Results 91 to 100 of about 14,656 (238)

Noncrystalline uric acid inhibits proteoglycan and glycosaminoglycan synthesis in distal tubular epithelial cells (MDCK) [PDF]

, 2010
Hyperuricemia is associated with renal stones, not only consisting of uric acid (UrAc) but also of calcium oxalate (CaOx). Glycosaminoglycans (GAGs) are well-known inhibitors of growth and aggregation of CaOx crystals.
Borges, Fernanda Teixeira, Dalboni, Maria Aparecida, Michelacci, Yara Maria, Schor, Nestor   +3 more
core   +2 more sources

Membrane trafficking of synaptic adhesion molecules

The Journal of Physiology, Volume 603, Issue 20, Page 5921-5934, October 15, 2025.
Abstract figure legend Synaptic cellular adhesion molecules are surface transmembrane receptors that have been shown to internalize via endocytosis, and possibly also recycle, in a process that has been linked to the function and the turnover of the synaptic contact site.
Cristian A. Bogaciu, Silvio O. Rizzoli
wiley   +1 more source

Searching urinary tumor-associated proteins for bladder transitional cell carcinoma in southwestern Taiwan using gel-based proteomics

Urological Science, 2016
Background and purpose: We try to search for specific serum or urinary biomarkers for the early detection, follow-up, and prediction of tumor recurrence, progression, and clinical outcome is a difficult task in individuals with bladder cancer.
Chia-Cheng Su, Kun-Hung Sheng, Shih-Ying Chen, Yeou-Guang Tsay, Ting-Feng Wu   +4 more
doaj   +1 more source

The Pathophysiological Functions of Heparanases: From Evolution, Structural and Tissue‐Specific Perspectives

The FASEB Journal, Volume 39, Issue 17, 15 September 2025.
Heparanase 1 (HPSE1) and Heparanase 2 (HPSE2) exhibit opposing expression patterns and functions in pathological contexts, such as cancer. Here, we describe their specific expression in immune cells and their implications in skin diseases. Although they are structurally similar and considered to be ‘cousins’, we found no common ancestor and that HPSE2 ...
Elham Vahdatahar, Clément Daviaud, Hugo Main, Rachel Havret, Claire Debarnot, Laure Favot‐Laforge, Jean‐François Jégou, Ingrid Fruitier‐Arnaudin, Antoine Dufour, Romain Vivès, Franck Morel, Yves Bourne, Kévin Baranger   +12 more
wiley   +1 more source

The perlecan LDL-binding receptor needs sugar: Implication of perlecan core protein interaction with LDL for atherosclerosis [PDF]

Receptors & Clinical Investigation, 2015
Cardiovascular disease (CVD) is the deadliest disease in the US and finding cures for CVD has been a pressing and challenging problem in biomedical science. Atherosclerosis is a pathological condition caused by an elevated plasma LDL cholesterol level and its deposition in the arterial wall.
openaire   +1 more source

Exploiting Heparan Sulfate Proteoglycans in Human Neurogenesis—Controlling Lineage Specification and Fate

Frontiers in Integrative Neuroscience, 2017
Unspecialized, self-renewing stem cells have extraordinary application to regenerative medicine due to their multilineage differentiation potential.
Chieh Yu, Lyn R. Griffiths, Larisa M. Haupt   +2 more
doaj   +1 more source

A Biomimetic Approach toward Enhancing Angiogenesis: Recombinantly Expressed Domain V of Human Perlecan Is a Bioactive Molecule That Promotes Angiogenesis and Vascularization of Implanted Biomaterials

Advanced Science, 2020
Angiogenic therapy involving delivery of pro‐angiogenic growth factors to stimulate new blood vessel formation in ischemic disease is promising but has seen limited clinical success due to issues associated with the need to deliver supra‐physiological ...
Xiaoting Lin, Fengying Tang, Shouyuan Jiang, Heba Khamis, Andre Bongers, John M. Whitelock, Megan S. Lord, Jelena Rnjak‐Kovacina   +7 more
doaj   +1 more source

Heparan sulfate proteoglycans: structure, protein interactions and cell signaling [PDF]

