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HYAL1 (h.HYAL1 , FUS2, NAT6, LUCA1, Hyal-1, LuCa-1, Hyaluronidase-1, Hyaluronoglucosaminidase-1, Lung carcinoma protein 1) Catalog number 144710 Supplier United States Biological Hyaluronidase-1, also known as HYAL1 or LUCA1, is an enzyme that in humans is encoded by the HYAL1 gene. The gene is one of several related genes in a region of chromosome 3p21.3 associated with tumor suppression. This gene encodes a lysosomal hyaluronidase. Hyaluronidases intracellularly degrade hyaluronan, one of the major glycosaminoglycans of the extracellular matrix. Hyaluronan is thought to be involved in cell proliferation, migration and differentiation. This enzyme is active at an acidic pH and is the major hyaluronidase in plasma. Mutations in this gene are associated with mucopolysaccharidosis type IX, or hyaluronidase deficiency. UniProt Number Q12794 Gene ID HYAL1 Applications Suitable for use in Western Blot, Immunohistochemistry (Paraffin and Frozen), and Immunocytochemistry. Recommended Dilution Optimal dilutions to be determined by the researcher. Storage and Handling Store at -20˚C for one year. After reconstitution, store at 4˚C for one month. Can also be aliquoted and stored frozen at -20˚C for long term. Avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Immunogen A synthetic peptide corresponding to a sequence at the N-terminus of human HYAL1. Formulation Supplied as a lyophilized powder. Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3. Reconstitution: Add 0.2ml of distilled water will yield a concentration of 500ug/ml. Purity Purified by immunoaffinity chromatography. Specificity Recognizes human h.HYAL1. No crossreactivity with other proteins. Product Type Pab Source human Isotype IgG Grade Affinity Purified Applications IC IHC WB Crossreactivity Hu Storage 4°C/-20°C Reference 1. Csoka, A. B., Frost, G. I., Heng, H. H. Q., Scherer, S. W., Mohapatra, G., Stern, R. The hyaluronidase gene HYAL1 maps to chromosome 3p21.2-p21.3 in human and 9F1-F2 in mouse, a conserved candidate tumor suppressor locus. Genomics 48: 63-70, 1998. Note: Erratum: Genomics 84: 227 only, 2004. 2. Martin, D. C., Atmuri, V., Hemming, R. J., Farley, J., Mort, J. S., Byers, S., Hombach-Klonisch, S., Csoka, A. B., Stern, R., Triggs-Raine, B. L. A mouse model of human mucopolysaccharidosis IX exhibits osteoarthritis. Hum. Molec. Genet. 17: 1904-1915, 2008. Note: Erratum: Hum. Molec. Genet. 17: 2919 only, 2008. Powered by TCPDF (www.tcpdf.org).

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Evaluation of the Prognostic Potential of Hyaluronic Acid and Hyaluronidase (HYAL1) for Prostate Cancer1
[CANCER RESEARCH 63, 2638–2644, May 15, 2003] Evaluation of the Prognostic Potential of Hyaluronic Acid and Hyaluronidase (HYAL1) for Prostate Cancer1 J. Timothy Posey, Mark S. Soloway, Sinan Ekici, Mario Sofer, Francisco Civantos, Robert C. Duncan, and Vinata B. Lokeshwar2 Departments of Urology [J. T. P., M. S. S., S. E., M. S., F. C., V. B. L.], Department of Epidemiology [R. C. D.], and Cell Biology and Anatomy [V. B. L.], University of Miami School of Medicine, Miami, Florida 33101 ABSTRACT lapse), local/systemic recurrence] in ϳ10–50% of cases, depending on a variety of prognostic factors (5–7). Treatment failure may be Despite the development of nomograms designed to evaluate the prog- attributable to a local recurrence or distant metastasis. Existing pre- nosis of a patient with prostate cancer (CaP), the information has been operative indicators (i.e., PSA levels, clinical stage, biopsy Gleason limited to prostate-specific antigen (PSA), clinical stage, Gleason score, and tumor volume estimates. To improve our ability to predict prognosis, sum) or their combination in nomograms, as well as surgical and ϩ Ϫ information regarding the molecular properties of CaP is needed. Hyalu- pathologic parameters (i.e., prostatectomy Gleason sum, margin / , ronic acid (HA) is a glycosaminoglycan that promotes tumor metastasis. node status, seminal vesicle, and EPE), provide a limited estimate of Hyaluronidase (HAase) is an enzyme that degrades HA into angiogenic the prognosis for CaP (8, 9). Identifying molecules that are expressed fragments. We recently showed that in CaP tissues, whereas HA is local- in clinically localized CaP but associate with CaP invasion and ized mostly in the tumor-associated stroma, HYAL1 type HAase is exclu- metastasis might significantly improve the prognostic capabilities and sively localized in CaP cells (Lokeshwar et al.
