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Journal articles on the topic 'Small Leucine Rich Proteoglycans'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Schaefer, Liliana. "Small Leucine-Rich Proteoglycans in Kidney Disease." Journal of the American Society of Nephrology 22, no. 7 (2011): 1200–1207. http://dx.doi.org/10.1681/asn.2010050570.

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2

Sandell, L. J., and T. M. Hering. "Small Leucine-rich Proteoglycans: Prelude to a Function." Trends in Glycoscience and Glycotechnology 5, no. 21 (1993): 13–22. http://dx.doi.org/10.4052/tigg.5.13.

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3

Iozzo, Renato V. "The Biology of the Small Leucine-rich Proteoglycans." Journal of Biological Chemistry 274, no. 27 (1999): 18843–46. http://dx.doi.org/10.1074/jbc.274.27.18843.

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4

Low, Shermaine W. Y., Thomas B. Connor, Iris S. Kassem, Deborah M. Costakos, and Shyam S. Chaurasia. "Small Leucine-Rich Proteoglycans (SLRPs) in the Retina." International Journal of Molecular Sciences 22, no. 14 (2021): 7293. http://dx.doi.org/10.3390/ijms22147293.

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Retinal diseases such as age-related macular degeneration (AMD), retinopathy of prematurity (ROP), and diabetic retinopathy (DR) are the leading causes of visual impairment worldwide. There is a critical need to understand the structural and cellular components that play a vital role in the pathophysiology of retinal diseases. One potential component is the family of structural proteins called small leucine-rich proteoglycans (SLRPs). SLRPs are crucial in many fundamental biological processes involved in the maintenance of retinal homeostasis. They are present within the extracellular matrix (

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5

Merline, Rosetta, Roland M. Schaefer, and Liliana Schaefer. "The matricellular functions of small leucine-rich proteoglycans (SLRPs)." Journal of Cell Communication and Signaling 3, no. 3-4 (2009): 323–35. http://dx.doi.org/10.1007/s12079-009-0066-2.

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6

Moreth, Kristin, Renato V. Iozzo, and Liliana Schaefer. "Small leucine-rich proteoglycans orchestrate receptor crosstalk during inflammation." Cell Cycle 11, no. 11 (2012): 2084–91. http://dx.doi.org/10.4161/cc.20316.

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7

Embery, Graham, Rachel Hall, Rachel Waddington, Dominique Septier, and Michel Goldberg. "Proteoglycans in Dentinogenesis." Critical Reviews in Oral Biology & Medicine 12, no. 4 (2001): 331–49. http://dx.doi.org/10.1177/10454411010120040401.

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The predominant proteoglycans present in predentin and dentin are the chondroitin-sulphate-rich decorin and biglycan and the keratan-sulphate-rich lumican and fibromodulin. These are small, interstitial, leucine-rich proteoglycans which have recently been shown to exist in gradients across the predentin. Antibodies recognizing chondroitin sulphate show a decreasing gradient from the pulpal aspect toward the mineralizing front, the converse being true for keratan sulphate. Anti-decorin shows an increase toward the mineralization front. Evidence from biochemical, autoradiographic, and immunohist

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8

Waddington, RJ, HC Roberts, RV Sugars, and E. Schönherr. "Differential roles for small leucine-rich proteoglycans in bone formation." European Cells and Materials 6 (October 6, 2003): 12–21. http://dx.doi.org/10.22203/ecm.v006a02.

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9

Kalamajski, Sebastian, and Åke Oldberg. "The role of small leucine-rich proteoglycans in collagen fibrillogenesis." Matrix Biology 29, no. 4 (2010): 248–53. http://dx.doi.org/10.1016/j.matbio.2010.01.001.

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10

Ni, G. X., Z. Li, and Y. Z. Zhou. "The role of small leucine-rich proteoglycans in osteoarthritis pathogenesis." Osteoarthritis and Cartilage 22, no. 7 (2014): 896–903. http://dx.doi.org/10.1016/j.joca.2014.04.026.

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11

Pietraszek-Gremplewicz, Katarzyna, Konstantina Karamanou, Aïchata Niang, et al. "Small leucine-rich proteoglycans and matrix metalloproteinase-14: Key partners?" Matrix Biology 75-76 (January 2019): 271–85. http://dx.doi.org/10.1016/j.matbio.2017.12.006.

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12

Yang, C. H., G. J. Culshaw, M. M. Liu, et al. "Canine tissue-specific expression of multiple small leucine rich proteoglycans." Veterinary Journal 193, no. 2 (2012): 374–80. http://dx.doi.org/10.1016/j.tvjl.2012.01.018.

