HSPG2 (heparan sulfate proteoglycan 2)

2008-10-01   Mary C Farach-Carson , Brian Grindel 

Department of Biological Sciences, University of Delaware, 209 Hullihen Hall, Newark DE 19716, USA





The HSPG2 gene consists of 115,014 bases and 97 exons. Evidence suggests that the encoded proteins modular structure is a result of gene duplication and exon shuffling (Cohen et al., 1993). The perlecan gene promoter lacks the TATA and CAAT boxes, but has four GC boxes and three GGGCGG hexanucleotides. The gene also was found to contain multiple start sites (Cohen et al., 1993).


The transcribed mRNA is 14,294 bp (Cohen et al., 1993). An alternative transcript for unc-52, the homologous gene to perlecan in C. elegans, has been reported (Spike et al., 2002). In addition, a human alternative transcript was submitted to the NCBI (Accession Q8TEU3_HUMAN) as a sequence for a short version variant, miniperl, encoding a 240 amino acid protein of 25.942 kD. Expression of HSPG2 was found to be induced by TGF-beta via NF-1 (Iozzo et al., 1997), and inhibited by NF-gamma via STAT1 (Sharma and Iozzo, 1998).


Atlas Image
Figure1: Perlecan as a Scaffold: Functional Uncoupling by Proteolysis (from Farach-Carson and Carson, 2007).


4,391 amino acids; 468,825 (core protein) to ~850,000 Da (depends upon amount of glycosaminoglycan (GAG) additions). Perlecan is composed of 5 domains. Following a 21 amino acid signal peptide for ER targeting is the N-terminal domain I, spanning amino acids 22-193 (Murdoch et al., 1992). Domain I contains 3 SGD sequences for attachment of heparan sulfate (HS) and/or chondroitin sulfate (CS) GAGs on serine residues, and a 120 amino acid SEA (Sperm protein, Enterokinase, Agrin) module. The SEA module has no definitive function, but deletion studies in domain I suggest it increases HS chain attachment (Dolan et al., 1997). Domain I of this protein is unique to perlecan, as it shares no significant homology with any other protein (Murdoch et al., 1992). The 210 amino acid domain II (amino acids 194-403) contains 4 cysteine-rich low-density lipoprotein (LDL) receptor-like modules. Adjacent to this is one immunoglobulin G (IgG)-like repeat (residues 404-504). Domain III (1,172 amino acids; residues 505-1676) consists of modules homologous to the short arm laminin alpha-chains including 3 laminin domain IV-like modules and eight laminin epidermal growth factor (EGF)-like repeats. Domain IV is the largest domain (2010 amino acids; residues 1677-3686), containing 21 IgG-like repeats (murine perlecan has only 14 IgG-like repeats, missing IgG repeats 5-12) similar to neural cell adhesion molecules (N-CAM). Domain V (705 amino acids; residues 3687-4391) has 3 modules with sequence homology to the globular domain of laminin alpha-chains and agrin. In addition, this domain contains 4 interspersed EGF-like repeats, and another GAG chain attachment site. Domain V of perlecan also is referred to as endorepellin for its angiostatic properties and was shown to be cleaved from perlecan by BMP-1/mTLL (Mongiat et al., 2003; Gonzalez et al., 2005). Several other cleavage sites are predicted for perlecan including sites for thrombin, plasmin, collagenase, and stromelysin, although some sites may be cryptic (Whitelock et al., 1996; dOrtho et al., 1997).
Atlas Image
Figure 2: from Farach-Carson and Carson, 2007.


Perlecan is expressed in the basement membranes of pituitary gland, skin, breast, thymus, prostate, colon, liver, pancreas, spleen, heart, and lung. Vascular basement membranes also express perlecan. In the subendothelial region, perlecan is highly expressed in the livers perisinusoidal space, spleen, lymph nodes, and pituitary gland (Murdoch et al., 1994). In the kidney, perlecan is found in the mesangium, Bowmans capsule, the tubular basement membrane, but is only slightly expressed in the glomerular basement membrane (Groffen et al., 1997). In bone, marrow but not the mineral compartment, is rich in perlecan (Schofield et al., 1999). In human fetal tissue (12-14 week old), pericellular perlecan expression was detected in the rudiment and growth plate chondrocytes, and was found in the perichondrial capillary networks and cartilage canals (Melrose et al., 2004).