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HYAL1LUCA-1, a Candidate Tumor Suppressor Gene on Chromosome 3P21.3, Is Inactivated in Head and Neck Squamous Cell Carcinomas by Aberrant Splicing of Pre-Mrna
Oncogene (2000) 19, 870 ± 878 ã 2000 Macmillan Publishers Ltd All rights reserved 0950 ± 9232/00 $15.00 www.nature.com/onc HYAL1LUCA-1, a candidate tumor suppressor gene on chromosome 3p21.3, is inactivated in head and neck squamous cell carcinomas by aberrant splicing of pre-mRNA Gregory I Frost1,3, Gayatry Mohapatra2, Tim M Wong1, Antonei Benjamin CsoÂ ka1, Joe W Gray2 and Robert Stern*,1 1Department of Pathology, School of Medicine, University of California, San Francisco, California, CA 94143, USA; 2Cancer Genetics Program, UCSF Cancer Center, University of California, San Francisco, California, CA 94115, USA The hyaluronidase ®rst isolated from human plasma, genes in the process of carcinogenesis (Sager, 1997; Hyal-1, is expressed in many somatic tissues. The Hyal- Baylin et al., 1998). Nevertheless, functionally 1 gene, HYAL1, also known as LUCA-1, maps to inactivating point mutations are generally viewed as chromosome 3p21.3 within a candidate tumor suppressor the critical `smoking gun' when de®ning a novel gene locus de®ned by homozygous deletions and by TSG. functional tumor suppressor activity. Hemizygosity in We recently mapped the HYAL1 gene to human this region occurs in many malignancies, including chromosome 3p21.3 (CsoÂ ka et al., 1998), con®rming its squamous cell carcinomas of the head and neck. We identity with LUCA-1, a candidate tumor suppressor have investigated whether cell lines derived from such gene frequently deleted in small cell lung carcinomas malignancies expressed Hyal-1 activity, using normal (SCLC) (Wei et al., 1996). The HYAL1 gene resides human keratinocytes as controls. Hyal-1 enzyme activity within a commonly deleted region of 3p21.3 where a and protein were absent or markedly reduced in six of potentially informative 30 kb homozygous deletion has seven carcinoma cell lines examined.
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Datasheet: 50309954
Datasheet: 50309954 Description: NATIVE BOVINE HYALURONIDASE Name: HYALURONIDASE Format: Purified Product Type: Purified Protein Quantity: 0.5 g Product Details Applications This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit www.bio-rad-antibodies.com/protocols. Yes No Not Determined Suggested Dilution ELISA Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using the appropriate negative/positive controls. Target Species Bovine Product Form Purified enzyme from bovine testes - liquid Preservative None present Stabilisers Approx. Protein Total protein concentration 0.2 g/ml Concentrations External Database UniProt: Links Q8SQG8 Related reagents Q5E985 Related reagents Entrez Gene: 281838 HYAL2 Related reagents 515397 HYAL1 Related reagents Product Information Hyaluronidase catalyzes the depolymerization of mucopolysaccharides, hyaluronic acid, and the chondroitin sulfates A and C. The enzyme is widely distributed in animal tissues but is found in great concentrations in the bovine and ovine testes. Molecular Weight MW: 55 kD Activity 315 U/mg protein 1 unit is defined as the amount of enzyme that liberates one micromole of N-acetylglucosamine Page 1 of 2 per minute at 37ºC and pH 4.0. EC 3.2.1.36 Storage Store at -20oC only.
