Alkaline Phosphatase, Calf Intestine

Total Page：16

File Type：pdf, Size：1020Kb

For Research Use Only. Not for use in diagnostic procedures. Rev: 07/15/2020 Alkaline Phosphatase, Calf Intestine CATALOG #: JM-7585-10 10 µg JM-7585-50 50 µg JM-7585-1000 1 mg ALTERNATE NAMES: ALP-1, ALPPL2, ALPPL, ALPP, ALP, PALP, PLAP, PLAP-1. SOURCE: Calf Intestine PURITY: ≥ 98% MOL. WEIGHT: 13 kDa FORM: Freeze dried powder RECONSTITUTION: Centrifuge the vial prior to opening. Reconstitute in distilled water or dilute buffer. Do not vortex. It is recommended to store it at -20°C. STORAGE CONDITIONS: Store at -20°C. After reconstitution, aliquot and store at -20°C. Avoid repeated freezing and thawing cycles. DESCRIPTION: Alkaline Phosphatase (ALP) is a hydrolase enzyme responsible for removing phosphate groups in the 5- and 3- positions from many types of molecules, including nucleotides, proteins, and alkaloids. In humans, alkaline phosphatase is present in all tissues throughout the entire body, but is particularly concentrated in liver, bile duct, kidney, bone, and the placenta. The optimal pH for the enzyme activity is pH 10 in standard conditions. There are at least four distinct but related alkaline phosphatases: intestinal, placental, placental-like, and liver/bone/kidney (tissue non-specific). The first three are located together on chromosome 2 while the tissue non- specific form is located on chromosome 1. The product of this gene is a membrane bound glycosylated enzyme, also referred to as the heat stable form that is expressed primarily in the placenta although it is closely related to the intestinal form of the enzyme as well as to the placental-like form. The coding sequence for this form of alkaline phosphatase is unique in that the 3' untranslated region contains multiple copies of an Alu family repeat. In addition, this gene is polymorphic and three common alleles (type 1, type 2 and type 3) for this form of alkaline phosphatase have been well characterized. ACTIVITY: 1,500-2,500 U/mg protein FOR RESEARCH USE ONLY! Not to be used in humans. 15A Constitution Way · Woburn, MA 01801 · Phone: 1.800.200.5459 · Fax: 781-939-6963 · www.mblintl.com .

Copy Link

Recommended publications

Epigenome-Wide Association Study of Wellbeing
Twin Research and Human Genetics Volume 18 Number 6 pp. 710–719 C The Author(s) 2015 doi:10.1017/thg.2015.85 Epigenome-Wide Association Study of Wellbeing Bart M. L. Baselmans,1,2 Jenny van Dongen,1,2 Michel G. Nivard,1 Bochao D. Lin,1 BIOS Consortium,3 Nuno R. Zilhao,˜ 1 Dorret I. Boomsma,1,2,4 and Meike Bartels1,2,4 1Department of Biological Psychology, VU University, Amsterdam, the Netherlands 2EMGO+ Institute for Health and Care Research, VU University Medical Center, Amsterdam, the Netherlands 3The Biobank-Based Integrative Omics Study (BIOS) Consortium 4Neuroscience Campus Amsterdam, Amsterdam, the Netherlands Wellbeing (WB) is a major topic of research across several scientific disciplines, partly driven by its strong association with psychological and mental health. Twin-family studies have found that both genotype and environment play an important role in explaining the variance in WB. Epigenetic mechanisms, such as DNA methylation, regulate gene expression, and may mediate genetic and environmental effects on WB. Here, for the first time, we apply an epigenome-wide association study (EWAS) approach to identify differentially methylated sites associated with individual differences in WB. Subjects were part of the longitudinal survey studies of the Netherlands Twin Register (NTR) and participated in the NTR biobank project between 2002 and 2011. WB was assessed by a short inventory that measures satisfaction with life (SAT). DNA methylation was measured in whole blood by the Illumina Infinium HumanMethylation450 BeadChip (HM450k array) and the association between WB and DNA methylation level was tested at 411,169 autosomal sites. Two sites (cg10845147, p = 1.51 ∗ 10-8 and cg01940273, p = 2.34 ∗ 10-8) reached genome-wide significance following Bonferonni correction.
