Results 11 to 20 of about 16,351 (268)

Perlecan: a review of its role in neurologic and musculoskeletal disease

Frontiers in Physiology, 2023
Perlecan is a 500 kDa proteoglycan residing in the extracellular matrix of endothelial basement membranes with five distinct protein domains and three heparan sulfate chains.
Tessa R. Lavorgna, Timothy E. Gressett, Timothy E. Gressett, Wesley H. Chastain, Wesley H. Chastain, Gregory J. Bix, Gregory J. Bix, Gregory J. Bix   +7 more
doaj   +4 more sources

Maternal serum perlecan levels in women with preeclampsia

Hypertension in Pregnancy, 2020
Objective: Perlecan is an extracellular matrix proteoglycan suggested to maintain endothelial functions. We aimed to measure maternal serum perlecan levels in different preeclampsia phenotypes.
Murat Akbas, Faik Mumtaz Koyuncu, Burcu Artunc-Ulkumen, Fatma Taneli, Habib Ozdemir   +4 more
doaj   +6 more sources

Perlecan, A Multi-Functional, Cell-Instructive, Matrix-Stabilizing Proteoglycan With Roles in Tissue Development Has Relevance to Connective Tissue Repair and Regeneration

Frontiers in Cell and Developmental Biology, 2022
This review highlights the multifunctional properties of perlecan (HSPG2) and its potential roles in repair biology. Perlecan is ubiquitous, occurring in vascular, cartilaginous, adipose, lymphoreticular, bone and bone marrow stroma and in neural tissues.
Anthony J. Hayes, Brooke L. Farrugia, Ifechukwude J. Biose, Gregory J. Bix, James Melrose, James Melrose   +5 more
doaj   +2 more sources

3D distribution of perlecan within intervertebral disc chondrons suggests novel regulatory roles for this multifunctional modular heparan sulphate proteoglycan [PDF]

European Cells & Materials, 2021
Perlecan is a modular, multifunctional heparan sulphate-proteoglycan (HS-PG) that is present in the pericellular and wider extracellular matrix of connective tissues.
AJ Hayes, J Melrose
doaj   +2 more sources

Loss of the extracellular matrix protein Perlecan disrupts axonal and synaptic stability during Drosophila development

eLife, 2023
Heparan sulfate proteoglycans (HSPGs) form essential components of the extracellular matrix (ECM) and basement membrane (BM) and have both structural and signaling roles.
Ellen J Guss, Yulia Akbergenova, Karen L Cunningham, J Troy Littleton   +3 more
doaj   +2 more sources

Hypoxia-Induced Biosynthesis of the Extracellular Matrix Molecules, Perlecan and Fibronectin, Promotes the Growth of Pleomorphic Adenoma Cells In Vitro Models

Biomedicines, 2023
Salivary pleomorphic adenoma is histopathologically characterized by its colorful stroma with myxoid, chondroid, and hyaline appearances, due to enhanced biosynthesis of extracellular matrix (ECM) molecules and poor vascularity. Thus, pleomorphic adenoma
Satoshi Maruyama, Manabu Yamazaki, Tatsuya Abé, Jun Cheng, Takashi Saku, Jun-ichi Tanuma   +5 more
doaj   +2 more sources

Perlecan in the Natural and Cell Therapy Repair of Human Adult Articular Cartilage: Can Modifications in This Proteoglycan Be a Novel Therapeutic Approach?

Biomolecules, 2021
Articular cartilage is considered to have limited regenerative capacity, which has led to the search for therapies to limit or halt the progression of its destruction.
John Garcia, Helen S. McCarthy, Jan Herman Kuiper, James Melrose, Sally Roberts   +4 more
doaj   +2 more sources

Increased Risk of Aortic Dissection with Perlecan Deficiency [PDF]

International Journal of Molecular Sciences, 2021
Perlecan (HSPG2), a basement membrane-type heparan sulfate proteoglycan, has been implicated in the development of aortic tissue. However, its role in the development and maintenance of the aortic wall remains unknown.
Risa Nonaka, T. Iesaki, A. Kerever, E. Arikawa-Hirasawa   +3 more
semanticscholar   +3 more sources

