proteoglycan

Plays a role in boundary lubrication within articulating joints. Prevents protein deposition onto cartilage from synovial fluid by controlling adhesion-dependent synovial growth and inhibiting the adhesion of synovial cells to the cartilage surface.; Isoform F plays a role as a growth factor acting on the primitive cells of both hematopoietic and endothelial cell lineages. Proteoglycan 4 Protein, Human, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 16.8 kDa and the accession number is Q92954.

Proteoglycan 4 Protein, Human, Recombinant (His & Myc) is expressed in Baculovirus.

Proteoglycan 3, also known as Eosinophil major basic protein homolog, Prepro-major basic protein homolog, PRG3 and MBPH, contains one C-type lectin domain. Proteoglycans are a major component of the animal extracellular matrix. PRG3 localizes to the eosinophil secondary granule and is expressed in bone marrow, not detected in placenta. PRG3 has similar cytotoxic and cytostimulatory activities to PRG2/MBP. In vitro, PRG3 can stimulate neutrophil superoxide production and IL8 release, histamine and leukotriene C4 release from basophils.

May affect the rate of fibrils formation. Decorin Protein, Bovine, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 40.5 kDa and the accession number is P21793.

HSPG2 Protein, Human, Recombinant (His & Myc) is expressed in HEK293.

CSPG4 Protein, Human, Recombinant (His & Myc) is expressed in HEK293 mammalian cells with N-10xHis and C-Myc tag. The predicted molecular weight is 73.2 kDa and the accession number is Q6UVK1.

May function in hyaluronic acid binding. HAPLN3 Protein, Mouse, Recombinant (His & Myc) is expressed in HEK293 mammalian cells with N-10xHis and C-Myc tag. The predicted molecular weight is 43.9 kDa and the accession number is Q80WM5.

May be involved in collagen fiber assembly. Biglycan Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 43.4 kDa and the accession number is P28653.

Brevican Core Protein (BCAN) is a secreted protein that belongs to the aggrecan/versican proteoglycan family. BCAN contains one C-type lectin domain, one EGF-like domain, one Ig-like V-type domain, one Sushi (CCP/SCR) domain and two Link domains. BCAN may play a role in the terminally differentiating and the adult nervous system during postnatal development. BCAN could stabilize interactions between hyaluronan (HA) and brain proteoglycans.

May function in hyaluronic acid binding. HAPLN3 Protein, Human, Recombinant (His) is expressed in Baculovirus insect cells with N-10xHis tag. The predicted molecular weight is 41.6 kDa and the accession number is Q96S86.

Binds to hyaluronic acid and may be involved in formation of the extracellular matrix.

Bone Marrow Proteoglycan (BMPG) is a secreted protein that contains one C-type lectin domain. BMPG is the predominant constituent of the crystalline core of the eosinophil granule. BMPG is highly expressed in placenta and pregnancy serum. BMPG may be involved in antiparasitic defense mechanisms as a cytotoxin and helminthotoxin. BMPG induces non-cytolytic histamine release from human basophils. In addition, BMPG also participated in antiparasitic defense mechanisms and immune hypersensitivity reactions.

Decorin, also known as PG40 and DCN, is a member of the class I family of small leucine-rich proteoglycans (SLRPs) that is expressed in the stroma of various forms of cancer and has been recently proposed to act as a guardian from the matrix. Mature human Decorin contains 12 tandem LRR and shares 80% and 78% aa sequence identity with mouse and rat Decorin, respectively. Decorin embraces numerous functions including: regulation of collagen fibrillogenesis, hepatic carcinogenesis, fetal membrane and calcium homeostasis, keratinocyte function, and suppression of angiogenesis. Most recently, soluble decorin has been shown to induce autophagy in endothelial cells and mitophagy in breast carcinoma cells.

Cytotoxin and helminthotoxin. Also induces non-cytolytic histamine release from human basophils. Involved in antiparasitic defense mechanisms and immune hypersensitivity reactions. The proform acts as a proteinase inhibitor, reducing the activity of PAPPA. PRG2 Protein, Human, Recombinant (GST & His) is expressed in E. coli expression system with N-6xHis-GST tag. The predicted molecular weight is 41.2 kDa and the accession number is P13727.