[Show full text]
Anti-ALPPL2 Antibody (ARG58232)
Product datasheet [email protected] ARG58232 Package: 100 μl anti-ALPPL2 antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes ALPPL2 Tested Reactivity Hu, Ms Tested Application WB Host Rabbit Clonality Polyclonal Isotype IgG Target Name ALPPL2 Antigen Species Human Immunogen Recombinant fusion protein corresponding to aa. 20-280 of Human ALPPL2 (NP_112603.2). Conjugation Un-conjugated Alternate Names Alkaline phosphatase, placental-like; Placental alkaline phosphatase-like; PLAP-like; EC 3.1.3.1; Germ cell alkaline phosphatase; ALPG; Alkaline phosphatase Nagao isozyme; ALP-1; ALPPL; GCAP Application Instructions Application table Application Dilution WB 1:500 - 1:2000 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Positive Control HeLa Calculated Mw 57 kDa Observed Size 70 kDa Properties Form Liquid Purification Affinity purified. Buffer PBS (pH 7.3), 0.02% Sodium azide and 50% Glycerol. Preservative 0.02% Sodium azide Stabilizer 50% Glycerol Storage instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. Note For laboratory research only, not for drug, diagnostic or other use. www.arigobio.com 1/2 Bioinformation Gene Symbol ALPPL2 Gene Full Name alkaline phosphatase, placental-like 2 Background There are at least four distinct but related alkaline phosphatases: intestinal, placental, placental-like, and liver/bone/kidney (tissue non-specific).
[Show full text]
Myopia Genetics Report
Special Issue IMI – Myopia Genetics Report Milly S. Tedja,1,2 Annechien E. G. Haarman,1,2 Magda A. Meester-Smoor,1,2 Jaakko Kaprio,3,4 David A. Mackey,5–7 Jeremy A. Guggenheim,8 Christopher J. Hammond,9 Virginie J. M. Verhoeven,1,2,10 and Caroline C. W. Klaver1,2,11; for the CREAM Consortium 1Department of Ophthalmology, Erasmus Medical Center, Rotterdam, the Netherlands 2Department of Epidemiology, Erasmus Medical Center, Rotterdam, the Netherlands 3Institute for Molecular Medicine, University of Helsinki, Helsinki, Finland 4Department of Public Health, University of Helsinki, Helsinki, Finland 5Centre for Eye Research Australia, Ophthalmology, Department of Surgery, University of Melbourne, Royal Victorian Eye and Ear Hospital, Melbourne, Victoria, Australia 6Department of Ophthalmology, Menzies Institute of Medical Research, University of Tasmania, Hobart, Tasmania, Australia 7Centre for Ophthalmology and Visual Science, Lions Eye Institute, University of Western Australia, Perth, Western Australia, Australia 8School of Optometry and Vision Sciences, Cardiff University, Cardiff, United Kingdom 9Section of Academic Ophthalmology, School of Life Course Sciences, King’s College London, London, United Kingdom 10Department of Clinical Genetics, Erasmus Medical Center, Rotterdam, the Netherlands 11Department of Ophthalmology, Radboud University Medical Center, Nijmegen, the Netherlands Correspondence: Caroline C. W. The knowledge on the genetic background of refractive error and myopia has expanded Klaver, Erasmus Medical Center, dramatically in the past few years. This white paper aims to provide a concise summary of Room Na-2808, P.O. Box 2040, 3000 current genetic ﬁndings and deﬁnes the direction where development is needed. CA, Rotterdam, the Netherlands; [email protected]. We performed an extensive literature search and conducted informal discussions with key MST and AEGH contributed equally to stakeholders.