Perlecan is found in the extracellular matrix (ECM), most commonly in the basement membrane underlying epithelial and endothelial cells. It also is found at high levels in cartilage, bone marrow and in muscle tissue.


Perlecan is a multifunctional protein involved in maintaining the basement membrane, growth factor binding and signaling, cell differentiation, angiogenesis, neuromuscular function and bone development. Perlecan is an important component of the basement membrane. It binds several other basement membrane proteins including aminin 1, fibronectin, nidogen, PRELP, and collagen IV via its core protein or HS chains (Sasaki et al., 1998; Hopf et al., 2001; Kvansakul et al., 2001; Bengtsson et al., 2002). Endorepellin (domain V) also interacts with cell surface integrins (alpha2beta1), forming additional complexes linking the ECM with the cell (Bix et al., 2004). The loss of perlecan and the basement membrane architecture is sometimes indicative of carcinomas, as is the case with invasive breast carcinoma (Nerlich et al., 1997). Perlecan has extensive growth factor regulating functions afforded to its ability to bind, sequester, and activate growth factors and growth factor binding proteins. This function connects perlecan to several actions concerning cell differentiation and proliferation. Perlecan has both pro-angiogenic (whole molecule) and anti-angiogenic (endorepellin) properties, linked to its ability regulate factors such as VEGF and FGF2. Consequently, perlecan has been implicated in supporting tumor angiogenesis in several cancers (reviewed in Bix and Iozzo, 2008). In all, perlecan has been shown to bind many growth factors including BMP-2, CTGF, PDGF, several FGFs, and VEGF and modulate several others (reviewed in Bix and Iozzo, 2008; Melrose et al., 2008). Perlecan has important functions in bone development. Perlecan sustains growth plate chondrocyte organization and hypertrophic chondrocytes, greatly assists endochondral ossification, and maintains cartilage stability in general (Arikawa-Hirasawa et al., 1999; Costell et al., 1999). The complex structure and function of perlecan suggest that it acts as an extracellular matrix scaffold. Based upon rotary shadowing of individual domains and atomic force microscopy, intact perlecan is predicted to span 100-200 nm (Chakravarti et al., 1995; Costell et al., 1996; Brown et al., 1997; Dolan et al., 1997; Hopf et al., 1999; Chen and Hansma, 2000). Given that this matches the dimensions of other scaffolding domains and that perlecan has a modular structure capable of binding many partners at once, perlecan may create stable "signalosomes" by clustering transmembrane proteins and stabilizing their interactions. As a result, perlecan may be essential in directing cell signaling and hence function as an extracellular signaling scaffold (Farach-Carson and Carson, 2007).
Atlas Image
Figure 3: Perlecan as a Scaffold: Domains and interactions (from Farach-Carson and Carson, 2007).


Mouse (~85%), Chicken (67%), Zebrafish (62%), Fruitfly (35%), Worm (35%).



Perlecan has 37 reported mutations. Over 34 mutations are attributed to Schwartz-Jampel Syndrome (SJS) and 3 are attributed to dyssegmental dysplasia, Silverman-Handmaker type (DDHS).
Atlas Image