HAPLN3 Protein, Mouse, Recombinant (E. coli, His & Myc) is expressed in E. coli.

Exostosin-like 2 (EXTL2) is a member of the exostosin (EXT)-related family which contains five members: EXT1, EXT2, EXTL1, EXTL2, and EXTL3. Studies have shown that EXT gene family members have the activities of heparan sulfate-synthesizing glycosyltransferases. EXT1 and EXT2, which have been identified as causal genes for hereditary multiple exostoses, have HS-GlcAT-II and GlcNAcT-II activities. EXTL1 has GlcNAcT-II activity and EXTL3 has GlcNAcT-I and -II activities. EXTL2 has GlcNAcT-I and N-acetylgalactosaminyltransferase activities, and transfers a GlcNAc residue to the tetrasaccharide linkage region when this region is phosphorylated by a xylose kinase 1 (FAM20B) and thereby terminate chain elongation. In mice, lack of EXTL2 causes glycosaminoglycan (GAG) overproduction and structural changes of GAGs associated with pathological processes.

Mediates a firm binding of versican V2 to hyaluronic acid. May play a pivotal role in the formation of the hyaluronan-associated matrix in the central nervous system (CNS) which facilitates neuronal conduction and general structural stabilization. Binds to hyaluronic acid.

May participate in diverse steps of neurogenesis. Binds calcium. Testican-2 Protein, Mouse, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 52.1 kDa and the accession number is Q9ER58.

Hyaluronan (HA) is a high MW glycosaminoglycan significantly involved in the formation and stability of extracellular matrix via its association with specific HA-binding proteins. HAPLN1, also known as CRTL1 (Cartilage Link Protein 1, CLP) and link protein, is a member of the HA-binding protein (hyaladherins) family, and contains a common structural domain of about 100 amino acids that is termed a Link module with two α-helices and two antiparallel β-sheets. HAPLN1/CRTL1 stabilizes the interaction between hyaluronan (HA) and versican, two extracellular matrix components essential for cardiac development. Link module superfamily can be divided into three subgroups, and the HAPLN family are C domain-type proteins that have an extended structure with one N-terminal V-type Ig-like domain followed by two link modules. In cartilage, aggrecan forms - CLP stabilized aggregates with HA that provides the tissue with its load-bearing properties. HAPLN1 is a component of the follicular matrix, was shown to enhance cumulus-oocyte complex (COC) expansion in vitro. HAPLN1 may promote periovulatory granulosa cell survival, which would facilitate their differentiation into luteal cells.

Osteonectin, also known as SPOCK1, is an extracellular heparan/chondroitin sulfate proteoglycan. Members of this family are known as testicans, also called SPOCKs. They are characterized structurally by an N-terminal testican-specific domain, a follistatin-like region, a calcium-binding domain, a thyroglobulin-like domain, and an acidic C-terminal domain with two putative glycosaminoglycan attachment sites. SPOCKs are enriched in brain and have been shown to regulate neuronal attachment and outgrowth. They contain inhibitory regions in several domains targeted to different classes of protease, and in some cases may act as protease inhibitors. Osteonectin contains 1 Kazal-like domain and 1 thyroglobulin type-1 domain. Up to now, little is known about osteonectin’s function. It may play a role in cell-cell and cell-matrix interactions. Osteonectin also may contribute to various neuronal mechanisms in the central nervous system.

Keratan sulfate proteoglycan lumican, mostly known as lumican, belongs to the SLRP class II subfamily and the small leucine-rich proteoglycan (SLRP) family. Lumican binds to laminin. It has positive regulation of transcription from RNA polymerase II promoter and transforming growth factor beta1 production. Lumican is expressed in a variety of tissues, including skin, artery, lung, cornea, kidney, bone, aorta, and articular cartilage. The abnormal connective tissue phenotype seen in the Lumican null mice shows the importance of the role of Lumican in collagen fibrillogenesis. In addition to the control of collagen fibril assembly, Lumican has been shown to play a role in the regulation of cell proliferation, migration, and adhesion.

Syndecan-2 is a member of the Syndecans family comprised of type I transmembrane heparan sulfate proteoglycans (HSPG) that are involved in the regulation of many cellular processes. Four sub-types of mammalian Syndecans have been reported and among them. Syndecan-2 plays a role in the cancer development. It can affect the basal and chemotherapy-induced apoptosis in osteosarcoma. It can also suppress MMP2 activation, suppressing metastasis.

