Effect of non-surgical periodontal therapy (NSPT) on salivary and serum levels of a disintegrin-like and metalloproteinase with thrombospondin-1 (ADAMTS-1)

https://doi.org/10.53730/ijhs.v6nS1.8348

Authors

  • Kirti Anil Shetgaonkar Post-graduate student, Department of Periodontology
  • Girish Suragimath Professor and Head, Department of Periodontology
  • A. Siddhartha Varma Reader, Department of Periodontology
  • Sameer A. Zope Reader, Department of Periodontology
  • Ashwinirani SR Senior lecturer, Department of Oral Medicine and Radiology

Keywords:

ADAMTS-1, Clinical attachment level, Non-Surgical Periodontal Therapy, Periodontitis, Probing pocket depth, Saliva, Serum

Abstract

Objectives: A Disintegrin -like and Metalloproteinase with Thrombospondin-1 (ADAMTS-1) is a protease with structure similar to Matrix metalloproteinase. ADAMTS-1 has role in wound healing, fibroblast migration, tissue modeling, vasculogenesis and development of neuronal system. The levels of ADAMTS-1 vary in periodontal health and disease. To evaluate the effect of Non-Surgical Periodontal Therapy (NSPT) on salivary and serum ADAMTS-1 levels in generalized periodontitis patients. Methodology: Forty-five subjects suffering from generalized periodontitis were selected and periodontal parameters were assessed using periodontal probing depth (PPD) and clinical attachment level (CAL). Salivary and serum ADAMTS-1 levels were assessed using enzyme-linked immunosorbent assay. NSPT was performed involving scaling and root planning, followed by oral hygiene instructions. The patients were recalled after three months, periodontal parameters and ADMATS-1 levels were analyzed. Pre- NSPT levels of periodontal parameters and ADAMTS-1 levels were compared with post NSPT. Descriptive statistics and paired t-test were applied to compare the variables. P-value < 0.05 was considered statistically significant. Results: Serum ADAMTS-1 levels pre NSPT was 119.45ng/L and elevated post NSPT to 143.43ng/L. The salivary ADAMTS-1 at baseline was 157.81 and post NSPT 161.53 ng/L and both the values were statistically significant post NSPT.

Downloads

Download data is not yet available.

References

Krampert M, Kuenzle S, Thai SN-M, Lee N, Iruela-Arispe ML, Werner S. ADAMTS1 proteinase is up-regulated in wounded skin and regulates migration of fibroblasts and endothelial cells. J Biol Chem. 2005;280(25):23844–52.

Kinane DF, Stathopoulou PG, Papapanou PN. Periodontal diseases. Nat Rev Dis Primers. 2017;3:17038.

Tan I de A, Ricciardelli C, Russell DL. The metalloproteinase ADAMTS1: a comprehensive review of its role in tumorigenic and metastatic pathways: The metalloproteinase ADAMTS1. Int J Cancer. 2013;133(10):2263–76.

Kuno K, Kanada N, Nakashima E, Fujiki F, Ichimura F, Matsushima K. Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene. J Biol Chem. 1997;272(1):556–62.

Mittaz L, Russell DL, Wilson T, Brasted M, Tkalcevic J, Salamonsen LA, et al. Adamts-1 is essential for the development and function of the urogenital system. Biol Reprod [Internet]. 2004;70(4):1096–105.

Brown HM, Dunning KR, Robker RL, Pritchard M, Russell DL. Requirement for ADAMTS-1 in extracellular matrix remodeling during ovarian folliculogenesis and lymphangiogenesis. Dev Biol [Internet]. 2006;300(2):699–709.

Porter S, Clark IM, Kevorkian L, Edwards DR. The ADAMTS metalloproteinases. Biochem J. 2005;386(Pt 1):15–27.Table 1.

Kaushal GP, Shah SV. The new kids on the block: ADAMTSs, potentially multifunctional metalloproteinases of the ADAM family. J Clin Invest [Internet]. 2000;105(10):1335–7.

Yang G, Yao G, Xu Z, Fan H, Liu X, He J, et al. Expression level of ADAMTS1 in granulosa cells of PCOS patients is related to granulosa cell function, oocyte quality, and embryo development. Front Cell Dev Biol. 2021;9:647522

Park M, Park SH, Park H, Kim H-R, Lim HJ, Song H. ADAMTS-1: a novel target gene of an estrogen-induced transcription factor, EGR1, critical for embryo implantation in the mouse uterus. Cell Biosci. 2021;11(1):155.