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13

Yuan, Xiaoyong, Xia Hua, and Kirk R. Wilhelmus. "Expression of Small Leucine-Rich Proteoglycans During Experimental Fungal Keratitis." Cornea 29, no. 6 (2010): 674–79. http://dx.doi.org/10.1097/ico.0b013e3181c29744.

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14

Nikitovic, Dragana, John Aggelidakis, Marian F. Young, Renato V. Iozzo, Nikos K. Karamanos, and George N. Tzanakakis. "The Biology of Small Leucine-rich Proteoglycans in Bone Pathophysiology." Journal of Biological Chemistry 287, no. 41 (2012): 33926–33. http://dx.doi.org/10.1074/jbc.r112.379602.

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15

Zou, Wei, Junhui Wan, Min Li, et al. "Small leucine rich proteoglycans in host immunity and renal diseases." Journal of Cell Communication and Signaling 13, no. 4 (2018): 463–71. http://dx.doi.org/10.1007/s12079-018-0489-8.

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16

Appunni, Sandeep, Vivek Anand, Madhuram Khandelwal, Nidhi Gupta, Muni Rubens, and Alpana Sharma. "Small Leucine Rich Proteoglycans (decorin, biglycan and lumican) in cancer." Clinica Chimica Acta 491 (April 2019): 1–7. http://dx.doi.org/10.1016/j.cca.2019.01.003.

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17

Nikitovic, Dragana, Paulos Katonis, Aristidis Tsatsakis, Nikos K. Karamanos, and George N. Tzanakakis. "Lumican, a small leucine-rich proteoglycan." IUBMB Life 60, no. 12 (2008): 818–23. http://dx.doi.org/10.1002/iub.131.

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18

Hultgårdh-Nilsson, A., J. Borén, and S. Chakravarti. "The small leucine-rich repeat proteoglycans in tissue repair and atherosclerosis." Journal of Internal Medicine 278, no. 5 (2015): 447–61. http://dx.doi.org/10.1111/joim.12400.

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19

Solis Hernandez, Maria Del Pilar, Olivia Pilar García-Suárez, Ivan Fernández-Vega, Luis M. Quirós, and Beatriz García. "Alterations in small leucine-rich proteoglycans in right-sided colorectal cancer." Journal of Clinical Oncology 35, no. 4_suppl (2017): 652. http://dx.doi.org/10.1200/jco.2017.35.4_suppl.652.

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652 Background: Colorectal cancer (CRC) is a heterogeneous disease, and there are anatomic, functional and molecular differences between the tumors of the proximal and distal colorectum. Various molecular phenotypes have been associated with aggressive subtypes in these pathologies, and several of these markers show a relationship with proteoglycans, which in turn show significant alterations in colon tumors, which affect both their core proteins and their glycosaminoglycan chains. Small leucine-rich proteoglycans (SLRPs) constitute a family of molecules encoded by 18 distinct genes. They are

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20

Horiguchi, Kotaro, Rahimi Syaidah, Ken Fujiwara, et al. "Expression of small leucine-rich proteoglycans in rat anterior pituitary gland." Cell and Tissue Research 351, no. 1 (2012): 207–12. http://dx.doi.org/10.1007/s00441-012-1513-6.

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21

Frikeche, Jihane, George Maiti, and Shukti Chakravarti. "Small leucine-rich repeat proteoglycans in corneal inflammation and wound healing." Experimental Eye Research 151 (October 2016): 142–49. http://dx.doi.org/10.1016/j.exer.2016.08.015.

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22

Hua, Rui, and Jean X. Jiang. "Small leucine-rich proteoglycans in physiological and biomechanical function of bone." Matrix Biology Plus 11 (August 2021): 100063. http://dx.doi.org/10.1016/j.mbplus.2021.100063.

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23

Seidler, Daniela G., Jasna Peter-Katalinic, and Alina D. Zamfir. "Galactosaminoglycan Function and Oligosaccharide Structure Determination." Scientific World JOURNAL 7 (2007): 233–41. http://dx.doi.org/10.1100/tsw.2007.63.

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This review will discuss the importance of sequencing long chondroitin sulfate and dermatan sulfate chains specifically derived from decorin. Decorin is a member of the small leucine-rich repeat proteoglycans and ubiquitously expressed primarily in the skin. Sequence information and diverse function of glycosaminoglycans is further influenced by variable expression through the core protein indicating the importance to analyse glycosaminoglycans from specific proteoglycans.