CALEB also known as chondroitin sulfate proteoglycan (CSPG)5 or neuroglycan C, is a neural chondroitin sulfate-containing and epidermal growth factor (EGF)-domain-containing transmembrane protein that is implicated in synaptic maturation. An involvement of CALEB in the presynaptic differentiation of cerebellar GABAergic synapses and revealed a new role for CALEB in synapse elimination in Purkinje cells.

May function in hyaluronic acid binding. HAPLN3 Protein, Human, Recombinant (E. coli, His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 42.8 kDa and the accession number is Q96S86.

May play a role in intercellular signaling and in connecting cells with the extracellular matrix. May take part in the regulation of cell motility, growth and differentiation. Binds hyaluronic acid.

May play a role in intercellular signaling and in connecting cells with the extracellular matrix. May take part in the regulation of cell motility, growth and differentiation. Binds hyaluronic acid. VCAN Protein, Mouse, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 20.9 kDa and the accession number is Q62059.

SPOCK3 Protein, Mouse, Recombinant (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 48.3 kDa and the accession number is Q8BKV0-1.

The Glypicans are a small multigene family of GPI-linked proteoglycans that play a key role in growth factor signaling. Human Glypican 1 (GPC1) is synthesized as a 558 amino acid (aa) preproprecursor that contains a 23 aa signal sequence, a 507 aa mature segment, and a 28 aa C-terminal prosegment. There are two potential N-linked and four potential O-linked sites for glycosylation or glycanation. There are potentially two heparan sulfate (HS) modifications on GPC1 that could contribute to a native molecular weight of approximately 200 kDa. Mature human GPC1 shares 91% aa identity with mature mouse GPC1. Cells known to express GPC1 include neurons, smooth and skeletal muscle cells, keratinocytes, osteoblasts, Schwann cells, immature dendritic cells, and tumor, plus tumorassociated vascular endothelial cells. The function of GPC1 is complex and varied. As a proteoglycan, it appears to make use of its HS adduct to impact select growth factor activity. This is accomplished by having juxtramembrane HS attachment sites, and a flexible, GPI-linkage.

Chondroitin sulfate proteoglycan 5 (CSPG-5), also known as neuroglycan C, has been previously associated to differentiation since it shapes neurite growth and synapse forming. CSPG-5 expression shifts in brain areas of the default mode network of suicide victims, which may reflect an impact in the pathogenesis of psychiatric diseases or support diagnostic power.

Tryptases are Trypsin-like Serine Proteases. β-Tryptases are the main isoenzymes in mast cells. Βtryptases form active tetramers with heparin proteoglycan. In the tetramer, the unique arrangement of the active sites facing a narrow central pore, β-Tryptases are resistant to macromolecule protease inhibitors . When mast cells are activated, β-Tryptases are released and participate in provoking inflammatory conditions . β-Tryptases have been implicated as mediators in the pathogenesis of asthma and other allergic disorders.

Interleukin-17 is a potent pro-inflammatory cytokine produced by activated memory T cells. There are at least six members of the IL-17 family in humans and in mice. Mature mouse IL-17A shares 61% and 89% amino acid sequence identity with human and rat IL-17A, respectively. As IL-17 shares properties with IL-1 and TNF-alpha, it may induce joint inflammation and bone and cartilage destruction. This cytokine is found in synovial fluids of patients with rheumatoid arthritis, and produced by rheumatoid arthritis synovium. It increases IL-6 production, induces collagen degradation and decreases collagen synthesis by synovium and cartilage and proteoglycan synthesis in cartilage. IL-17 is also able to increase bone destruction and reduce its formation. Blocking of interleukin-17 with specific inhibitors provides a protective inhibition of cartilage and bone degradation.

Fibromodulin (FMOD), an ECM small leucine-rich proteoglycan (SLRP), was reported to promote angiogenesis not only during wound healing, but also in optical and cutaneous angiogenesis-dependent diseases. The autocrine FMOD of cancer cells may promote tumor angiogenesis of SCLC by upregulating the expression of angiogenic factors that act in concert to facilitate the angiogenic phenotype of endothelial cells as a proangiogenic factor. Therefore, silencing FMOD may be a potentially clinical therapy for repressing tumor angiogenesis.