[Show full text]
Genomic and Expression Profiling of Human Spermatocytic Seminomas: Primary Spermatocyte As Tumorigenic Precursor and DMRT1 As Candidate Chromosome 9 Gene
Research Article Genomic and Expression Profiling of Human Spermatocytic Seminomas: Primary Spermatocyte as Tumorigenic Precursor and DMRT1 as Candidate Chromosome 9 Gene Leendert H.J. Looijenga,1 Remko Hersmus,1 Ad J.M. Gillis,1 Rolph Pfundt,4 Hans J. Stoop,1 Ruud J.H.L.M. van Gurp,1 Joris Veltman,1 H. Berna Beverloo,2 Ellen van Drunen,2 Ad Geurts van Kessel,4 Renee Reijo Pera,5 Dominik T. Schneider,6 Brenda Summersgill,7 Janet Shipley,7 Alan McIntyre,7 Peter van der Spek,3 Eric Schoenmakers,4 and J. Wolter Oosterhuis1 1Department of Pathology, Josephine Nefkens Institute; Departments of 2Clinical Genetics and 3Bioinformatics, Erasmus Medical Center/ University Medical Center, Rotterdam, the Netherlands; 4Department of Human Genetics, Radboud University Medical Center, Nijmegen, the Netherlands; 5Howard Hughes Medical Institute, Whitehead Institute and Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts; 6Clinic of Paediatric Oncology, Haematology and Immunology, Heinrich-Heine University, Du¨sseldorf, Germany; 7Molecular Cytogenetics, Section of Molecular Carcinogenesis, The Institute of Cancer Research, Sutton, Surrey, United Kingdom Abstract histochemistry, DMRT1 (a male-specific transcriptional regulator) was identified as a likely candidate gene for Spermatocytic seminomas are solid tumors found solely in the involvement in the development of spermatocytic seminomas. testis of predominantly elderly individuals. We investigated these tumors using a genome-wide analysis for structural and (Cancer Res 2006; 66(1): 290-302) numerical chromosomal changes through conventional kar- yotyping, spectral karyotyping, and array comparative Introduction genomic hybridization using a 32 K genomic tiling-path Spermatocytic seminomas are benign testicular tumors that resolution BAC platform (confirmed by in situ hybridization).
[Show full text]
Genomic Sequencing and Analysis of a Chinese Hamster Ovary Cell Line
Hammond et al. BMC Genomics 2011, 12:67 http://www.biomedcentral.com/1471-2164/12/67 RESEARCHARTICLE Open Access Genomic sequencing and analysis of a Chinese hamster ovary cell line using Illumina sequencing technology Stephanie Hammond1,2, Jeffrey C Swanberg1,2, Mihailo Kaplarevic2, Kelvin H Lee1,2* Abstract Background: Chinese hamster ovary (CHO) cells are among the most widely used hosts for therapeutic protein production. Yet few genomic resources are available to aid in engineering high-producing cell lines. Results: High-throughput Illumina sequencing was used to generate a 1x genomic coverage of an engineered CHO cell line expressing secreted alkaline phosphatase (SEAP). Reference-guided alignment and assembly produced 3.57 million contigs and CHO-specific sequence information for ~ 18,000 mouse and ~ 19,000 rat orthologous genes. The majority of these genes are involved in metabolic processes, cellular signaling, and transport and represent attractive targets for cell line engineering. Conclusions: This demonstrates the applicability of next-generation sequencing technology and comparative genomic analysis in the development of CHO genomic resources. Background currently used to examine differential expression of With over half of all recombinant therapeutic proteins high-producing cell lines and to identify gene candidates produced in mammalian cell lines, Chinese hamster for host cell engineering [5-7]. Transcriptomic studies ovary (CHO) cells remain the predominant production which rely on cross-hybridization to mouse DNA micro- system for glycosylated biopharmaceuticals [1]. Although arrays showed some success [8,9], but also demonstrated improvements in cell engineering, cell line selection, and the need for CHO-specific sequence information. Con- culture conditions have increased productivity levels [2], tinued EST sequencing of CHO cells lines has generated the genetic basis underlying hyperproductivity remains databases containing more than 60,000 sequences and poorly defined.
[Show full text]
Tissue-Nonspecific Alkaline Phosphatase
biomolecules Review Tissue-Nonspecific Alkaline Phosphatase— A Gatekeeper of Physiological Conditions in Health and a Modulator of Biological Environments in Disease Daniel Liedtke 1,* , Christine Hofmann 2, Franz Jakob 3, Eva Klopocki 1 and Stephanie Graser 3 1 Institute for Human Genetics, Biocenter, Julius-Maximilians-University Würzburg, 97074 Würzburg, Germany; [email protected] 2 Section of Pediatric Rheumatology and Osteology, University Children’s Hospital of Würzburg, 97080 Würzburg, Germany; [email protected] 3 Bernhard-Heine-Center for Locomotion Research, Julius-Maximilians-University Würzburg, 97076 Würzburg, Germany; [email protected] (F.J.); [email protected] (S.G.) * Correspondence: [email protected] Received: 30 October 2020; Accepted: 5 December 2020; Published: 8 December 2020 Abstract: Tissue-nonspecific alkaline phosphatase (TNAP) is a ubiquitously expressed enzyme that is best known for its role during mineralization processes in bones and skeleton. The enzyme metabolizes phosphate compounds like inorganic pyrophosphate and pyridoxal-50-phosphate to provide, among others, inorganic phosphate for the mineralization and transportable vitamin B6 molecules. Patients with inherited loss of function mutations in the ALPL gene and consequently altered TNAP activity are suffering from the rare metabolic disease hypophosphatasia (HPP). This systemic disease is mainly characterized by impaired bone and dental mineralization but may also be accompanied by neurological symptoms, like anxiety disorders, seizures, and depression. HPP characteristically affects all ages and shows a wide range of clinical symptoms and disease severity, which results in the classification into different clinical subtypes. This review describes the molecular function of TNAP during the mineralization of bones and teeth, further discusses the current knowledge on the enzyme’s role in the nervous system and in sensory perception.
