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The Mechanistic studies showed that CSPG4 (show MCSP Proteins) bound to perlecan via hydrophobic protein-protein interactions involving multiple sites on perlecan including the C-terminal region.
The results indicate that increase of heparan sulfate content and up-regulation of perlecan/HSPG2 expression in glioblastoma tissues contribute to tumour development through the transformation of brain extracellular matrix into tumour microenvironment, and represent negative prognostic factors for glioblastoma progression.
Perlecan functions in autophagy and angiogenesis where its proangiogenesis activity is counteracted by endorepellin, the C-terminal fragment of perlecan, in these cellular and morphogenic events. (Review)
We found that perlecan expression decreased during chronological skin aging. Our in vitro studies revealed reduced perlecan transcript levels in aged keratinocytes. Perlecan down-regulation in cultured keratinocytes caused depletion of the cell population that expressed keratin 15 (show KRT15 Proteins).Finally, we found defects in keratin 15 (show KRT15 Proteins) expression in the epidermis of aging skin.
Putative stem cell populations associated with hair bulbs, humeral perichondrium, humeral and ulnar rudiment stromal/perivascular tissues expressed the Chondroitin sulfate motifs 4C3, 7D4, and 3B3[-] along with perlecan in close association but not colocalized.
Heterozygous variants in HSPG2 regulate the ATP2B4 (show ATP2B4 Proteins) expression via a variety of transcription factors including GATA1 (show GATA1 Proteins), RFX1 (show RFX1 Proteins) and MAZ (show MAZ Proteins).
the HSPG2-rs3767140 might be associated with the decreased fasting plasma glucose and LDL-C and with the increased HDL (show HSD11B1 Proteins)-C in diabetics.
Together, perlecan fragments in sera and MMP-7 (show MMP7 Proteins) in tissues of Prostate cancer patients are measures of invasive Prostate cancer.
Results show that perlecan has physical properties that would allow it to act as a strong but elastic tether in the lacunar canalicular system of cortical bone.
We were able to identify perlecan as the most likely candidate for the major estrogen-binding protein in the follicular fluid.
Nidogen-1 (show NID1 Proteins) and nidogen-2 (show NID2 Proteins) mRNAs were highly expressed in keratocytes, whereas perlecan was highly expressed in myofibroblasts.
RUS3108 is a novel perlecan-inducing compound which may prevent in-stent restenosis.
Perlecan is a defining factor in both the biochemical and biomechanical properties of the pericellular matrix.
Confocal laser scanning microscopy co-localised perlecan with type VI collagen as pericellular components of intervertebral disc (IVD (show IVD Proteins)) cells and translamellar cross-bridges in ovine and murine IVDs.
Perlecan knockdown altered matrix organization and significantly decreased the stiffness of both chondrocytes and interstitial matrix as a function of age and genotype.
Perlecan is required for the chondrogenic and adipogenic differentiation from SMCs via its regulation of the Sox9 (show SOX9 Proteins) and PPARgamma (show PPARG Proteins) gene expression, but not for osteogenic differentiation via Runx2 (show RUNX2 Proteins)
The reduced deposition of TGF-beta1 (show TGFB1 Proteins) observed in the present study would be expected to impact detrimentally on the remodelling and healing capacity of skin in mutant mice compounding on the poor wound-healing properties already reported for perlecan exon 3 null mice due to an inability to signal with FGF-2 (show FGF2 Proteins) and promote angiogenic repair processes.
Hspg2 inhibits autophagy to maintain muscle homeostasis in mouse soleus muscle.
Perlecan HS has significant roles in directing the development of posttraumatic OA, potentially via the alteration of FGF/HS/FGFR (show FGFR2 Proteins) signaling.
An in situ hybridization study of perlecan, DMP1, and MEPE in developing condylar cartilage of the fetal mouse mandible and limb bud cartilage.
LG3, through interactions with alpha2beta1 integrins on recipient-derived cells leading to activation of ERK1/2 and increased migration, favors myointimal thickening
Perlecan binds the clustering molecule gliomedin (show GLDN Proteins) and enhances clustering of node of Ranvier components.
perlecan deficiency alters cartilage matrix patterning and, as we now show, coordinately influences bone formation and calcification
Blocking of perlecan by anti-perlecan antiserum inhibited the migration of vascular endothelial cells (VECs) and bone marrow-derived mesenchymal stem cells, and exogenous perlecan added to the culture medium promoted the migration of these cell types.
Hyperglycemia-induced structural changes in perlecan may result in a subendothelial matrix that is more favorable to retention of monocytes. 2 forms of perlecan exist in BAEC SEM, 1 with HS chains only and 1 with both HS and CS/DS chains.
results suggest that perlecan made by growth plate chondrocytes is a low affinity receptor for FGF-2 (show FGF2 Proteins) and acts to sequester FGF-2 (show FGF2 Proteins) away from the high affinity receptor
data show that growth plate perlecan binds to FGF-2 (show FGF2 Proteins) by its heparan sulfate chains but can only deliver FGF-2 (show FGF2 Proteins) to FGF receptors when its chondroitin sulfate chains are removed.
This gene encodes the perlecan protein, which consists of a core protein to which three long chains of glycosaminoglycans (heparan sulfate or chondroitin sulfate) are attached. The perlecan protein is a large multidomain proteoglycan that binds to and cross-links many extracellular matrix components and cell-surface molecules. It has been shown that this protein interacts with laminin, prolargin, collagen type IV, FGFBP1, FBLN2, FGF7 and Transthyretin, etc. and plays essential roles in multiple biological activities. Perlecan is a key component of the vascular extracellular matrix, where it helps to maintain the endothelial barrier function. It is a potent inhibitor of smooth muscle cell proliferation and is thus thought to help maintain vascular homeostasis. It can also promote growth factor (e.g., FGF2) activity and thus stimulate endothelial growth and re-generation. It is a major component of basement membranes, where it is involved in the stabilization of other molecules as well as being involved with glomerular permeability to macromolecules and cell adhesion. Mutations in this gene cause Schwartz-Jampel syndrome type 1, Silverman-Handmaker type of dyssegmental dysplasia, and Tardive dyskinesia.
basement membrane-specific heparan sulfate proteoglycan core protein
, endorepellin (domain V region)
, perlecan proteoglycan
, heparan sulfate proteoglycan 2
, basement membrane-specific heparan sulfate proteoglycan core protein-like
, perlecan (heparan sulfate proteoglycan 2)