Interleukin-17 is a potent pro-inflammatory cytokine produced by activated memory T cells. There are at least six members of the IL-17 family in humans and in mice. As IL-17 shares properties with IL-1 and TNF-alpha, it may induce joint inflammation and bone and cartilage destruction. This cytokine is found in synovial fluids of patients with rheumatoid arthritis, and produced by rheumatoid arthritis synovium. It increases IL-6 production, induces collagen degradation and decreases collagen synthesis by synovium and cartilage and proteoglycan synthesis in cartilage. IL-17 is also able to increase bone destruction and reduce its formation. Blocking of interleukin-17 with specific inhibitors provides a protective inhibition of cartilage and bone degradation.

Aggrecan is a large proteoglycan that forms giant hydrated aggregates with hyaluronan in the extracellular matrix (ECM). The extraordinary resistance of these aggregates to compression explains their abundance in articular cartilage of joints where they ensure adequate load-bearing. In the brain, they provide mechanical buffering and contribute to formation of perineuronal nets, which regulate synaptic plasticity. Aggrecan is also present in cardiac jelly, developing heart valves, and blood vessels during cardiovascular development. Whereas aggrecan is essential for skeletal development, its function in the developing cardiovascular system remains to be fully elucidated.

Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. Could also be a critical factor in the exacerbation of neurodegeneration in Alzheimer disease. Cleaves aggrecan at the '392-Glu-|-Ala-393' site. ADAMTS4 Protein, Human, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 39.0 kDa and the accession number is O75173.

Lumican, a prototypic leucine-rich proteoglycan with keratan sulfate side chains, is a major component of the cornea, dermal, and muscle connective tissues. In these bifunctional molecules, the protein moiety binds collagen fibrils and the highly charged hydrophilic glycosaminoglycans regulate interfibrillar spacings. Lumican is the major keratan sulfate proteoglycan of the cornea but is also distributed in interstitial collagenous matrices throughout the body. Lumican regulates collagenous matrix assembly as a keratan sulfate proteoglycan in the cornea and is also present in the connective tissues of other organs and embryonic corneal stroma as a glycoprotein. Lumican may regulate collagen fibril organization and circumferential growth, corneal transparency, and epithelial cell migration, and tissue repair. lumican expressed in injured epithelium may modulate cell behavior such as adhesion or migration, thus contributing to corneal epithelial wound healing. Lumican plays a crucial role in the regulation of collagen assembly into fibrils in various connective tissues and serve as a definitive link between a necessity for lumican in the development of a highly organized collagenous matrix and corneal transparency.

Angiopoietin-like 7 (ANGPTL7) is a secreted glycoprotein that is structurally related to the angiopoietins. Members of this protein family contain an N-terminal coiled coil domain and a C-terminal fibrinogen-like domain. ANGPTL7 shares 89% aa sequence identity with mouse and rat ANGPTL7. It is secreted as a 45-50kDa monomer that forms disulfide-linked homotrimers and tetramers via the coiled coil domain. ANGPTL7 is expressed in the corneal stroma, trabecular meshwork, and sclera and is elevated in glaucoma aqueous humor. Its production is up-regulated in trabecular meshwork cells by glucocorticoids and TGF-β and in cartilage by TNF-α. Overexpression of ANGPTL7 in trabecular meshwork cells inhibits the production of collagen and proteoglycans. When overexpressed in tumor cells it promotes collagen and proteoglycan deposition but inhibits tumor xenograft progression and tumor angiogenesis.

Human P-Selectin (GMP-140, LECAM-3, PADGEM, CD62P), a member of the Selectin family, is a cell surface glycoprotein expressed by activated platelets and endothelial cells. A SLe(x)-type proteoglycan, which through high affinity, calcium-dependent interactions with E-, P- and L-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation.

The chondroitin sulfate proteoglycan-4 (CSPG4) is a cell surface proteoglycan overexpressed in a huge range of human and canine neoplastic lesions by tumor cells, tumor microenvironment and cancer initiating cells. CSPG4 plays a central role in the oncogenic pathways required for malignant progression and metastatization.