[Show full text]
Myopia Genetics Report
Special Issue IMI – Myopia Genetics Report Milly S. Tedja,1,2 Annechien E. G. Haarman,1,2 Magda A. Meester-Smoor,1,2 Jaakko Kaprio,3,4 David A. Mackey,5–7 Jeremy A. Guggenheim,8 Christopher J. Hammond,9 Virginie J. M. Verhoeven,1,2,10 and Caroline C. W. Klaver1,2,11; for the CREAM Consortium 1Department of Ophthalmology, Erasmus Medical Center, Rotterdam, the Netherlands 2Department of Epidemiology, Erasmus Medical Center, Rotterdam, the Netherlands 3Institute for Molecular Medicine, University of Helsinki, Helsinki, Finland 4Department of Public Health, University of Helsinki, Helsinki, Finland 5Centre for Eye Research Australia, Ophthalmology, Department of Surgery, University of Melbourne, Royal Victorian Eye and Ear Hospital, Melbourne, Victoria, Australia 6Department of Ophthalmology, Menzies Institute of Medical Research, University of Tasmania, Hobart, Tasmania, Australia 7Centre for Ophthalmology and Visual Science, Lions Eye Institute, University of Western Australia, Perth, Western Australia, Australia 8School of Optometry and Vision Sciences, Cardiff University, Cardiff, United Kingdom 9Section of Academic Ophthalmology, School of Life Course Sciences, King’s College London, London, United Kingdom 10Department of Clinical Genetics, Erasmus Medical Center, Rotterdam, the Netherlands 11Department of Ophthalmology, Radboud University Medical Center, Nijmegen, the Netherlands Correspondence: Caroline C. W. The knowledge on the genetic background of refractive error and myopia has expanded Klaver, Erasmus Medical Center, dramatically in the past few years. This white paper aims to provide a concise summary of Room Na-2808, P.O. Box 2040, 3000 current genetic ﬁndings and deﬁnes the direction where development is needed. CA, Rotterdam, the Netherlands; [email protected]. We performed an extensive literature search and conducted informal discussions with key MST and AEGH contributed equally to stakeholders.
[Show full text]
Mapping Mrna Libraries
Mapping mRNA libraries STAR-2.5.2b was used with options shown below. Index generation: $STAR --runThreadN 16 \ --runMode genomeGenerate \ --genomeDir $IndexPref \ --genomeFastaFiles $GenomePref/Mus_musculus.GRCm38.dna.primary_assembly.fa \ --sjdbGTFfile $AnnoPref/Mus_musculus.GRCm38.86.gtf \ --sjdbOverhang 100 Aligning and counting reads with the genes (annotated transcripts): $STAR --runThreadN 8 \ --runMode alignReads \ --genomeDir $IndexPref \ --readFilesIn $FileOne $FileTwo \ --outFileNamePrefix $OutDir \ --outFilterType BySJout \ --outFilterMismatchNoverLmax 0.05 \ --alignSJoverhangMin 8 \ --alignSJDBoverhangMin 1 \ --alignIntronMin 20 \ --alignMatesGapMax 1000000 \ --outSAMtype BAM SortedByCoordinate Complex homology groups discussed in this paper Modencode project declares more homology pairs than homologene. When we combine homology pairs from different sources there exists a potential for amplifying the number of incorrect homology pairs, therefore here we review the complex homology groups that are mentioned in the paper. Homology of genes is defined on the basis of the evolutionary history of genomes which cannot be easily assessed by looking at the data from two species, but we can compare clues from synteny and expression profiles. While we see many differences in expression profiles among members of the same homology group, given a choice of different sets of homology pairs we prefer one that explains more cases of high gene expressions with homology. These homology groups were included in our specific findings while they are not consistently identified by modencode and homologene: • Alkaline phosphatases • Amylases • Kallikrein 1-related peptidases • Defensins with high expression in mouse skin and vagina More authoritative methods to determine homology collect information from many species. However, we use a method which allows to choose most plausible homology when we have two-three alternatives.