The multifaceted roles of perlecan in fibrosis [PDF]

Matrix Biology, 2018
Perlecan, or heparan sulfate proteoglycan 2 (HSPG2), is a ubiquitous heparan sulfate proteoglycan that has major roles in tissue and organ development and wound healing by orchestrating the binding and signaling of mitogens and morphogens to cells in a ...
Al-Ahmad, Andersson-Sjoland, Andersson-Sjoland, Arthur, Ashikari-Hada, Asplund, Aviezer, Barkefors, Barros, Behrens, Beller, Bengtsson, Bingley, Bishop, Bittencourt, Bix, Bix, Borkham-Kamphorst, Bremnes, Burgess, Cailhier, Cassiman, Celie, Ceol, Chakravarti, Chen, Chilosi, Chuang, Chuang, Cohen, Conde-Knape, Conte, Costell, Di Sario, Dos Santos, Duffield, Ebefors, Edgar, Esko, Evanko, Farach-Carson, Farach-Carson, Fengying Tang, Fernandez, Forsberg, Friedman, Friedman, Fujii, Gallai, Garl, Ge, Gellersen, Giros, Gohring, Gonzalez, Gonzalez, Goyal, Gressner, Gubbiotti, Guo, Hajari Case, Hallgren, Hammond, Hashimoto, Haubst, Hayashi, Hayward, Hedin, Hedin, Hering, Hilberg, Hisatomi, Ichimaru, Ikeguchi, Iozzo, Iozzo, Iozzo, Iredale, James G.W. Smith, James Melrose, Jelena Rnjak-Kovacina, John M. Whitelock, Jung, Kahari, Kaji, Kennett, Kinsella, Knox, Knox, Knox, Knox, Kotaru, Kovalszky, Koyama, Krimmer, Kunjathoor, Kvist, Laplante, Laplante, Leask, Leask, Leask, Lee, Lee, Lee, Lekkerkerker, Levy, Liang, Lord, Lord, Lord, Lord, Lundkvist, Mak, Mak, Mak, Malmstrom, Marra, Martinez-Hernandez, Martinez-Hernandez, Marx, Marzoll, Masola, Matsui, Matsuo, Megan S. Lord, Melrose, Melrose, Menzel, Mitra, Mollmark, Mongiat, Mongiat, Moon, Murphy, Musso, Nagy, Nakamura, Nakayama, Narita, Nguyen, Nihlberg, Nilsson, Ogawa, Ohkawara, Ozaki, Paka, Patel, Pillarisetti, Pinzani, Poluri, Pozzi, Raines, Raj, Rauch, Raymond, Rees, Rienstra, Rnjak-Kovacina, Rojkind, Rolls, Rosenzweig, Roskams, Ross, Sahin, Sakai, Salem, Sato, Schaefer, Schafer, Segev, Sharma, Shimizu-Hirota, Singh, Sofroniew, Sweeney, Tang, Tang, Tannock, Tao, Teh, Teimouri, Theret, Thomas, Thyberg, Timpl, Tomasek, Tran, Tran, Tran-Lundmark, Tátrai, Uchimura, Vanheule, Venkatesan, Venkatesan, Wang, Weiser, Weiser, Westergren-Thorsson, Westergren-Thorsson, Westergren-Thorsson, Whitelock, Whitelock, Whitelock, Whitelock, Willis, Wollin, Wollin, Woodall, Xu, Yamamoto, Yang, Yaoi, Yue, Yung, Yung, Zeisberg, Zeisberg   +217 more
core   +7 more sources

Atherosclerosis in perlecan heterozygous mice [PDF]

Journal of Lipid Research, 2004
The hypothesis that lipoprotein association with perlecan is atherogenic was tested by studying atherosclerosis in mice that had a heterozygous deletion of perlecan, the primary extracellular heparan sulfate proteoglycan in arteries. We first studied the
Reeba K. Vikramadithyan, Yuko Kako, Guangping Chen, Yunying Hu, Eri Arikawa-Hirasawa, Yoshihiko Yamada, Ira J. Goldberg   +6 more
doaj   +4 more sources