 (87) 080418 CSCs - 2 (51) 1 (1) 1 (3) 2 (47) 2 (83) 2 (54) 1 (4) 1 (2) 1 (3) + 2 (81) 3 (76) 5 (75) 2 (50) 2 (83) 3 (71) 1 (3) 2 (87) 1 (2) 080418 FBS - 1 (3) 3 (70) 2 (88) 1 (4) 3 (87) 2 (76) 1 (3) 1 (3) 1 (2) + 2 (78) 7 (98) 5 (99) 2 (94) 5 (100) 3 (100) 1 (4) 2 (100) 1 (2) 070104 CSCs - 1 (2) 1 (3) 1 (3) 2 (78) 1 (3) 1 (2) 1 (3) 1 (3) 1 (2) + 2 (98) 8 (100) 10 (88) 4 (89) 3 (98) 3 (94) 1 (4) 2 (86) 2 (79) * expression of APM molecules was evaluated by intracellular staining and cytofluorimetric analysis; ‡ cells were treatead or not (+/-) for 72 h with 1000 IU/ml of IFN-α; # β-2 microglobulin; § β-2 microglobulin-free HLA-A heavy chain; ∞ values are indicated as ratio between the mean of fluorescence intensity of cells stained with the selected mAb and that of the negative control; bold values indicate significant MRFI (≥ 2). -
Rhoa Promotes Epidermal Stem Cell Proliferation Via PKN1-Cyclin D1 Signaling
RESEARCH ARTICLE RhoA promotes epidermal stem cell proliferation via PKN1-cyclin D1 signaling Fan Wang1, Rixing Zhan2, Liang Chen1, Xia Dai1, Wenping Wang1, Rui Guo1, Xiaoge Li1, Zhe Li1, Liang Wang1, Shupeng Huang1, Jie Shen1, Shirong Li1☯*, Chuan Cao1☯* 1 Department of Plastic and Reconstructive Surgery, Southwestern Hospital, Third Military Medical University, Chongqing, China, 2 School of Nursing, Third Military Medical University, Chongqing, China ☯ These authors contributed equally to this work. * [email protected] (LS); [email protected] (CC) a1111111111 Abstract a1111111111 a1111111111 a1111111111 a1111111111 Objective Epidermal stem cells (ESCs) play a critical role in wound healing, but the mechanism under- lying ESC proliferation is not well defined. Here, we explore the effects of RhoA on ESC pro- liferation and the possible underlying mechanism. OPEN ACCESS Citation: Wang F, Zhan R, Chen L, Dai X, Wang W, Methods Guo R, et al. (2017) RhoA promotes epidermal (+/+) (-/- stem cell proliferation via PKN1-cyclin D1 Human ESCs were enriched by rapid adhesion to collagen IV. RhoA (G14V), RhoA ) signaling. PLoS ONE 12(2): e0172613. (T19N) and pGFP control plasmids were transfected into human ESCs. The effect of RhoA doi:10.1371/journal.pone.0172613 on cell proliferation was detected by cell proliferation and DNA synthesis assays. Induction Editor: Austin John Cooney, University of Texas at of PKN1 activity by RhoA was determined by immunoblot analysis, and the effects of PKN1 Austin Dell Medical School, UNITED STATES on RhoA in terms of inducing cell proliferation and cyclin D1 expression were detected using Received: August 10, 2016 specific siRNA targeting PKN1. The effects of U-46619 (a RhoA agonist) and C3 transferase Accepted: February 6, 2017 (a RhoA antagonist) on ESC proliferation were observed in vivo. -
Angio-Associated Migratory Cell Protein Interacts with Epidermal
Cellular Signalling 61 (2019) 10–19 Contents lists available at ScienceDirect Cellular Signalling journal homepage: www.elsevier.com/locate/cellsig Angio-associated migratory cell protein interacts with epidermal growth factor receptor and enhances proliferation and drug resistance in human T non-small cell lung cancer cells Shun Yaoa, Feifei Shia, Yingying Wanga,b, Xiaoyang Suna, Wenbo Suna, Yifeng Zhanga, ⁎ ⁎ Xianfang Liuc, Xiangguo Liua,b, , Ling Sua,b, a Shandong Provincial Key Laboratory of Animal Cell and Developmental Biology, School of Life Sciences, Shandong University, Qingdao, China b Shandong Provincial Collaborative Innovation Center of Cell Biology, School of Life Sciences, Shandong Normal University, Jinan, China c The Department of Otolaryngology Head and Neck Surgery, Shandong Provincial Hospital, Affiliated to Shandong University, Jinan, China ARTICLE INFO ABSTRACT Keywords: Angio-associated migratory cell protein (AAMP) is expressed in some human cancer cells. Previous studies have