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HYAL1 and HYAL2 Inhibit Tumour Growth in Vivo but Not in Vitro
HYAL1 and HYAL2 Inhibit Tumour Growth In Vivo but Not In Vitro Fuli Wang1., Elvira V. Grigorieva1,2., Jingfeng Li1.¤, Vera N. Senchenko3, Tatiana V. Pavlova1,3, Ekaterina A. Anedchenko3, Anna V. Kudryavtseva3, Alexander Tsimanis4, Debora Angeloni5,6, Michael I. Lerman5, Vladimir I. Kashuba1,7, George Klein1, Eugene R. Zabarovsky1* 1 Microbiology and Tumour Biology Center, Karolinska Institute, Stockholm, Sweden, 2 Institute of Molecular Biology and Biophysics, SD RAMS, Novosibirsk, Russia, 3 Engelhardt Institute of Molecular Biology, Russian Acad. Sciences, Moscow, Russia, 4 Bioactivity Ltd., Rehovot, Israel, 5 Cancer-Causing Genes Section, Laboratory of Immunobiology, Center for Cancer Research, National Cancer Institute, Frederick, Maryland, United States of America, 6 Scuola Superiore Sant’Anna and Institute of Clinical Physiology – CNR, Pisa, Italy, 7 Institute of Molecular Biology and Genetics, Ukrainian Academy of Sciences, Kiev, Ukraine Abstract Background: We identified two 3p21.3 regions (LUCA and AP20) as most frequently affected in lung, breast and other carcinomas and reported their fine physical and gene maps. It is becoming increasingly clear that each of these two regions contains several TSGs. Until now TSGs which were isolated from AP20 and LUCA regions (e.g.G21/NPRL2, RASSF1A, RASSF1C, SEMA3B, SEMA3F, RBSP3) were shown to inhibit tumour cell growth both in vitro and in vivo. Methodology/Principal Findings: The effect of expression HYAL1 and HYAL2 was studied by colony formation inhibition, growth curve and cell proliferation tests in vitro and tumour growth assay in vivo. Very modest growth inhibition was detected in vitro in U2020 lung and KRC/Y renal carcinoma cell lines. In the in vivo experiment stably transfected KRC/Y cells expressing HYAL1 or HYAL2 were inoculated into SCID mice (10 and 12 mice respectively).
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Upregulation of the Microrna Cluster at the Dlk1-Dio3 Locus in Lung Adenocarcinoma
Oncogene (2015) 34, 94–103 & 2015 Macmillan Publishers Limited All rights reserved 0950-9232/15 www.nature.com/onc ORIGINAL ARTICLE Upregulation of the microRNA cluster at the Dlk1-Dio3 locus in lung adenocarcinoma PN Valdmanis1,2, B Roy-Chaudhuri1,2, HK Kim1,2, LC Sayles3, Y Zheng3, C-H Chuang2,4,5, DR Caswell2,4,5, K Chu1,2, Y Zhang1,2, MM Winslow2,4,5, EA Sweet-Cordero1,3,5 and MA Kay1,2 Mice in which lung epithelial cells can be induced to express an oncogenic KrasG12D develop lung adenocarcinomas in a manner analogous to humans. A myriad of genetic changes accompany lung adenocarcinomas, many of which are poorly understood. To get a comprehensive understanding of both the transcriptional and post-transcriptional changes that accompany lung adenocarcinomas, we took an omics approach in profiling both the coding genes and the non-coding small RNAs in an induced mouse model of lung adenocarcinoma. RNAseq transcriptome analysis of KrasG12D tumors from F1 hybrid mice revealed features specific to tumor samples. This includes the repression of a network of GTPase-related genes (Prkg1, Gnao1 and Rgs9) in tumor samples and an enrichment of Apobec1-mediated cytosine to uridine RNA editing. Furthermore, analysis of known single- nucleotide polymorphisms revealed not only a change in expression of Cd22 but also that its expression became allele specific in tumors. The most salient finding, however, came from small RNA sequencing of the tumor samples, which revealed that a cluster of B53 microRNAs and mRNAs at the Dlk1-Dio3 locus on mouse chromosome 12qF1 was markedly and consistently increased in tumors.
