Results 191 to 200 of about 13,898 (220)
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Expression and significance of biglycan in endometrial cancer
Archives of Gynecology and Obstetrics, 2013This study aimed to determine the expression level of biglycan in different lesion properties of endometrium and to investigate the possible function and prognostic value of biglycan in endometrial cancer.Immunohistochemical staining (IHC) and quantitative realtime reverse transcription polymerase chain reaction (qRT-PCR) were used to determine the ...
Jie Jiang
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Hyperelongated biglycan: the surreptitious initiator of atherosclerosis
Current Opinion in Lipidology, 2008To outline a role for the dermatan sulfate proteoglycan biglycan and specifically its growth factor modified form having elongated glycosaminoglycan chains as being a primary initiator of atherosclerosis.Antiatherosclerotic therapies have mostly targeted epidemiologically identified, experimentally confirmed risk factors. The efficacy of such therapies
Little, Peter J. +2 more
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Hematopoietic Activity Associated with Biglycan-like Proteoglycan
Biochemical and Biophysical Research Communications, 1993One of the monocytic cell colony stimulating factors produced by thymic myoid cells, a 100 kDa factor, was purified by reversed phase HPLC and found to be homologous to the secreted form of proteoglycan 1 (biglycan) core protein. This biglycan associated colony stimulating factor did not carry an immunological motif of macrophage colony stimulating ...
I, Kamo +4 more
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Developmental regulation of biglycan expression in muscle and tendon
Muscle and Nerve, 2006AbstractBiglycan is an extracellular ligand for the dystrophin‐associated protein complex (DAPC) that is upregulated in both dystrophic and regenerating muscle. Biglycan also binds to collagen VI, mutations of which cause a congenital muscular dystrophy (Ullrich's; UCMD) that is also characterized by connective tissue abnormalities.
Beatrice E Lechner, Justin R Fallon
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Regulation, Regulatory Activities, and Function of Biglycan
Critical Reviews in Eukaryotic Gene Expression, 2004Biglycan is a member of the small leucine repeat proteoglycan family (SLRP). The biglycan gene is located on the X chromosome. Based on the amino acid sequence, the protein core of biglycan can be divided into six distinct domains: (1) a signal sequence, (2) a propeptide region, (3) a N-terminal glycosaminoglycan attachment region, (4) a cysteine loop,
Sunil, Wadhwa +3 more
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Increased atherosclerosis in mice with increased vascular biglycan content [PDF]
Atherosclerosis, 2014 The response to retention hypothesis of atherogenesis proposes that atherosclerosis is initiated via the retention of atherogenic lipoproteins by vascular proteoglycans. Co-localization studies suggest that of all the vascular proteoglycans, biglycan is the one most closely co-localized with LDL.
Lisa R Tannock
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The Role of Biglycan in the Heart
Connective Tissue Research, 2008Biglycan, a member of the small leucine rich proteoglycan family, is known to be expressed in almost every tissue of our body. Although there are increasing amount of data on the biological role of biglycan, its cardiac function is still not totally clarified.
Erika, Bereczki, Miklós, Sántha
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Biglycan knockout mice: New models for musculoskeletal diseases
Glycoconjugate Journal, 2002Biglycan is a Class I Small Leucine Rich Proteoglycans (SLRP) that is localized on human chromosome Xq28-ter. The conserved nature of its intron-exon structure and protein coding sequence compared to decorin (another Class I SLRP) indicates the two genes may have arisen from gene duplication. Biglycan contains two chondroitin sulfate glycosaminoglycan (
Marian F, Young +3 more
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cDNA sequence for bovine biglycan (PGI) protein core
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1993The nucleotide sequence of the protein core for bovine aortic smooth muscle cell biglycan was determined using recombinant DNA technology. Analysis of the deduced amino acid sequence for bovine biglycan revealed a striking homology, 94.6% and 95.7%, to human and rat biglycan, respectively.
M A, Torok, S A, Evans, J A, Marcum
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Biglycan and Decorin Expression and Distribution in Palatal Adhesion
Journal of Dental Research, 2017Previous studies demonstrated that chondroitin sulfate proteoglycans (CSPGs) on apical surfaces of palatal medial edge epithelial (MEE) cells were necessary for palatal adhesion. In this study, we identified 2 proteoglycans, biglycan and decorin, that were expressed in the palatal shelves prior to adhesion.
I, Ibrahim +3 more
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