Implicated in

Entity name
Prostate Cancer
Perlecan expression was correlated with aggressive prostate tumors (high Gleason score). Primary prostate cancer tumors and metastatic prostate cancer to the lung and liver showed increased perlecan expression, but metastasis to the lymph nodes showed decreased perlecan protein expression. Furthermore, perlecan expression was shown to promote survival of tumors in low androgen and/or low growth factor environments. Perlecan may mediate prostate cancer progression through its regulation of the sonic hedgehog signaling pathway, whose activity has been implicated in prostate cancer (Datta et al., 2006). Targeted reduction of perlecan in prostate cancer xenografts growing in mice reduced tumor growth and vascularization (Savorè et al., 2005).
Prostate cancer is an adenocarcimona affecting the gland cells of the prostate. It is a slow growing cancer usually affecting older men. The most common site of metastasis of prostate cancer is the bone.
Entity name
Breast Cancer
Perlecan mRNA expression was shown to be increased in invasive breast carcinomas, yet immunohistochemical analysis showed a lack of perlecan deposition in the carcinoma (Nerlich et al., 1997; Nerlich et al., 1998). This suggests subsequent proteolytic cleavage of perlecan or translational defects in breast cancer. However, in breast cancer stromal cells, high perlecan deposition was also reported (Iozzo et al., 1994).
Breast cancer refers to the many types of cancer affecting breast tissue including ductal carcinoma and lobular carcinoma. Breast cancers are further defined as in situ or invasive. An especially deadly form is inflammatory breast cancer. The most common target of breast cancer metastasis is the lymphatic system. It is the most common form of cancer for women and the second cause of cancer-related deaths for women.
Entity name
In metastatic melanoma, perlecan mRNA expression was increased 15 fold over normal tissue, which correlated with enhanced perlecan deposition in the melanomas pericellular matrix (Cohen et al., 1994). When perlecan expression was blocked with a perlecan antisense cDNA construct in metastatic melanoma cells, the proliferative and invasive properties were reduced. Perlecan serves as a reservoir for growth factors involved in angiogenesis and proliferation (VEGF, bFGF/FGF-2, FGF-7), and is needed for growth factor signaling. bFGF/FGF-2 was shown to be an important autocrine regulator of metastatic melanoma, and perlecan is needed for bFGF to advance melanoma. Without perlecan, growth factor activity is diminished, abrogating tumor progression (Adatia et al., 1997).
Melanoma is a type of skin cancer originating in the melanocytes.
Entity name
Colon cancer
When perlecan was blocked by antisense targeting in xenografts with human colon carcinoma cells and tumor allografts, tumor progression and neovascularization were substantially decreased in a mouse model. Perlecan inhibition is thought to suppress FGF-7 binding and receptor activation, thereby blocking tumor growth and angiogenesis (Sharma et al., 1998). As in other cancers, perlecan is a contributing factor in colon cancer progression.
Colon cancer usually begins as a non-cancerous adenomatous polyp and spreads into the wall of the colon, where it may metastasize through blood vessels or the lymphatic system.
Entity name
In contrast to other cancers, when perlecan was suppressed by antisense cDNA in fibrosarcoma cells, the phenotype became more aggressive in that they had increased migration, invasion, and adhesiveness to type IV collagen substrates. Perlecan action in fibrosarcoma is thought to be independent of the bFGF pathway and possibly prevent mesenchymal tumor invasion (Mathiak et al., 1997).
Fibrosarcoma is a type of malignant tumor originating in the connective tissue, mostly affecting the leg, arm, and jawbone in humans.
Entity name
Adenoid cystic carcinoma (ACC)
Perlecan expression was increased in ACC cells forming small stromal pseudocysts, but not in advanced flat ACC cells producing large pseudocysts or already attached to peripheral nerves, which have abundant perlecan. This suggests perlecan is needed for initial ACC cell growth (Kimura et al., 2000).
ACC is a tumor affecting the salivary glands. It is usually slow growing and not as aggressive as other salivary gland cancers.
Entity name
Intrahepatic cholangiocarcinoma (ICC)
Perlecan is highly expressed in the tumor specific fibro-myxoid stroma of ICC. In addition, the ICC cells on the invading fronts expressed higher levels of perlecan than other ICC cells, suggesting that perlecan is an important component of ICC tumor invasiveness (Sabit et al., 2001).