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24

Iozzo, Renato V., and Liliana Schaefer. "Proteoglycans in health and disease: novel regulatory signaling mechanisms evoked by the small leucine-rich proteoglycans." FEBS Journal 277, no. 19 (2010): 3864–75. http://dx.doi.org/10.1111/j.1742-4658.2010.07797.x.

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25

San Martin, S. "Small leucine-rich proteoglycans (SLRPs) in uterine tissues during pregnancy in mice." Reproduction 125, no. 4 (2003): 585–95. http://dx.doi.org/10.1530/reprod/125.4.585.

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26

Schaefer, Liliana, and Renato V. Iozzo. "Small leucine-rich proteoglycans, at the crossroad of cancer growth and inflammation." Current Opinion in Genetics & Development 22, no. 1 (2012): 56–57. http://dx.doi.org/10.1016/j.gde.2011.12.002.

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27

Chen, Shoujun, and David E. Birk. "The regulatory roles of small leucine-rich proteoglycans in extracellular matrix assembly." FEBS Journal 280, no. 10 (2013): 2120–37. http://dx.doi.org/10.1111/febs.12136.

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28

Chen, Lili, Jingwen Liao, Eric Klineberg, Victor YL Leung, and Shishu Huang. "Small leucine-rich proteoglycans (SLRPs): characteristics and function in the intervertebral disc." Journal of Tissue Engineering and Regenerative Medicine 11, no. 3 (2015): 602–8. http://dx.doi.org/10.1002/term.2067.

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29

Mikaelsson, Eva, Mahmood Jeddi-Tehrani, Anders Ã–Sterborg, Fazel Shokri, Hodjattallah Rabbani, and Håkan Mellstedt. "Small Leucine Rich Proteoglycans as Novel Tumor Markers In Chronic Lymphocytic Leukemia." Blood 116, no. 21 (2010): 694. http://dx.doi.org/10.1182/blood.v116.21.694.694.

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Abstract Abstract 694 Background: Small leucine rich proteoglycans (SLRPs) are a family of glycosylated proteins normally expressed in the extracelluar matrix (ECM) of collagen rich tissues. The biological role of the SLRPs is multifactoral, but mostly these proteins are secreted and bind to membrane receptors or ECM proteins affecting cell proliferation and cell migration. Some SLRPs (eg. Decorin, Lumican) have been reported to be expressed in cancer, but the expression as well as the glycosylation pattern differ. Microarray studies have revealed that the SLRP family member fibromodulin (FMOD

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30

Nastase, Madalina V., Andrea Janicova, Heiko Roedig, Louise Tzung-Harn Hsieh, Malgorzata Wygrecka, and Liliana Schaefer. "Small Leucine-Rich Proteoglycans in Renal Inflammation: Two Sides of the Coin." Journal of Histochemistry & Cytochemistry 66, no. 4 (2018): 261–72. http://dx.doi.org/10.1369/0022155417738752.

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31

Pedersen, ME, E. Ytteborg, A. Kohler, et al. "Small leucine-rich proteoglycans in the vertebrae of Atlantic salmon Salmo salar." Diseases of Aquatic Organisms 106, no. 1 (2013): 57–68. http://dx.doi.org/10.3354/dao02638.

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32

Juneja, Subhash C., and Christian Veillette. "Defects in Tendon, Ligament, and Enthesis in Response to Genetic Alterations in Key Proteoglycans and Glycoproteins: A Review." Arthritis 2013 (November 10, 2013): 1–30. http://dx.doi.org/10.1155/2013/154812.

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This review summarizes the genetic alterations and knockdown approaches published in the literature to assess the role of key proteoglycans and glycoproteins in the structural development, function, and repair of tendon, ligament, and enthesis. The information was collected from (i) genetically altered mice, (ii) in vitro knockdown studies, (iii) genetic variants predisposition to injury, and (iv) human genetic diseases. The genes reviewed are for small leucine-rich proteoglycans (lumican, fibromodulin, biglycan, decorin, and asporin); dermatan sulfate epimerase (Dse) that alters structure of

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33

SZTROLOVICS, Robert, Robert J. WHITE, A. Robin POOLE, John S. MORT, and Peter J. ROUGHLEY. "Resistance of small leucine-rich repeat proteoglycans to proteolytic degradation during interleukin-1-stimulated cartilage catabolism." Biochemical Journal 339, no. 3 (1999): 571–77. http://dx.doi.org/10.1042/bj3390571.