, 2009
Heparan sulfate proteoglycans are ubiquitously found at the cell surface and extracellular matrix in all the animal species. This review will focus on the structural characteristics of the heparan sulfate proteoglycans related to protein interactions ...
ABRAMSSON A, ALEXOPOULOU AN, ALLIEL PM, ALMEIDA PC, ARICESCU AR, ASHIKARI-HADA S, ATHANASSIADES A, AVIEZER D, BAEG GH, BAKER AB, BARTLETT AH, BEAUVAIS DM, BECKETT K, BELFORD DA, BELLIN R, BELTING M, BEN-ZAKEN O, BERNFIELD M, BEZAKOVA G, BLACKHALL FH, BOUCHE G, Caio V. Regatieri, CAIZERGUES-FERRER M, CAMPBELL EJ, CANO-GAUCI DF, CAPILA I, CAPILA I, CAPILA I, CAPURRO MI, CARDIN AD, CARNERO A, CASSARO CM, CASU B, CHAVANTE SF, CHEN CL, CHENG F, CHUANG WL, COHEN MM JR, COLE GJ, CONRAD HE, COOMBE DR, CROWN SE, CZUBAYKO F, DEANGELIS PL, DERKSEN PW, DIETRICH CP, DIETRICH CP, DIETRICH CP, DIETRICH CP, DIETRICH CP, DIETZ F, DUCHESNE L, ESCRIBA PV, FAN TC, FARACH-CARSON MC, FARACH-CARSON MC, FEARS CY, FEDARKO NS, FERREIRA TM, FERRO DR, FEYZI E, FILMUS J, FILMUS J, FJELDSTAD K, FOX AN, FRANCO CR, FRANSSON LA, FRANSSON LA, FUKI IV, FUKI IV, FURUKAWA K, GAGLIARDI M, GALLAGHER JT, GAMBARINI AG, GIROS A, GITAY-GOREN H, GLASS DJ, GOMES PB, GRUNERT M, GUERRINI M, GUERRINI M, GUMIENNY TL, HABUCHI H, HACKER U, HANDEL TM, HARMER NJ, HARRISON CA, HAUSSER HJ, Helena B. Nader, HENKE CA, HILEMAN RE, HSIA E, HUBER R, IOZZO RV, IOZZO RV, ISHIHARA M, ISHIHARA M, ISHITSUKA R, JASTREBOVA N, JERONIMO SM, JIANG X, JOHNSON KG, JOHNSON Z, Juliana L. Dreyfuss, JURY EC, KAYED H, KEMP LE, KIRKPATRICK CA, KNOX SM, KOOPMANN W, KREUGER J, KRILLEKE D, LAU EK, LEICHT DT, LEWIS KA, LINDNER JR, LOO BM, LOPES CC, LOPES CC, LORTAT-JACOB H, Lucia O. Sampaio, MA YQ, MIYAZONO K, MOBLI M, MOHAMMADI M, MOHAMMADI M, MONGIAT M, MOREIRA CR, MORGAN MR, MULLOY B, MULLOY B, MULLOY B, MURRAY AJ, NADER HB, NADER HB, NADER HB, NADER HB, NADER HB, NADER HB, NAKADA M, NASCIMENTO FD, NASCIMENTO FD, NG YS, NGO ST, NOTI C, NOZIK-GRAYCK E, NUGENT MA, NUNES SS, OBA-SHINJO SM, OH ES, PADERA R, PANKONIN MS, PARISH CR, PATEL VN, PATEY SJ, PELLEGRINI L, PERETTI T, POON GM, PORCIONATTO MA, PORCIONATTO MA, PORCIONATTO MA, POWELL AK, POWERS CJ, PRESTA M, QUARTO N, RAGAZZI M, RAMAN R, RAPRAEGER AC, RAPRAEGER AC, Renan P. Cavalheiro, RIDER CC, ROHDE LH, ROLNY C, RUBIN JS, RUHRBERG C, SAITO Y, SAKSELA O, SAMPAIO L, SANDERSON RD, SASAKI N, SASAKI S, SASISEKHARAN R, SCHNEPP A, SCHWALL RH, SHINJO SK, SMIRNOV SP, SONCIN F, SONG HH, SPIVAK-KROIZMAN T, STIGLIANO I, STRAUS AH, STRINGER SE, SU G, SUAREZ ER, SUGAYA N, SULPICE E, TANTRAVAHI RV, TAYLOR KR, TELCI D, TERSARIOL IL, TERSARIOL IL, Thais R. Jarrouge, TKACHENKO E, TKACHENKO E, TOLEDO OM, TOUROVSKAIA A, TRAISTER A, UTANI A, VEIGA SS, VEUGELERS M, VEUGELERS M, VIVES RR, VLODAVSKY I, WALKER A, WATT SM, WHITELOCK JM, WIEDLOCHA A, WILCOX-ADELMAN SA, WILKINS-PORT CE, WILLIAMS S, WOJTAL KA, WOODS A, WU DQ, YATES EA, YAYON A, YU WH, YU WH, ZHANG F   +227 more
core   +2 more sources

Microphysiological Glomerular Filtration Barriers: Current Insights, Innovations, and Future Applications

Advanced Biology, Volume 9, Issue 9, September 2025.
The glomerular filtration barrier (GFB) is the first step of blood filtration by the kidneys. The concerning increase of kidney diseases makes the development of new models essential. In this context, microphysiological glomerular filtration barriers focus on closely reproducing the physiological architecture of the in vivo GFB: podocytes, glomerular ...
Manon Miran, Kieu Ngo, David Buob, Hanna Debiec, Pierre Ronco, Guillaume Perry   +5 more
wiley   +1 more source

Differential expression of proteoglycans in tissue remodeling and lymphangiogenesis after experimental renal transplantation in rats. [PDF]

PLoS ONE, 2010
BACKGROUND: Chronic transplant dysfunction explains the majority of late renal allograft loss and is accompanied by extensive tissue remodeling leading to transplant vasculopathy, glomerulosclerosis and interstitial fibrosis. Matrix proteoglycans mediate
Heleen Rienstra, Kirankumar Katta, Johanna W A M Celie, Harry van Goor, Gerjan Navis, Jacob van den Born, Jan-Luuk Hillebrands   +6 more
doaj   +1 more source