AAMP shown AAMP high expression predicted poor prognosis. But its biological role in non-small cell lung cancer Proliferation (NSCLC) cells is still unknown. In our present study, we attempted to explore the functions of AAMP in NSCLC Tumorigenesis cells. According to our findings, AAMP knockdown inhibited lung cancer cell proliferation and inhibited lung EGFR cancer cell tumorigenesis in the mouse xenograft model. Epidermal growth factor receptor (EGFR) is a primary Icotinib receptor tyrosine kinase (RTK) that promotes proliferation and plays an important role in cancer pathology. We Doxorubicin found AAMP interacted with EGFR and enhanced its dimerization and phosphorylation at tyrosine 1173 which activated ERK1/2 in NSCLC cells. In addition, we showed AAMP conferred the lung cancer cells resistance to chemotherapeutic agents such as icotinib and doxorubicin. -
The Impact of Endogenous Annexin A1 on Glucocorticoid Control of Infl Ammatory Arthritis
Basic and translational research Ann Rheum Dis: first published as 10.1136/annrheumdis-2011-201180 on 5 May 2012. Downloaded from EXTENDED REPORT The impact of endogenous annexin A1 on glucocorticoid control of inß ammatory arthritis Hetal B Patel,1 Kristin N Kornerup,1 AndreÕ LF Sampaio,1 Fulvio DÕAcquisto,1 Michael P Seed,1 Ana Paula Girol,2 Mohini Gray,3 Costantino Pitzalis,1 Sonia M Oliani,2 Mauro Perretti1 ▶ Additional (Þ gures and tables) ABSTRACT Annexin A1 (AnxA1) is an effector of resolution.4 are published online only. To view Objectives To establish the role and effect of Highly expressed in immune cells (eg, polymorpho- these Þ les please visit the journal nuclear cells and macrophages), this protein is exter- online (http://ard.bmj.com/ glucocorticoids and the endogenous annexin A1 (AnxA1) content/early/recent). pathway in inß ammatory arthritis. nalised to exert paracrine and juxtacrine effects, the vast majority of which are mediated by the formyl- 1William Harvey Research Methods Ankle joint mRNA and protein expression Institute, Barts and The London of AnxA1 and its receptors were analysed in peptide receptor type 2 (FPR2/ALX ([Lipoxin A4 School of Medicine, London UK naive and arthritic mice by real-time PCR and receptor]) or FPR2, in rodents).5 Intriguingly, FPR2/ 2Department of Biology; 6 immunohistochemistry. Inß ammatory arthritis was ALX is also the lipoxin A4 receptor indicating the Instituto de Bioci•ncias, Letras +/+ existence of important – yet not fully appreci- e Ci•ncias Exatas (IBILCE), S‹o induced with the K/BxN arthritogenic serum in AnxA1 −/− ated – networks in resolution.7 Paulo State University, S‹o JosŽ and AnxA1 mice; in some experiments, animals Another receptor do Rio Preto, Brazil were treated with dexamethasone (Dex) or with human is also advocated to mediate the effects of AnxA1, 3Medical Research Council recombinant AnxA1 or a protease-resistant mutant the formyl-peptide receptor type 1 or FPR1 (FPR1 Centre for Inß ammation, (termed SuperAnxA1). -
Supplemental Figure 1. Vimentin
Double mutant specific genes Transcript gene_assignment Gene Symbol RefSeq FDR Fold- FDR Fold- FDR Fold- ID (single vs. Change (double Change (double Change wt) (single vs. wt) (double vs. single) (double vs. wt) vs. wt) vs. single) 10485013 BC085239 // 1110051M20Rik // RIKEN cDNA 1110051M20 gene // 2 E1 // 228356 /// NM 1110051M20Ri BC085239 0.164013 -1.38517 0.0345128 -2.24228 0.154535 -1.61877 k 10358717 NM_197990 // 1700025G04Rik // RIKEN cDNA 1700025G04 gene // 1 G2 // 69399 /// BC 1700025G04Rik NM_197990 0.142593 -1.37878 0.0212926 -3.13385 0.093068 -2.27291 10358713 NM_197990 // 1700025G04Rik // RIKEN cDNA 1700025G04 gene // 1 G2 // 69399 1700025G04Rik NM_197990 0.0655213 -1.71563 0.0222468 -2.32498 0.166843 -1.35517 10481312 NM_027283 // 1700026L06Rik // RIKEN cDNA 1700026L06 gene // 2 A3 // 69987 /// EN 