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A bovine nasal-cartilage culture system has been utilized to analyse the catabolic events occurring in response to interleukin-1β over a 14-day period. An early event following the start of interleukin-1 treatment was the release of glycosaminoglycan into the culture medium. This release was accompanied by the appearance in the tissue, and shortly thereafter also in the culture media, of a globular domain (G1)-containing aggrecan degradation product generated by the action of aggrecanase. Link protein was also released from the cartilage with a similar timeframe to that of the G1 fragment, alt

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34

McEwan, Paul A., Paul G. Scott, Paul N. Bishop, and Jordi Bella. "Structural correlations in the family of small leucine-rich repeat proteins and proteoglycans." Journal of Structural Biology 155, no. 2 (2006): 294–305. http://dx.doi.org/10.1016/j.jsb.2006.01.016.

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35

Marzoll, Andrea, Ariane Melchior-Becker, Francesco Cipollone, and Jens W. Fischer. "Small leucine-rich proteoglycans in atherosclerotic lesions: novel targets of chronic statin treatment?" Journal of Cellular and Molecular Medicine 15, no. 2 (2011): 232–43. http://dx.doi.org/10.1111/j.1582-4934.2009.00986.x.

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36

Honardoust, Dariush, Mathew Varkey, Keijiro Hori, Jie Ding, Heather A. Shankowsky, and Edward E. Tredget. "Small leucine-rich proteoglycans, decorin and fibromodulin, are reduced in postburn hypertrophic scar." Wound Repair and Regeneration 19, no. 3 (2011): 368–78. http://dx.doi.org/10.1111/j.1524-475x.2011.00677.x.

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37

Salgado, Renato M., Rodolfo R. Favaro, Sebastian San Martin, and Telma M. T. Zorn. "The Estrous Cycle Modulates Small Leucine-Rich Proteoglycans Expression in Mouse Uterine Tissues." Anatomical Record: Advances in Integrative Anatomy and Evolutionary Biology 292, no. 1 (2009): 138–53. http://dx.doi.org/10.1002/ar.20797.

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38

Dupuis, Loren E., and Christine B. Kern. "Small leucine-rich proteoglycans exhibit unique spatiotemporal expression profiles during cardiac valve development." Developmental Dynamics 243, no. 4 (2014): 601–11. http://dx.doi.org/10.1002/dvdy.24100.

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39

Hancock, S., A. P. L. Kwan, and V. C. Duance. "Type-X collagen interacts with the small leucine-rich proteoglycans decorin and biglycan." International Journal of Experimental Pathology 85, no. 1 (2008): A41. http://dx.doi.org/10.1111/j.0959-9673.2004.369bb.x.

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40

Solis Hernandez, Maria Del Pilar, Ivan Fernandez-Vega, Olivia García-Suárez, Natalia Perez Lopez, Luis M. Quirós, and Beatriz García. "Different small leucine-rich proteoglycans expression pattern by tumor location in colorectal cancer." Journal of Clinical Oncology 35, no. 15_suppl (2017): e15138-e15138. http://dx.doi.org/10.1200/jco.2017.35.15_suppl.e15138.

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e15138 Background: Colorectal cancer (CRC) is a heterogeneous disease defined by anatomic, functional and molecular differences depending on the primary tumor location (PTL). Several molecular phenotypes have been associated with aggressive behavior, and some of these markers are related with proteoglycans, which in turn show alterations in CRC. Small leucine-rich proteoglycans (SLRPs) are a family of molecules encoded by18 genes that may appear coupled to different glycosaminoglycan chains ––including chondroitin/dermatan or keratan sulphate–– or not, depending on the specific species. They a

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41

Solis Hernandez, Maria Del Pilar, Natalia Perez Lopez, Yolanda Garcia Mesa, et al. "Small leucine-rich proteoglycans expression in colorectal cancer: Differences by primary tumor location." Journal of Clinical Oncology 36, no. 4_suppl (2018): 721. http://dx.doi.org/10.1200/jco.2018.36.4_suppl.721.

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721 Background: SLRP are present in normal and tumor colorectal tissue, with different patterns of expression, being predominant in L CRC. However, due to the small sample the differences observed in survival were no statistically significative. These alterations could be related to interactions at the extracellular matrix level. Further prospective and larger analysis are needed for a better comprehension of tumor microenvironment. Aims: To describe SLRP expression pattern by PTL and survival rate. Methods: 32 tumor specimens and their respective healthy tissue (fresh frozen tissue) from prim

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42

Schaefer, Liliana, and Renato V. Iozzo. "Biological Functions of the Small Leucine-rich Proteoglycans: From Genetics to Signal Transduction." Journal of Biological Chemistry 283, no. 31 (2008): 21305–9. http://dx.doi.org/10.1074/jbc.r800020200.