[Show full text]
Epigenome-450K-Wide Methylation Signatures of Active Cigarette Smoking: the Young Finns Study
Bioscience Reports (2020) 40 BSR20200596 https://doi.org/10.1042/BSR20200596 Research Article Epigenome-450K-wide methylation signatures of active cigarette smoking: The Young Finns Study Pashupati P. Mishra1,2,3,*, Ismo Hanninen¨ 1,2,3,*, Emma Raitoharju1,2,3, Saara Marttila1,2,3,4, Binisha H. Mishra1,2,3, Nina Mononen1,2,3,MikaKah¨ onen¨ 2,5, Mikko Hurme4,6, Olli Raitakari7,8,9, Petri Tor¨ onen¨ 10, Liisa Holm10,11 and Terho Lehtimaki¨ 1,2,3 Downloaded from http://portlandpress.com/bioscirep/article-pdf/40/7/BSR20200596/887717/bsr-2020-0596.pdf by guest on 27 September 2021 1Department of Clinical Chemistry, Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland; 2Finnish Cardiovascular Research Center-Tampere, Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland; 3Department of Clinical Chemistry, Fimlab Laboratories, Tampere, Finland; 4Gerontology Research Center (GEREC), Tampere University, Tampere, Finland; 5Department of Clinical Physiology, Tampere University Hospital, Tampere, Finland; 6Department of Microbiology and Immunology, Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland; 7Centre for Population Health Research, University of Turku and Turku University Hospital, Turku, Finland; 8Research Centre of Applied and Preventive Cardiovascular Medicine, University of Turku, Turku, Finland; 9Department of Clinical Physiology and Nuclear Medicine, Turku University Hospital, Turku, Finland; 10Institute of Biotechnology, Helsinki Institute of Life Sciences (HiLife), University of Helsinki, Helsinki, Finland; 11Organismal and Evolutionary Biology Research Program, Faculty of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland Correspondence: Pashupati P. Mishra (pashupati.mishra@tuni.ﬁ) Smoking as a major risk factor for morbidity affects numerous regulatory systems of the human body including DNA methylation.
[Show full text]
ALPPL2 (9-YD35): Sc-134255
SANTA CRUZ BIOTECHNOLOGY, INC. ALPPL2 (9-YD35): sc-134255 BACKGROUND APPLICATIONS ALPPL2 (alkaline phosphatase, placental-like 2), also known as ALPG, GCAP or ALPPL2 (9-YD35) is recommended for detection of ALPPL2 of human origin ALPPL, is a 532 amino acid protein that is lipid-anchored to the cell membrane by Western Blotting (starting dilution 1:200, dilution range 1:100-1:1000), and belongs to the alkaline phosphatase family. Expressed at low levels in immunoprecipitation [1-2 µg per 100-500 µg of total protein (1 ml of cell thymus and testis, ALPPL2 functions as a homodimer that uses magnesium and lysate)], immunofluorescence (starting dilution 1:50, dilution range 1:50- zinc as cofactors to catalyze the conversion of a phosphate monoester to an 1:500), immunohistochemistry (including paraffin-embedded sections) alcohol and a free phosphate. ALPPL2 is overexpressed in germ cell tumors, (starting dilution 1:50, dilution range 1:50-1:500) and solid phase ELISA suggesting a role in tumor development and progression. The gene encoding (starting dilution 1:30, dilution range 1:30-1:3000). ALPPL2 maps to human chromosome 2, which houses over 1,400 genes and Suitable for use as control antibody for ALPPL2 siRNA (h): sc-105390, comprises nearly 8% of the human genome. Harlequin icthyosis, a rare and ALPPL2 shRNA Plasmid (h): sc-105390-SH and ALPPL2 shRNA (h) Lentiviral morbid skin deformity, is associated with mutations in the ABCA12 gene, while Particles: sc-105390-V. the lipid metabolic disorder sitosterolemia is associated with defects in the ABCG5 and ABCG8 genes. Additionally, an extremely rare recessive genetic Molecular Weight of ALPPL2: 57 kDa.
