Results 141 to 150 of about 7,104 (177)
Some of the next articles are maybe not open access.

Developmental Regulation of Biglycan Expression in Muscle and Tendon

Muscle and Nerve, 2006
AbstractBiglycan 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.
Justin R Fallon   +2 more
exaly   +3 more sources

Hyperelongated biglycan: the surreptitious initiator of atherosclerosis

Current Opinion in Lipidology, 2008
To 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
openaire   +5 more sources

Biglycan Deficiency Interferes With Ovariectomy-Induced Bone Loss [PDF]

open access: yesJournal of Bone and Mineral Research, 2003
Abstract Biglycan is a matrix proteoglycan with a possible role in bone turnover. In a 4-week study with sham-operated or OVX biglycan-deficient or wildtype mice, we show that biglycan-deficient mice are resistant to OVX-induced trabecular bone loss and that there is a gender difference in the response to biglycan deficiency.
Matthew R. Allen   +2 more
exaly   +5 more sources

Regulation, Regulatory Activities, and Function of Biglycan

Critical Reviews™ in Eukaryotic Gene Expression, 2004
Biglycan 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
openaire   +2 more sources

Expression and significance of biglycan in endometrial cancer

Archives of Gynecology and Obstetrics, 2013
This 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 ...
Yang, Liu   +6 more
openaire   +2 more sources

Transcriptional and posttranscriptional regulators of biglycan in cardiac fibroblasts

Basic Research in Cardiology, 2009
Biglycan, a small leucine-rich proteoglycan, is essential for scar formation and preservation of hemodynamic function after myocardial infarction, as shown in biglycan-knockout mice. Because of this important role in cardiac pathophysiology, we aimed to identify regulators of biglycan expression and posttranslational modifications in cardiac ...
Tiede, Karen   +2 more
openaire   +2 more sources

Hematopoietic Activity Associated with Biglycan-like Proteoglycan

Biochemical and Biophysical Research Communications, 1993
One 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
openaire   +2 more sources

Expression of tenascin, biglycan and decorin in disorders of keratinization

British Journal of Dermatology, 1994
The distribution of three (recently discovered) extracellular matrix components (tenascin, biglycan and decorin) was studied in normal adult human skin and in a number of monogenic disorders of keratinization, using immunohistology. The expression of tenascin, which is sparsely distributed in normal human dermis, was found to be grossly increased in ...
P M, Steijlen   +6 more
openaire   +2 more sources

Biglycan and Decorin Expression and Distribution in Palatal Adhesion

Journal of Dental Research, 2017
Previous 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
openaire   +2 more sources

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