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43

Nastase, Madalina V., Renato V. Iozzo, and Liliana Schaefer. "Key roles for the small leucine-rich proteoglycans in renal and pulmonary pathophysiology." Biochimica et Biophysica Acta (BBA) - General Subjects 1840, no. 8 (2014): 2460–70. http://dx.doi.org/10.1016/j.bbagen.2014.01.035.

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44

Appunni, Sandeep, Vivek Anand, Madhuram Khandelwal, Amlesh Seth, Sandeep Mathur, and Alpana Sharma. "Altered expression of small leucine-rich proteoglycans (Decorin, Biglycan and Lumican): Plausible diagnostic marker in urothelial carcinoma of bladder." Tumor Biology 39, no. 5 (2017): 101042831769911. http://dx.doi.org/10.1177/1010428317699112.

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Small leucine-rich proteoglycans are components of extracellular matrix that regulates neoplastic transformation. Among small leucine rich proteoglycans, Decorin, Biglycan and Lumican are most commonly implicated markers, and their expression is well studied in various malignancies. In this novel study, we have collectively evaluated expression of these three molecules in urothelial carcinoma of bladder. Thirty patients of confirmed untreated bladder cancer, 30 healthy controls for blood and 30 controls for adjacent non-tumour tissue were enrolled. Blood was collected from all subjects and tum

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45

Vuillermoz, Boris, Yanusz Wegrowski, Jean-Luc Contet-Audonneau, Louis Danoux, Gilles Pauly, and François-Xavier Maquart. "Influence of aging on glycosaminoglycans and small leucine-rich proteoglycans production by skin fibroblasts." Molecular and Cellular Biochemistry 277, no. 1-2 (2005): 63–72. http://dx.doi.org/10.1007/s11010-005-5073-x.

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46

Paracuellos, Patricia, Sebastian Kalamajski, Arkadiusz Bonna, Dominique Bihan, Richard W. Farndale, and Erhard Hohenester. "Structural and functional analysis of two small leucine-rich repeat proteoglycans, fibromodulin and chondroadherin." Matrix Biology 63 (November 2017): 106–16. http://dx.doi.org/10.1016/j.matbio.2017.02.002.

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47

Gaspar, R., A. Gorbe, J. Paloczi, et al. "P148Cardiac myocytes are protected by small leucine rich proteoglycans against simulated ischemia/reperfusion injury." Cardiovascular Research 103, suppl 1 (2014): S26.2—S26. http://dx.doi.org/10.1093/cvr/cvu082.87.

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48

Li, Xin, Angela Pennisi, and Shmuel Yaccoby. "Small Leucine-Rich Proteoglycans (SLRPs) Are Involved in the Anti-Myeloma Response of Osteoblasts." Blood 110, no. 11 (2007): 815. http://dx.doi.org/10.1182/blood.v110.11.815.815.

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Abstract Multiple myeloma (MM) is closely associated with severe osteolytic bone disease caused by stimulation of osteoclastogenesis and suppression of osteoblastogenesis. We have recently demonstrated that while osteoclasts support MM growth, osteoblasts have negative impact on survival and proliferation of MM cells from a subset of patients in vitro and in vivo (Yaccoby et al., Cancer Res 2004: Haematologica 2006), indicating that MM bone disease drives tumor progression. To unravel anti-MM molecular mechanism of osteoblasts we performed global gene expression profiling on osteoblasts and th

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49

Zeng-Brouwers, Jinyang, Sony Pandey, Jonel Trebicka, Malgorzata Wygrecka, and Liliana Schaefer. "Communications via the Small Leucine-rich Proteoglycans: Molecular Specificity in Inflammation and Autoimmune Diseases." Journal of Histochemistry & Cytochemistry 68, no. 12 (2020): 887–906. http://dx.doi.org/10.1369/0022155420930303.

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Inflammation is a highly regulated biological response of the immune system that is triggered by assaulting pathogens or endogenous alarmins. It is now well established that some soluble extracellular matrix constituents, such as small leucine-rich proteoglycans (SLRPs), can act as danger signals and trigger aseptic inflammation by interacting with innate immune receptors. SLRP inflammatory signaling cascade goes far beyond its canonical function. By choosing specific innate immune receptors, coreceptors, and adaptor molecules, SLRPs promote a switch between pro- and anti-inflammatory signalin

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50

Brown, Sharon, James Melrose, Bruce Caterson, Peter Roughley, Stephen M. Eisenstein, and Sally Roberts. "A comparative evaluation of the small leucine-rich proteoglycans of pathological human intervertebral discs." European Spine Journal 21, S2 (2012): 154–59. http://dx.doi.org/10.1007/s00586-012-2179-1.

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