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HSPG2 encodes the perlecan protein, which consists of a core protein to which three long chains of glycosaminoglycans (heparan sulfate or chondroitin sulfate) are attached. Additionally we are shipping HSPG2 Antibodies (57) and HSPG2 Kits (12) and many more products for this protein.
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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.
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.
Knockdown of agrin (show AGRN Proteins) and perlecan promoted a decrease on cell migration and adhesion, and on resistance of cells to cisplatin.
As five of the seven missense mutations in Schwartz-Jampel syndrome affect domain III of perlecan, domain III is likely to be essential for secretion of perlecan into the extracellular space.
Rare variants in the HSPG2 gene potentially contribute to the idiopathic scoliosis phenotype in a subset of patients with idiopathic scoliosis
The perlecan is the primary ECM (show MMRN1 Proteins) molecule comprising intraepithelial stroma of the junctional epithelium, in which leukocytes may migrate on ECM (show MMRN1 Proteins) scaffolds in intercellular space toward the surface of the gingival sulci or pockets.
We conclude that enzymatic processing of perlecan in the BM or territorial matrix by MMP-7 (show MMP7 Proteins) as occurs in the invasive tumor microenvironment acts as a molecular switch to alter PCa (show FLVCR1 Proteins) cell behavior and favor cell dispersion and invasiveness.
Mutant genes (CELA1, HSPG2, and KCNK5) in Balkan endemic nephropathy patients encode proteins involved in basement membrane/extracellular matrix and vascular tone, tightly connected to process of angiogenesis.
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.
Perlecan is a defining factor in both the biochemical and biomechanical properties of the pericellular matrix.
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
applied a fluorescent technique to older mice expressing or deficient for perlecan/HSPG2, a large heparan-sulfate proteoglycan normally secreted in osteocytic PCM (show PCMT1 Proteins)
[review] Perlecan domain V is present acutely and chronically after ischemic stroke and could have a role in acute neuroprotection and chronic neurorepair at the site of stroke brain injury.
Synovial perlecan plays an important role in osteophyte development in osteoarthritis.
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.
heparan sulfate proteoglycan 2
, basement membrane-specific heparan sulfate proteoglycan core protein-like
, basement membrane-specific heparan sulfate proteoglycan core protein
, endorepellin (domain V region)
, perlecan proteoglycan
, perlecan (heparan sulfate proteoglycan 2)