ICC is a tumor originating in the biliary system (bile ducts) of the liver. It is associated with the hepatitis C virus and chronic cholangitis.
Entity name
Amyloidosis and related diseases
In a murine model of AA amyloidogenesis perlecan expression increased before the deposits of AA amyloids, indicating that perlecan is required for the earliest stages of amyloid fibrillogenesis (Ailles et al., 1993). Perlecan was shown to accelerate beta-amyloid fibril formation and also stabilize the formed fibrils, demonstrating perlecans role in beta-amyloidogenesis in Alzheimers disease (Castillo et al., 1997). In addition, during hemodialysis induced beta2-microglobulin (beta2M) amyloidosis, increased amounts of HSPGs, like perlecan, direct where beta2M deposits will occur and assist fibrillogenesis (Ohashi, 2001).
Amyloidosis refers to a wide spectrum of diseases where the abnormal deposition of amyloid species (insoluble proteins in a beta-pleated secondary conformation) occurs in any organ or tissue. Alzheimers disease is an example of amyloidosis affecting the brain.
Entity name
Schwartz-Jampel Syndrome (SJS)
Mutations in the perlecan gene were implicated in SJS in 2000 by (Nicole et al., 2000). Two mutations are found in the C-terminal region of domain III, SJS1-H C1532Y and SJS1-B 4740G→A, resulting in lost disulfide bonds. One mutation was found in domain IV, SJS1-A IVS64+4a→g, leaving a truncated protein missing domain IV Ig-like repeats 13-21 and domain V. (Arikawa-Hirasawa et al., 2002) reported additional mutations resulting in early stop codons. (Stum et al., 2006) reported an additional 22 perlecan mutations. In all of these mutational analyses, no evidence of a founder effect existed. The mutated perlecan proteins are secreted in lower amounts or are more susceptible to proteases and have varying degrees of functionality, resulting in the defects characteristic of SJS. However, (Rodgers et al., 2007) using mice with site specific perlecan mutations suggested that it was not the truncated protein or faulty secretion, but a downregulation of perlecan at the transcriptional level. With respect to myotonia, perlecan was shown to localize acetylcholinesterase (AChE) to the neuromuscular junction. With less functional perlecan, AChE is largely absent at the synapse, resulting in a higher concentration of ACh. This aberrantly stimulates the ACh receptor causing muscle contractions associated with myotonia.
SJS is a rare autosomal recessive disease characterized by skeletal dysplasias and myotonia, a neuromuscular disorder resulting in prolonged muscle contraction. Patients with the disorder have short stature, blepharophimosis (drooping eyelids with reduced size, flat nasal bridge, underdeveloped orbital rim), pursed lips, low-set ears, myopia, and a fixed facial expression. SJS is characterized by several skeletal dysplasias including kyphoscloliosis, platyspondyly (flattened vertebrae), joint contractures, and metaphyseal and epiphyseal dysplasias. Based upon clinical examination, several other disorders including kyphomelic chondrodyplasia, Burtons disease, micromelic chondrodysplasia were suggested by (Spranger et al., 2000) to be reclassified as SJS.
Entity name
Dyssegmental dysplasia, Silverman-Handmaker type (DDHS)
Functional null mutations of perlecan have been implicated in DDHS. (Arikawa-Hirasawa et al., 2001) reported an 89-bp duplication in exon 34, and a 5 donor site mutation in intron 52 and exon 73, resulting in a truncated perlecan protein core. In contrast to SJS, the truncated perlecan protein is not secreted and deposited, causing a functional null mutation similar to the homozygous perlecan knockout mice. This manifests in more severe defects than SJS, as all DDHS individuals are stillbirths or die shortly thereafter.
DDSH is a rare autosomal recessive lethal disease characterized by severe skeletal dysplasias, anisospondyly and micromelia. DDSH patients also have a flat face, cleft palate, low joint mobility, micrognathia (undersized jaw), and encephalocoele. The endochondral growth plate has shortening defects, the resting cartilage shows mucoid degeneration, and hypertrophic chondrocytes produce calcospherites that fail to fuse.
Entity name
Intracranial aneurysms
Two SNPs in the perlecan gene were associated with intracranial aneurysms (Ruigrok et al., 2006). A defect in perlecan is thought to contribute to faulty ECM in the arterial wall, increasing the likelihood of an aneurysm.
An aneurysm is the dilation of the arterial wall due to defects in the ECM. A dilated blood vessel may rupture resulting in a subarachnoid hemorrhage.