1700026L06Rik NM_027283 0.0503754 -1.46385 0.0140999 -2.19537 0.0825609 -1.49972 10351465 BC150846 // 1700084C01Rik // RIKEN cDNA 1700084C01 gene // 1 H3 // 78465 /// NM_ 1700084C01Rik BC150846 0.107391 -1.5916 0.0385418 -2.05801 0.295457 -1.29305 10569654 AK007416 // 1810010D01Rik // RIKEN cDNA 1810010D01 gene // 7 F5 // 381935 /// XR 1810010D01Rik AK007416 0.145576 1.69432 0.0476957 2.51662 0.288571 1.48533 10508883 NM_001083916 // 1810019J16Rik // RIKEN cDNA 1810019J16 gene // 4 D2.3 // 69073 / 1810019J16Rik NM_001083916 0.0533206 1.57139 0.0145433 2.56417 0.0836674 1.63179 10585282 ENSMUST00000050829 // 2010007H06Rik // RIKEN cDNA 2010007H06 gene // --- // 6984 2010007H06Rik ENSMUST00000050829 0.129914 -1.71998 0.0434862 -2.51672 -
Annexin A1 Expression Is Associated with Epithelial–Mesenchymal Transition (EMT), Cell Proliferation, Prognosis, and Drug Response in Pancreatic Cancer
cells Article Annexin A1 Expression Is Associated with Epithelial–Mesenchymal Transition (EMT), Cell Proliferation, Prognosis, and Drug Response in Pancreatic Cancer Masanori Oshi 1,2 , Yoshihisa Tokumaru 1,3 , Swagoto Mukhopadhyay 1, Li Yan 4, Ryusei Matsuyama 2, Itaru Endo 2 and Kazuaki Takabe 1,2,5,6,7,8,* 1 Department of Surgical Oncology, Roswell Park Comprehensive Cancer Center, Buffalo, NY 14263, USA; [email protected] (M.O.); [email protected] (Y.T.); [email protected] (S.M.) 2 Department of Gastroenterological Surgery, Yokohama City University School of Medicine, Yokohama, Kanagawa 236-0004, Japan; [email protected] (R.M.); [email protected] (I.E.) 3 Department of Surgical Oncology, Graduate School of Medicine, Gifu University, 1-1 Yanagido, Gifu 501-1194, Japan 4 Department of Biostatistics & Bioinformatics, Roswell Park Comprehensive Cancer Center, Buffalo, NY 14263, USA; [email protected] 5 Department of Gastrointestinal Tract Surgery, Fukushima Medical University School of Medicine, Fukushima 960-1295, Japan 6 Department of Surgery, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo the State University of New York, Buffalo, NY 14263, USA 7 Department of Surgery, Niigata University Graduate School of Medical and Dental Sciences, Niigata 951-8510, Japan Citation: Oshi, M.; Tokumaru, Y.; 8 Department of Breast Surgery and Oncology, Tokyo Medical University, Tokyo 160-8402, Japan Mukhopadhyay, S.; Yan, L.; * Correspondence: [email protected]; Tel.: +1-716-8-455-540; Fax: +1-716-8-451-668 Matsuyama, R.; Endo, I.; Takabe, K. Annexin A1 Expression Is Associated Abstract: Annexin A1 (ANXA1) is a calcium-dependent phospholipid-binding protein overexpressed with Epithelial–Mesenchymal in pancreatic cancer (PC). -
A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated. -
Clinical Study High Complement Factor I Activity in the Plasma of Children with Autism Spectrum Disorders
Hindawi Publishing Corporation Autism Research and Treatment Volume 2012, Article ID 868576, 6 pages doi:10.1155/2012/868576 Clinical Study High Complement Factor I Activity in the Plasma of Children with Autism Spectrum Disorders Naghi Momeni,1 Lars Brudin,2 Fatemeh Behnia,3 Berit Nordstrom,¨ 4 Ali Yosefi-Oudarji,5 Bengt Sivberg,4 Mohammad T. Joghataei,5 and Bengt L. Persson1 1 School of Natural Sciences, Linnaeus University, 39182 Kalmar, Sweden 2 Department of Clinical Physiology, Kalmar County Hospital, 39185 Kalmar, Sweden 3 Department of Occupational Therapy, University of Social Welfare and Rehabilitation Sciences, Tehran, Iran 4 Department of Health Sciences, Autism Research, Faculty of Medicine, Lund University, Box 157, 22100 Lund, Sweden 5 Cellular and Molecular Research Centre, Tehran University of Medical Sciences (TUMS), Tehran, Iran Correspondence should be addressed to Bengt Sivberg, [email protected] Received 17 June 2011; Revised 22 August 2011; Accepted 22 August 2011 Academic Editor: Judy Van de Water