Rose KWJ, Taye N, Karoulias SZ, Hubmacher D. Regulation of ADAMTS proteases. Front Mol Biosci. 2021;8:701959.

Tang BL. ADAMTS: a novel family of extracellular matrix proteases. Int J Biochem Cell Biol. 2001;33:33–44.

Kuno K, Iizasa H, Ohno S, Matsushima K. The exon/intron organization and chromosomal mapping of the mouse ADAMTS-1 gene encoding an ADAM family protein with TSP motifs. Genomics. 1997;46:466–71.

Kuno K, Matsushima K. ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region. J Biol Chem. 1998;273:13912–13917.

Bevitt D J, Mohamed J, Catterall JB, Li Z, Arris CE, Hiscott P, McKie N. Expression of ADAMTS metalloproteinases in the retinal pigment epithelium derived cell line ARPE-19: transcriptional regulation by TNFα. Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 2003;1626: 83–91.

Ozler S, Demircan K. The investigation of the role of proteoglycans and ADAMTS levels in fetal membranes in physiopathological process of gestational diabetes. Med Hypotheses 2017;104:182-4.

Yung Y, Maman E, Konopnicki S, Cohen B, Brengauz M, Lojkin I, et al. ADAMTS-1: a new human ovulatory gene and a cumulus marker for fertilization capacity. Mol Cell Endocrinol 2010; 328: 104-8.

Young KA, Tumlinson B, Stouffer RL. ADAMTS-1/METH-1 and TIMP3 expression in the primate corpus luteum: divergent patterns and stage-dependent regulation during the natural menstrual cycle. Mol Hum Reprod 2004; 10: 559-65.

Kornman K. S., Crane A., Wang H. Y., di Giovine F. S., Newman M. G., Pirk F. W., Wilson, Jr T. G., Higginbottom F. L., Duff G. W. The interleukin-1 genotype as a severity factor in adult periodontal disease. J. Clin. Periodontol. 1997;24:72–77.

Diaz PS, Solar PA, Juica NE, Orihuela PA, Cardenas H, Christodoulides M, et al. Differential expression of extracellular matrix components in the Fallopian tubes throughout the menstrual cycle. Reprod Biol Endocrinol. 2012; 10: 56.

Pyun JA, Kim S, Cho NH, Koh I, Lee JY, Shin C, Kwack K. Genomewide association studies and epistasis analyses of candidate genes related to age at menarche and age at natural menopause in a Korean population. Menopause. 2014; 21: 522-9.

Koller DL, Ichikawa S, Lai D, Padgett LR, Doheny KF, Pugh E, et al. Genome-wide association study of bone mineral density in premenopausal European-American women and replication in African-American women. J Clin Endocrinol Metab. 2010; 95: 1802- 9.

Keightley MC, Sales KJ, Jabbour HN. PGF2alpha-F-prostanoid receptor signalling via ADAMTS1 modulates epithelial cell invasion and endothelial cell function in endometrial cancer. BMC Cancer. 2010; 10: 488

Gao YX, Yu CA, Lu JH, Gao HM, Li G Kong W, Zheng JA. ADAMTS-7 Expression Increases in the Early Stage of Angiotensin II-Induced Renal Injury in Elderly Mice. Kidney and Blood Pressure Research. 2013; 38: 121–131.

El Hour M, Moncada-Pazos A, Blacher S, et al. Higher sensitivity of Adamts12-deficient mice to tumor growth and angiogenesis. Oncogene. 2010;29:3025–32.

M Shozu, N Minami, H Yokoyama, M Inoue1, H Kurihara, K Matsushima, K Kuno. ADAMTS-1 is involved in normal follicular development, ovulatory process and organization of the medullary vascular network in the ovary. J. Mol. Endocrinol. 2005;35: 343-55.

Vázquez F, Hastings G, Ortega MA, Lane TF, Oikemus S, Lombardo M, Iruela-Arispe ML. METH-1, a Human Ortholog of ADAMTS-1, and METH-2 Are Members of a New Family of Proteins with Angio-inhibitory Activity. J Biol Chem. 1999; 274(33), 23349–23357

Iruela-Arispe M L, Carpizo D, Luque A. ADAMTS1: A Matrix Metalloprotease with Angioinhibitory Properties. Ann NY Acad Sci. 2003; 995: 183–190.