Pubmed IDLast YearTitleAuthors
94963921997Suppression of invasive behavior of melanoma cells by stable expression of anti-sense perlecan cDNA.Adatia R et al
82311121993Induction of perlecan gene expression precedes amyloid formation during experimental murine AA amyloidogenesis.Ailles L et al
119415382002Structural and functional mutations of the perlecan gene cause Schwartz-Jampel syndrome, with myotonic myopathy and chondrodysplasia.Arikawa-Hirasawa E et al
118472102002The leucine-rich repeat protein PRELP binds perlecan and collagens and may function as a basement membrane anchor.Bengtsson E et al
152405722004Endorepellin causes endothelial cell disassembly of actin cytoskeleton and focal adhesions through alpha2beta1 integrin.Bix G et al
183002852008Novel interactions of perlecan: unraveling perlecan's role in angiogenesis.Bix G et al
94319881997The C-terminal domain V of perlecan promotes beta1 integrin-mediated cell adhesion, binds heparin, nidogen and fibulin-2 and can be modified by glycosaminoglycans.Brown JC et al
93756781997Perlecan binds to the beta-amyloid proteins (A beta) of Alzheimer's disease, accelerates A beta fibril formation, and maintains A beta fibril stability.Castillo GM et al
78144011995Recombinant domain III of perlecan promotes cell attachment through its RGDS sequence.Chakravarti S et al
109459692000Basement membrane macromolecules: insights from atomic force microscopy.Chen CH et al
82343071993Structural characterization of the complete human perlecan gene and its promoter.Cohen IR et al
79543961994Abnormal expression of perlecan proteoglycan in metastatic melanomas.Cohen IR et al
105797291999Perlecan maintains the integrity of cartilage and some basement membranes.Costell M et al
89149721996Structural characterization of recombinant domain II of the basement membrane proteoglycan perlecan.Costell M et al
165071122006Perlecan, a candidate gene for the CAPB locus, regulates prostate cancer cell growth via the Sonic Hedgehog pathway.Datta MW et al
90201501997Identification of sites in domain I of perlecan that regulate heparan sulfate synthesis.Dolan M et al
174427082007Perlecan--a multifunctional extracellular proteoglycan scaffold.Farach-Carson MC et al
155910582005BMP-1/Tolloid-like metalloproteases process endorepellin, the angiostatic C-terminal fragment of perlecan.Gonzalez EM et al
92490241997Evidence for the existence of multiple heparan sulfate proteoglycans in the human glomerular basement membrane and mesangial matrix.Groffen AJ et al
114930062001Mapping of binding sites for nidogens, fibulin-2, fibronectin and heparin to different IG modules of perlecan.Hopf M et al
79451861994The biology of perlecan: the multifaceted heparan sulphate proteoglycan of basement membranes and pericellular matrices.Iozzo RV et al
90305921997Structural and functional characterization of the human perlecan gene promoter. Transcriptional activation by transforming growth factor-beta via a nuclear factor 1-binding element.Iozzo RV et al
109932712000Perlecan (heparan sulfate proteoglycan) gene expression reflected in the characteristic histological architecture of salivary adenoid cystic carcinoma.Kimura S et al
115744652001Structural basis for the high-affinity interaction of nidogen-1 with immunoglobulin-like domain 3 of perlecan.Kvansakul M et al
91871091997A role for perlecan in the suppression of growth and invasion in fibrosarcoma cells.Mathiak M et al
184047012008Perlecan, the "jack of all trades" proteoglycan of cartilaginous weight-bearing connective tissues.Melrose J et al
155053352004Perlecan immunolocalizes to perichondrial vessels and canals in human fetal cartilaginous primordia in early vascular and matrix remodeling events associated with diarthrodial joint development.Melrose J et al
124357332003Endorepellin, a novel inhibitor of angiogenesis derived from the C terminus of perlecan.Mongiat M et al
75071421994Widespread expression of perlecan proteoglycan in basement membranes and extracellular matrices of human tissues as detected by a novel monoclonal antibody against domain III and by in situ hybridization.Murdoch AD et al
98589331998Morphological aspects of altered basement membrane metabolism in invasive carcinomas of the breast and the larynx.Nerlich AG et al
111018502000Perlecan, the major proteoglycan of basement membranes, is altered in patients with Schwartz-Jampel syndrome (chondrodystrophic myotonia).Nicole S et al
111484562001Pathogenesis of beta2-microglobulin amyloidosis.Ohashi K et al
172132312007Reduced perlecan in mice results in chondrodysplasia resembling Schwartz-Jampel syndrome.Rodgers KD et al
170384842006Evidence in favor of the contribution of genes involved in the maintenance of the extracellular matrix of the arterial wall to the development of intracranial aneurysms.Ruigrok YM et al
113506062001Enhanced expression of basement-membrane-type heparan sulfate proteoglycan in tumor fibro-myxoid stroma of intrahepatic cholangiocarcinoma.Sabit H et al
97629011998Inhibition of glycosaminoglycan modification of perlecan domain I by site-directed mutagenesis changes protease sensitivity and laminin-1 binding activity.Sasaki T et al
162834812005Perlecan knockdown in metastatic prostate cancer cells reduces heparin-binding growth factor responses in vitro and tumor growth in vivo.Savorè C et al
105279461999Expression of proteoglycan core proteins in human bone marrow stroma.Schofield KP et al
97889741998Antisense targeting of perlecan blocks tumor growth and angiogenesis in vivo.Sharma B et al
94685231998Transcriptional silencing of perlecan gene expression by interferon-gamma.Sharma B et al
123971082002MEC-8 regulates alternative splicing of unc-52 transcripts in C. elegans hypodermal cells.Spike CA et al
110384412000Spectrum of Schwartz-Jampel syndrome includes micromelic chondrodysplasia, kyphomelic dysplasia, and Burton disease.Spranger J et al
169273152006Spectrum of HSPG2 (Perlecan) mutations in patients with Schwartz-Jampel syndrome.Stum M et al
86265651996The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases.Whitelock JM et al
94612981997Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases.d'Ortho MP et al