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Hyaluronan Synthases (HAS1-3) and Hyaluronidases (HYAL1-2) in The
Nykopp et al. BMC Cancer 2010, 10:512 http://www.biomedcentral.com/1471-2407/10/512 RESEARCH ARTICLE Open Access Hyaluronan synthases (HAS1-3) and hyaluronidases (HYAL1-2) in the accumulation of hyaluronan in endometrioid endometrial carcinoma Timo K Nykopp1,3, Kirsi Rilla2, Markku I Tammi2, Raija H Tammi2, Reijo Sironen1, Kirsi Hämäläinen1, Veli-Matti Kosma1, Seppo Heinonen3, Maarit Anttila3* Abstract Background: Hyaluronan accumulation correlates with the degree of malignancy in many solid tumor types, including malignant endometrial carcinomas. To elucidate the mechanism of hyaluronan accumulation, we examined the expression levels of the hyaluronan synthases (HAS1, HAS2 and HAS3) and hyaluronidases (HYAL1 and HYAL2), and correlated them with hyaluronan content and HAS1-3 immunoreactivity. Methods: A total of 35 endometrial tissue biopsies from 35 patients, including proliferative and secretory endometrium (n = 10), post-menopausal proliferative endometrium (n = 5), complex atypical hyperplasia (n = 4), grade 1 (n = 8) and grade 2 + 3 (n = 8) endometrioid adenocarcinomas were divided for gene expression by real- time RT-PCR, and paraffin embedded blocks for hyaluronan and HAS1-3 cytochemistry. Results: The mRNA levels of HAS1-3 were not consistently changed, while the immunoreactivity of all HAS proteins was increased in the cancer epithelium. Interestingly, HAS3 mRNA, but not HAS3 immunoreactivity, was increased in post-menopausal endometrium compared to normal endometrium (p = 0.003). The median of HYAL1 mRNA was 10-fold and 15-fold lower in both grade 1 and grade 2+3 endometrioid endometrial cancers, as compared to normal endometrium (p = 0.004-0.006), and post-menopausal endometrium (p = 0.002), respectively.
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HYAL1 (NM 153281) Human Tagged ORF Clone – RC212549 | Origene
OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 techsupport@origene.com EU: info-de@origene.com CN: techsupport@origene.cn Product datasheet for RC212549 HYAL1 (NM_153281) Human Tagged ORF Clone Product data: Product Type: Expression Plasmids Product Name: HYAL1 (NM_153281) Human Tagged ORF Clone Tag: Myc-DDK Symbol: HYAL1 Synonyms: HYAL-1; LUCA1; MPS9; NAT6 Vector: pCMV6-Entry (PS100001) E. coli Selection: Kanamycin (25 ug/mL) Cell Selection: Neomycin ORF Nucleotide >RC212549 ORF sequence Sequence: Red=Cloning site Blue=ORF Green=Tags(s) TTTTGTAATACGACTCACTATAGGGCGGCCGGGAATTCGTCGACTGGATCCGGTACCGAGGAGATCTGCC GCCGCGATCGCC ATGGCAGCCCACCTGCTTCCCATCTGCGCCCTCTTCCTGACCTTACTCGATATGGCCCAAGGCTTTAGGG