Copyright © 2012 Naghi Momeni 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. Autism spectrum disorders (ASDs) are neurodevelopmental and behavioural syndromes affecting social orientation, behaviour, and communication that can be classified as developmental disorders. ASD is also associated with immune system abnormality. Im- mune system abnormalities may be caused partly by complement system factor I deficiency. Complement factor I is a serine pro- tease present in human plasma that is involved in the degradation of complement protein C3b, which is a major opsonin of the complement system. -
Advances in Hematology
ADVANCES IN HEMATOLOGY Current Developments in the Management of Hematologic Disorders Hematology Section Editor: Craig M. Kessler, MD Atypical Hemolytic Uremic Syndrome: The Role of Complement Pathway Gene Mutation Analysis Ilene C. Weitz, MD Associate Professor of Clinical Medicine Jane Anne Nohl Division of Hematology Keck School of Medicine of USC Los Angeles, California H&O What causes atypical hemolytic uremic H&O Which mutations in complement alternative syndrome (aHUS)? pathway genes are linked to aHUS? IW We think that most people with aHUS have problems IW Multiple genetic mutations have been linked to with regulation of complement. As a result of excess com- aHUS, especially those involved in the complement plement, endothelial and organ damage occur. We know alternative pathway. These include mutations in comple- that mutations in the genes of complement regulatory pro- ment factor H, complement factor I, membrane cofactor teins are associated with aHUS. In addition, factors other protein, complement factor B, and C3 nephritic factor. than underlying mutations may play a role in increasing Mutations may cause the protein to be normal but low in activation and the expression of the clinical syndrome. quantity, or normal in quantity but abnormal in function; the degree of the abnormality may depend on whether the H&O How is the complement system activated patient is heterozygous or homozygous. and regulated? In addition, other factors such as thrombomodulin have been described that work through other enzymes. IW The complement system is a part of the innate Thrombomodulin is involved in complement regulation immune system that is necessary for fighting infections by activating thrombin activatable fibrinolytic inhibitor and aberrant immunologic stimuli. -
(12) United States Patent (10) Patent No.: US 9.284.609 B2 Tomlins Et Al
USOO9284609B2 (12) United States Patent (10) Patent No.: US 9.284.609 B2 Tomlins et al. (45) Date of Patent: Mar. 15, 2016 (54) RECURRENT GENE FUSIONS IN PROSTATE 4,683, 195 A 7, 1987 Mullis et al. CANCER 4,683.202 A 7, 1987 Mullis et al. 4,800,159 A 1/1989 Mullis et al. 4,873,191 A 10/1989 Wagner et al. (75) Inventors: Scott Tomlins, Ann Arbor, MI (US); 4,965,188 A 10/1990 Mullis et al. Daniel Rhodes, Ann Arbor, MI (US); 4,968,103 A 1 1/1990 McNab et al. Arul Chinnaiyan, Ann Arbor, MI (US); 5,130,238 A 7, 1992 Malek et al. Rohit Mehra, Ann Arbor, MI (US); 5,225,326 A 7/1993 Bresser 5,270,184 A 12/1993 Walker et al. Mark Rubin New York, NY (US); 5,283,174. A 2/1994 Arnold, Jr. et al. Xiao-Wei Sun, New York, NY (US); 5,283,317. A 2/1994 Saifer et al. Sven Perner, Ellwaugen (DE); Charles 5,399,491 A 3, 1995 Kacian et al. Lee, Marlborough, MA (US); Francesca 5,455,166 A 10/1995 Walker Demichelis, New York, NY (US) 5,480,784. A 1/1996 Kacian et al. s s 5,545,524 A 8, 1996 Trent 5,614,396 A 3/1997 Bradley et al. (73) Assignees: THE BRIGHAMAND WOMENS 5,631, 169 A 5/1997 Lakowicz et al. HOSPITAL, INC., Boston, MA (US); 5,710,029 A 1/1998 Ryder et al. THE REGENTS OF THE 5,776,782 A 7/1998 Tsuji UNIVERSITY OF MICHIGAN, Ann 5,814,447 A 9/1998 Ishiguro et al. -
Supplemental Material Annexin A2-S100A10 Represents the Regulatory Component of Maxi-Cl Channel Dependent on Protein Tyrosine De