Kuno K, Bannai K, Hakozaki M, Matsushima K, Hirose K. The carboxyl-terminal half region of ADAMTS-1 suppresses both tumorigenicity and experimental tumor metastatic potential. Biochem Biophys Res Commun. 2004;319(4):1327-33

Mittaz L, Russell D L, Wilson T, Brasted M. Tkalcevic J, Salamonsen LA et al. Adamts-1 Is Essential for the Development and Function of the Urogenital System1. Biol. Reprod. 2004;70: 1096–105.

Lee NV, Sato M, Annis DS, Loo JA, Wu L, Mosher DF, Iruela-Arispe ML. ADAMTS1 mediates the release of antiangiogenic polypeptides from TSP1 and 2. EMBO J. 2006 Nov 15;25(22):5270-83. doi: 10.1038/sj.emboj.7601400. PMID: 17082774; PMCID: PMC1636613.

Misra S, Lee N, Fu AA, et al. Increased expression of a disintegrin and metalloproteinase thrombospondin 1 in thrombosed hemodialysis grafts. J Vasc Interv Radiol 2008;19:111–9.

Rocks N, Paulissen G, Quesada-Calvo F, et al. ADAMTS-1 metalloproteinase promotes tumor development through the induction of a stromal reaction in vivo. Cancer Res 2008;68:9541–50.

Günther W, Skaftnesmo KO, Arnold H, Bjerkvig R, Terzis AJ. Distribution patterns of the anti-angiogenic protein ADAMTS-1 during rat development. Acta Histochem. 2005;107:121-31.

Gustavsson H, Wang W, Jennbacken K, et al. ADAMTS1, a putative anti-angiogenic factor, is decreased in human prostate cancer. BJU Int. 2009;104:1786–90.

Ricciardelli C, Frewin KM, Tan Ide A, et al. The ADAMTS1 protease gene is required for mammary tumor growth and metastasis. Am J Pathol. 2011;179:3075–85

Batista NMG , Moraes A , Balbinot K M, de Souza Neto O R , Brandão JM, kataoka SM. Immunohistochemical analysis of ADAMTS-1, versican and pEGFR expressions in periapical granuloma and radicular cyst. BMC Oral Health. 2021; 21: 102.

Rapraeger AC. Syndecan-regulated receptor signaling. J Cell Biol. 2000; 149(5):995-8

Brown hm, dunning kr, robker rl, et al. requirement for adamts-1 in extracellular matrix remodeling during ovarian folliculogenesis and lymphangiogenesis. dev biol 2006;300:699–709.

Chapple ILC, Matthews JB, Thorpe GHG, Glenwright HD, Smith JM, and Saxby M. A new ultrasensitive chemiluminescent assay for the site-specific quantification of alkaline phosphatase in gingival crevicular fluid. J Periodontal Res 1993; 28:4:266–273

Contreras A., Slots J. Herpesviruses in human periodontal disease. J. Periodontal Res. 2000;35:3–16

Lin SJ, Chen YL, Kuo MY, Li CL, Lu HK. Measurement of gp130 cytokines oncostatin M and IL-6 in gingival crevicular fluid of patients with chronic periodontitis. Cytokine. 2005; 21;30(4):160-167

Lamster IB, Oshrain RL, Fiorello LA, Celenti RS, Gordon JM. A comparison of 4 methods of data presentation for lysosomal enzyme activity in gingival crevicular fluid. J Clin Periodontol. 1988;15(6):347-52.

Oveland E, Karlsen TV, Haslene-Hox H, Semaeva E, Janaczyk B, Tenstad O, Wiig H. Proteomic evaluation of inflammatory proteins in rat spleen interstitial fluid and lymph during LPSinduced systemic inflammation reveals increased levels of ADAMST1. J Proteome Res. 2012; 11(11):5338-49

Gustavsson H, Jennbacken K, Welen K, et al. Altered expression of genes regulating angiogenesis in experimental androgenindependent prostate cancer. Prostate 2008;68:161–70

Thai SN, Iruela-Arispe ML. Expression of ADAMTS1 during murine development. Mech Dev 2002;115:181–5.

Shindo T, Kurihara H, Kuno K, et al. ADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and function. J Clin Invest 2000;105:1345–52.

Published

03-06-2022

How to Cite

Shetgaonkar, K. A., Suragimath, G., Varma, A. S., Zope, S. A., & Ashwinirani, S. R. (2022). Effect of non-surgical periodontal therapy (NSPT) on salivary and serum levels of a disintegrin-like and metalloproteinase with thrombospondin-1 (ADAMTS-1). International Journal of Health Sciences, 6(S1), 13395–13407. https://doi.org/10.53730/ijhs.v6nS1.8348

Issue

Section

Peer Review Articles

Most read articles by the same author(s)