GCCCCTTGCTACCCAACCGGCCCTTCACCACCGTCTGGAATGCAAACACCCAGTGGTGCCTGGAGAGGCA CGGTGTGGACGTGGATGTCAGTGTCTTCGATGTGGTAGCCAACCCAGGGCAGACCTTCCGCGGCCCTGAC ATGACAATTTTCTATAGCTCCCAGCTGGGCACCTACCCCTACTACACGCCCACTGGGGAGCCTGTGTTTG GTGGTCTGCCCCAGAATGCCAGCCTGATTGCCCACCTGGCCCGCACATTCCAGGACATCCTGGCTGCCAT ACCTGCTCCTGACTTCTCAGGGCTGGCAGTCATCGACTGGGAGGCATGGCGCCCACGCTGGGCCTTCAAC TGGGACACCAAGGACATTTACCGGCAGCGCTCACGGGCACTGGTACAGGCACAGCACCCTGATTGGCCAG CTCCTCAGGTGGAGGCAGTAGCCCAGGACCAGTTCCAGGGAGCTGCACGGGCCTGGATGGCAGGCACCCT CCAGCTGGGGCGGGCACTGCGTCCTCGCGGCCTCTGGGGCTTCTATGGCTTCCCTGACTGCTACAACTAT GACTTTCTAAGCCCCAACTACACCGGCCAGTGCCCATCAGGCATCCGTGCCCAAAATGACCAGCTAGGGT GGCTGTGGGGCCAGAGCCGTGCCCTCTATCCCAGCATCTACATGCCCGCAGTGCTGGAGGGCACAGGGAA GTCACAGATGTATGTGCAACACCGTGTGGCCGAGGCATTCCGTGTGGCTGTGGCTGCTGGTGACCCCAAT CTGCCGGTGCTGCCCTATGTCCAGATCTTCTATGACACGACAAACCACTTTCTGCCCCTGGATGAGCTGG
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Genome-Wide Association Study and Pathway Analysis for Female Fertility Traits in Iranian Holstein Cattle
Ann. Anim. Sci., Vol. 20, No. 3 (2020) 825–851 DOI: 10.2478/aoas-2020-0031 GENOME-WIDE ASSOCIATION STUDY AND PATHWAY ANALYSIS FOR FEMALE FERTILITY TRAITS IN IRANIAN HOLSTEIN CATTLE Ali Mohammadi1, Sadegh Alijani2♦, Seyed Abbas Rafat2, Rostam Abdollahi-Arpanahi3 1Department of Genetics and Animal Breeding, University of Tabriz, Tabriz, Iran 2Department of Animal Science, Faculty of Agriculture, University of Tabriz, Tabriz, Iran 3Department of Animal Science, University College of Abureyhan, University of Tehran, Tehran, Iran ♦Corresponding author: Sad-ali@tabrizu.ac.ir Abstract Female fertility is an important trait that contributes to cow’s profitability and it can be improved by genomic information. The objective of this study was to detect genomic regions and variants affecting fertility traits in Iranian Holstein cattle. A data set comprised of female fertility records and 3,452,730 pedigree information from Iranian Holstein cattle were used to predict the breed- ing values, which were then employed to estimate the de-regressed proofs (DRP) of genotyped animals. A total of 878 animals with DRP records and 54k SNP markers were utilized in the ge- nome-wide association study (GWAS). The GWAS was performed using a linear regression model with SNP genotype as a linear covariate. The results showed that an SNP on BTA19, ARS-BFGL- NGS-33473, was the most significant SNP associated with days from calving to first service. In total, 69 significant SNPs were located within 27 candidate genes. Novel potential candidate genes include OSTN, DPP6, EphA5, CADPS2, Rfc1, ADGRB3, Myo3a, C10H14orf93, KIAA1217, RBPJL, SLC18A2, GARNL3, NCALD, ASPH, ASIC2, OR3A1, CHRNB4, CACNA2D2, DLGAP1, GRIN2A and ME3.