Supplemental Material Annexin A2-S100A10 Represents the Regulatory Component of Maxi-Cl Channel Dependent on Protein Tyrosine Dephosphorylation and Intracellular Ca2+ Md. Rafiqul Islama Toshiaki Okadaa Petr G. Merzlyaka,b Abduqodir H. Toychieva,c Yuhko Ando-Akatsukad Ravshan Z. Sabirova,b Yasunobu Okadaa,e aDivision of Cell Signaling, National Institute for Physiological Sciences (NIPS), Okazaki, Japan, bInstitute of Biophysics and Biochemistry, National University of Uzbekistan, Tashkent, Uzbekistan, cDepartment of Biological Sciences, State University of New York College of Optometry, New York, NY, USA, dDepartment of Cell Physiology, Faculty of Pharmaceutical Sciences, Suzuka University of Medical Science, Suzuka, Japan, eDepartment of Physiology, Kyoto Prefectural University of Medicine, Kyoto, Japan Supplementary Material Supplementary Fig. 1. Maxi-Cl currents in C127 cells were unaffected by siRNA- mediated silencing of three annexin family member genes, Anxa1, Anxa3 and Anxa11. Effects of knockdown mediated by Anxa1-specific siRNA (A), Anxa3-specific siRNA (B) and Anxa11-specific siRNA (C). Top panels: The effects on expression of ANXA mRNAs in C127 cells treated with non-targeting siRNA (cnt) or Anxa1/3/11-specific siRNA (si) detected by RT-PCR using Gapdh as a control. M: molecular size markers (100-bp ladder). These data represent triplicate experiments. Upper-middle panels: Representative time courses of Maxi-Cl current activation recorded at +25 mV after patch excision from C127 cells transfected with Anxa1/3/11-specific siRNA. Lower-middle panels: Voltage- dependent inactivation pattern of Maxi-Cl currents elicited by applying single voltage step pulses from 0 to 25 and 50 mV. Bottom panels: Summary of the effects of non-targeting siRNA (Control) and Anxa1/3/11-specific siRNA on the mean Maxi-Cl currents recorded at +25 mV. -
Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases
International Journal of Molecular Sciences Review Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases Peter Goettig Structural Biology Group, Faculty of Molecular Biology, University of Salzburg, Billrothstrasse 11, 5020 Salzburg, Austria; [email protected]; Tel.: +43-662-8044-7283; Fax: +43-662-8044-7209 Academic Editor: Cheorl-Ho Kim Received: 30 July 2016; Accepted: 10 November 2016; Published: 25 November 2016 Abstract: Posttranslational modifications are an important feature of most proteases in higher organisms, such as the conversion of inactive zymogens into active proteases. To date, little information is available on the role of glycosylation and functional implications for secreted proteases. Besides a stabilizing effect and protection against proteolysis, several proteases show a significant influence of glycosylation on the catalytic activity. Glycans can alter the substrate recognition, the specificity and binding affinity, as well as the turnover rates. However, there is currently no known general pattern, since glycosylation can have both stimulating and inhibiting effects on activity. Thus, a comparative analysis of individual cases with sufficient enzyme kinetic and structural data is a first approach to describe mechanistic principles that govern the effects of glycosylation on the function of proteases. The understanding of glycan functions becomes highly significant in proteomic and glycomic studies, which demonstrated that cancer-associated proteases, such as kallikrein-related peptidase 3, exhibit strongly altered glycosylation patterns in pathological cases. Such findings can contribute to a variety of future biomedical applications. Keywords: secreted protease; sequon; N-glycosylation; O-glycosylation; core glycan; enzyme kinetics; substrate recognition; flexible loops; Michaelis constant; turnover number 1.