[Show full text]
Alkaline Phosphatase (ALPPL2) Rabbit Polyclonal Antibody 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 TA308201 Alkaline Phosphatase (ALPPL2) Rabbit Polyclonal Antibody Product data: Product Type: Primary Antibodies Applications: IF, IHC, WB Recommended Dilution: ICC/IF:1:100-1:1000; IHC:1:100-1:1000; WB:1:500-1:3000 Reactivity: Human (Predicted: Mouse) Host: Rabbit Isotype: IgG Clonality: Polyclonal Immunogen: Recombinant fragment contain a sequence corresponding to a region within amino acids 46 and 344 of ALPPL2 (Uniprot ID#P10696) Formulation: 0.1M Tris, 0.1M Glycine, 20% Glycerol (pH7). 0.01% Thimerosal was added as a preservative. Concentration: lot specific Purification: Purified by antigen-affinity chromatography. Conjugation: Unconjugated Storage: Store at -20°C as received. Stability: Stable for 12 months from date of receipt. Predicted Protein Size: 57 kDa Gene Name: alkaline phosphatase, placental like 2 Database Link: NP_112603 Entrez Gene 11650 MouseEntrez Gene 251 Human P10696 Background: There are at least four distinct but related alkaline phosphatases: intestinal, placental, placental-like, and liver/bone/kidney (tissue non-specific). The product of this gene is a membrane bound glycosylated enzyme, localized to testis, thymus and certain germ cell tumors, that is closely related to both the placental and intestinal forms of alkaline phosphatase. [provided by RefSeq] Synonyms: ALPG; ALPPL; GCAP Note: Seq homology of immunogen across species: Mouse (80%) This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 1 / 3 Alkaline Phosphatase (ALPPL2) Rabbit Polyclonal Antibody – TA308201 Protein Families: Druggable Genome Protein Pathways: Folate biosynthesis, Metabolic pathways Product images: Sample (30 ug of whole cell lysate).
[Show full text]
Large-Scale Gene Expression Analysis of Osteoblasts Cultured on Three Different Ti–6Al–4V Surface Treatments Ching-Hsin Kua,B, Martin Browneb, Peter J
CORE Metadata, citation and similar papers at core.ac.uk Provided by Infoscience - École polytechnique fédérale de Lausanne Biomaterials 23 (2002) 4193–4202 Large-scale gene expression analysis of osteoblasts cultured on three different Ti–6Al–4V surface treatments Ching-Hsin Kua,b, Martin Browneb, Peter J. Gregsonb, Jacques Corbeild, Dominique P. Piolettia,c,* a Bone Bioengineering Group, Institute for Biomedical Engineering, Swiss Federal Institute of Technology, Lausanne, Switzerland b Bioengineering Sciences Research Group, School of Engineering Sciences, University of Southampton, Southampton, UK c Orthopaedic Hospital, Lausanne, Switzerland d Department of Medicine, University of California, San Diego and San Diego Veterans Affairs, Healthcare System, La Jolla, USA Received 24 October 2001 Abstract To improve implant biocompatibility, we developed a simple cost-effective thermal surface treatment allowing an increase in the oxide layer thickness of a titanium (Ti) alloy used in orthopaedic implants. The goal of this study was to test in vitro the reaction of osteoblasts to the developed surface treatment and to compare it to the osteoblast reaction to two other surface treatments currently used in the practice of implant surgery. Quantiﬁcation of osteoblast gene expression on a large scale was used in this study. The kinetics of gene expression over 120 h was followed for 58 genes to quantify the effect of the developed surface treatment. Twenty eight genes were further selected to compare the effects of surface treatments on osteoblasts. Based on the genes studied, we could propose a general pathway for the cell reaction according to the surface treatments used: (1) metal ion release changes the time course of gene expression in the FAK pathway; (2) once the accumulation of metal ions released from the Ti surface exceeds a threshold value, cell growth is diminished and apoptosis may be activated; (3) PTK up-regulation is also induced by metal ion release; (4) the expression of Bcl-2 family and Bax may suggest that metal ions induce apoptosis.
[Show full text]