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Improved Surface Display of Human Hyal1 and Identification of Testosterone Propionate and Chicoric Acid As New Inhibitors
pharmaceuticals Article Improved Surface Display of Human Hyal1 and Identification of Testosterone Propionate and Chicoric Acid as New Inhibitors Isabelle Lengers 1, Fabian Herrmann 2, Marc Le Borgne 3 and Joachim Jose 1,* 1 Institute of Pharmaceutical and Medicinal Chemistry, PharmaCampus, Westfälische Wilhelms-Universtität Münster, 48149 Münster, Germany; isabelle.lengers@uni-muenster.de 2 Institute of Pharmaceutical Biology and Phytochemistry, PharmaCampus, Westfälische Wilhelms-Universtität Münster, 48149 Münster, Germany; shermanic@uni-muenster.de 3 Université de Lyon, Université Claude Bernard Lyon 1, Faculté de Pharmacie—ISPB, EA 4446 Bioactive Molecules and Medicinal Chemistry, SFR Santé Lyon-Est CNRS UMS3453—INSERM US7, 8 Avenue Rockefeller, F-69373 Lyon CEDEX 8, France; marc.le-borgne@univ-lyon1.fr * Correspondence: joachim.jose@uni-muenster.de; Tel.: +49-251-83-32200 Received: 3 February 2020; Accepted: 24 March 2020; Published: 26 March 2020 Abstract: Degradation of high molecular weight hyaluronic acid (HA) in humans is mainly catalyzed by hyaluronidase Hyal1. This enzyme is involved in many pathophysiological processes and therefore appears an interesting target for drug discovery. Until now, only a few inhibitors of human Hyal1 are known due to obstacles in obtaining active enzymes for inhibitor screening. The aim of the present work was to provide a convenient enzyme activity assay and show its feasibility by the identification of new inhibitors. By autodisplay, Escherichia coli F470 can present active Hyal1 on its surface. In this study, the inducible expression of Hyal1 on the cell surface of E. coli under the control of a rhamnose-dependent promoter (Prha) was performed and optimized. Enzyme activity per single cell was increased by a factor of 100 compared to the constitutive Hyal1 surface display, as described before.
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Characterization of Mutations and Phenotypes Associated with HYAL2
Characterization of mutations and phenotypes associated with HYAL2 deficiency By S M Naimul Hasan A Thesis submitted to the Faculty of Graduate Studies of The University of Manitoba in partial fulfillment of the requirements of the degree of Master of Science Department of Biochemistry and Medical Genetics Faculty of Health Sciences University of Manitoba Winnipeg Copyright © 2017 by S M Naimul Hasan Abstract Hyaluronidase 2 (HYAL2) is an endoglycosidase involved in the cleavage of hyaluronic acid (HA). HA is abundantly present in the extracellular matrix (ECM) and reported to have a functional role during embryonic development. Abundant HA has been found in the provisional matrix of the developing skeleton, craniofacial mesenchyme, endocardial cushions and smooth muscles of the gastrointestinal tract of the mouse. Cardiac cushion explant experiments showed that high molecular mass HA promoted epithelial to mesenchymal transition (EMT) while small HA fragments inhibited EMT signaling and induced cellular proliferation. Recently through linkage analysis, followed by next generation sequencing and computational analysis, two separate HYAL2 mutations (K148R and P250L) were identified in Amish and Saudi Arabian families with the syndromic cleft palate. We hypothesize that mutations in HYAL2 cause deficiency of HYAL2 enzyme and increase HA levels in the craniofacial region. Elevated HA in the craniofacial area interferes with the differentiation of osteoblasts leading to decreased bone development. Comparison of the phenotypes of patients with HYAL2-mutations to the phenotype of the Hyal2-/- mouse from our lab showed similarities including cleft palate (submucosal with underdeveloped viscerocranial bones in mice), heart abnormalities and hearing loss. Functional studies of the mutated forms of HYAL2 expressed in HYAL2-deficient mouse embryonic fibroblasts (MEFs) showed that both mutations destabilized the HYAL2 protein and significantly reduced the HYAL2 level compared to the wild type.