B3GAT3, encoding beta-1,3-glucuronyltransferase 3, has an important role in proteoglycan biosynthesis. Homozygous B3GAT3 mutations have been associated with short stature, skeletal deformities, and congenital heart defects. There is a novel B3GAT3-related disorder with craniosynostosis and bone fragility, due to a unique homozygous mutation in B3GAT3.

CHST11, also known as C4ST-1, belongs to the sulfotransferase 2 family. CHST11 localizes to the golgi membrane, and catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage, and is distributed on the surfaces of many cells and extracellular matrices. A chromosomal translocation involving CHST11 gene and IgH, t(12;14)(q23;q32), has been reported in a patient with B-cell chronic lymphocytic leukemia.

Carbohydrate sulfotransferase 3, also known as Chondroitin 6-O-sulfotransferase 1, Chondroitin 6-sulfotransferase and CHST3, is a single-pass type II membrane protein which belongs to thesulfotransferase 1 family and Gal / GlcNAc / GalNAc subfamily. CHST3 is widely expressed in adult tissues. It is expressed in heart, placenta, skeletal muscle and pancreas. CHST3 is also expressed in various immune tissues such as spleen, lymph node, thymus and appendix. CHST3 catalyzes the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. It is a chondroitin sulfate which constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. It can also sulfate Gal residues of keratan sulfate, another glycosaminoglycan, and the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides. It may play a role in the maintenance of naive T-lymphocytes in the spleen. Defects in CHST3 are the cause of spondyloepiphyseal dysplasia Omani type (SED Omani type) which is an autosomal recessive disorder characterized by normal length at birth but severely reduced adult height (11-13 cm), severe progressive kyphoscoliosis, arthritic changes with joint dislocations, genu valgum, cubitus valgus, mild brachydactyly, camptodactyly, microdontia and normal intelligence. As a consequence of the arthropathy and the contractures, affected individuals develop restricted joint movement. Defects in CHST3 are also a cause of humerospinal dysostosis (HSD) which is characterized by bifurcation of the ends of the humerus, subluxation in the elbow joints, widened iliac bones, talipes equinovarus and coronal cleft vertebrae. Congenital, progressive heart disease, possibly with fatal outcome, is observed in some patients.

Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-9 (gelatinase B) can degrade a broad range of substrates including gelatin, collagen types IV and V, elastin and proteoglycan core protein. It is believed to act synergistically with interstitial collagenase (MMP1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-9 is produced by keratinocytes, monocytes, macrophages and PMN leukocytes. MMP-9 is present in most cases of inflammatory responses. Structurally, MMP-9 may be divided into five distinct domains: a prodomain which is cleaved upon activation, a gelatinbinding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a prolinerich linker region, and a carboxyl terminal hemopexinlike domain.

Cell surface receptor that binds to glycosaminoglycans, including chondroitin sulfate proteoglycans and heparan sulfate proteoglycans. Binding to chondroitin sulfate and heparan sulfate proteoglycans has opposite effects on PTPRS oligomerization and regulation of neurite outgrowth. Contributes to the inhibition of neurite and axonal outgrowth by chondroitin sulfate proteoglycans, also after nerve transection. Plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. Required for normal brain development, especially for normal development of the pituitary gland and the olfactory bulb. Functions as tyrosine phosphatase. Mediates dephosphorylation of NTRK1, NTRK2 and NTRK3. Plays a role in down-regulation of signaling cascades that lead to the activation of Akt and MAP kinases. Down-regulates TLR9-mediated activation of NF-kappa-B, as well as production of TNF, interferon alpha and interferon beta.

OGN (Osteoglycin) is a Protein Coding gene. This gene encodes a member of the small leucine-rich proteoglycan (SLRP) family of proteins. It belongs to the small leucine-rich proteoglycan (SLRP) family. The encoded protein induces ectopic bone formation in conjunction with transforming growth factor-beta and may regulate osteoblast differentiation. OGN is broadly expressed in the gall bladder, endometrium, and other tissues. OGN reduced Zeb-1 expression via EGFR/Akt leading to inhibition of epithelial-mesenchymal transition. In vitro and in vivo, the OGN expression was demonstrated to reduce cell proliferation, inhibit invasion of colon cancer cells then impede cancer progression. Diseases associated with OGN include Inhibited Male Orgasm and Cornea Plana.