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HYAL1 Hyaluronidase in Prostate Cancer: a Tumor Promoter and Suppressor
Research Article HYAL1 Hyaluronidase in Prostate Cancer: A Tumor Promoter and Suppressor Vinata B. Lokeshwar,1,2,4 Wolfgang H. Cerwinka,1 Tadahiro Isoyama,1 and Bal L. Lokeshwar1,3,4 Departments of 1Urology, 2Cell Biology and Anatomy, and 3Radiation Oncology, and 4Sylvester Comprehensive Cancer Center, Miller School of Medicine, University of Miami, Miami, Florida Abstract motility, and regulates cell adhesion, migration, and proliferation Hyaluronidases degrade hyaluronic acid, which promotes (1–3). Hyaluronic acid concentration is elevated in several tumors, metastasis. HYAL1 type hyaluronidase is an independent including carcinomas of breast, colon, prostate, and bladder (4–8). prognostic indicator of prostate cancer progression and a We have shown that increased urinary hyaluronic acid levels serve biomarker for bladder cancer. However, it is controversial as an accurate marker for detecting bladder cancer, regardless of the tumor grade (9, 10). In prostate cancer tissues, hyaluronic acid whether hyaluronidase (e.g., HYAL1) functions as a tumor f promoter or as a suppressor. We stably transfected prostate is mainly produced by tumor-associated stroma; however, 40% of cancer cells, DU145 and PC-3 ML, with HYAL1-sense tumor cells express hyaluronic acid (11, 12). Tumor-associated (HYAL1-S), HYAL1-antisense (HYAL1-AS), or vector DNA. hyaluronic acid promotes tumor cell migration, aids in the loss of contact inhibition, and offers protection against immune sur- HYAL1-AS transfectants were not generated for PC-3 ML because it expresses little HYAL1. HYAL1-S transfectants veillance (13–15). Small hyaluronic acid fragments (3-25 disaccha- produced V42 milliunits (moderate overproducers) or z80 ride units), generated by hyaluronidase, are angiogenic (16, 17).
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Hyaluronidase 1 Deficiency Preserves Endothelial Function and Glycocalyx
Page 1 of 32 Diabetes Hyaluronidase 1 deficiency preserves endothelial function and glycocalyx integrity in early streptozotocin-induced diabetes Sophie Dogné,1 Géraldine Rath,2 François Jouret,3 Nathalie Caron,1 Chantal Dessy,2* and Bruno Flamion,1* 1 Molecular Physiology Research Unit, NARILIS, University of Namur, Namur, Belgium; 2 Pole of Pharmacology and Therapeutics, IREC, Université catholique de Louvain, Brussels, Belgium; 3 Groupe Interdisciplinaire de Génoprotéomique Appliquée (GIGA), Cardiovascular Sciences, University of Liège, Liège, Belgium. * These authors contributed equally to the study Corresponding author: Sophie Dogné, Laboratory of Physiology & Pharmacology, University of Namur, 61 rue de Bruxelles, 5000 Namur, Belgium; Phone: +3281725660; Fax: +3281724329; sophie.dogne@unamur.be Short running title: HYAL1 deficiency protects the endothelium Word count of main text (max 4000 words): 4052 Number of Tables: 1 Number of Figures: 7 Diabetes Publish Ahead of Print, published online May 31, 2016 Diabetes Page 2 of 32 ABSTRACT (max. 200 words): 193 Hyaluronic acid (HA) is a major component of the glycocalyx involved in vascular wall and endothelial glomerular permeability barrier. Endocytosed hyaluronidase HYAL1 is known to degrade HA into small fragments in different cell types including endothelial cells. In diabetes, the size and permeability of the glycocalyx are altered. In addition, type 1 diabetic patients present increased plasma levels of both HA and HYAL1. To investigate the potential implication of HYAL1 in the development of diabetes-induced endothelium dysfunction, we measured endothelial markers, endothelium-dependent vasodilation, arteriolar glycocalyx size, and glomerular barrier properties in wild-type and HYAL1 knockout (KO) mice with or without streptozotocin-induced diabetes.
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