Other Information

Locus ID:

NCBI: 3339
MIM: 142461
HGNC: 5273
Ensembl: ENSG00000142798


dbSNP: 3339
ClinVar: 3339
TCGA: ENSG00000142798


Gene IDTranscript IDUniprot

Expression (GTEx)



PathwaySourceExternal ID
ECM-receptor interactionKEGGko04512
ECM-receptor interactionKEGGhsa04512
Hepatitis BKEGGhsa05161
Proteoglycans in cancerKEGGhsa05205
Proteoglycans in cancerKEGGko05205
Metabolism of proteinsREACTOMER-HSA-392499
Diseases of glycosylationREACTOMER-HSA-3781865
Diseases associated with glycosaminoglycan metabolismREACTOMER-HSA-3560782
Defective B4GALT7 causes EDS, progeroid typeREACTOMER-HSA-3560783
Defective B3GAT3 causes JDSSDHDREACTOMER-HSA-3560801
Defective EXT1 causes exostoses 1, TRPS2 and CHDSREACTOMER-HSA-3656253
Defective EXT2 causes exostoses 2REACTOMER-HSA-3656237
Amyloid fiber formationREACTOMER-HSA-977225
Signal TransductionREACTOMER-HSA-162582
Visual phototransductionREACTOMER-HSA-2187338
Retinoid metabolism and transportREACTOMER-HSA-975634
Metabolism of carbohydratesREACTOMER-HSA-71387
Glycosaminoglycan metabolismREACTOMER-HSA-1630316
Heparan sulfate/heparin (HS-GAG) metabolismREACTOMER-HSA-1638091
A tetrasaccharide linker sequence is required for GAG synthesisREACTOMER-HSA-1971475
HS-GAG biosynthesisREACTOMER-HSA-2022928
HS-GAG degradationREACTOMER-HSA-2024096
Chondroitin sulfate/dermatan sulfate metabolismREACTOMER-HSA-1793185
Metabolism of vitamins and cofactorsREACTOMER-HSA-196854
Extracellular matrix organizationREACTOMER-HSA-1474244
Laminin interactionsREACTOMER-HSA-3000157
Non-integrin membrane-ECM interactionsREACTOMER-HSA-3000171
Degradation of the extracellular matrixREACTOMER-HSA-1474228
Integrin cell surface interactionsREACTOMER-HSA-216083
Defective B3GALT6 causes EDSP2 and SEMDJL1REACTOMER-HSA-4420332
Metabolism of fat-soluble vitaminsREACTOMER-HSA-6806667

Protein levels (Protein atlas)

Not detected


Entity IDNameTypeEvidenceAssociationPKPDPMIDs


Pubmed IDYearTitleCitations
241015242013Cancer cell exosomes depend on cell-surface heparan sulfate proteoglycans for their internalization and functional activity.223
152405722004Endorepellin causes endothelial cell disassembly of actin cytoskeleton and focal adhesions through alpha2beta1 integrin.88
199131212009Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.85
120368762002Identification of integrin alpha(M)beta(2) as an adhesion receptor on peripheral blood monocytes for Cyr61 (CCN1) and connective tissue growth factor (CCN2): immediate-early gene products expressed in atherosclerotic lesions.81
129004242003A novel interaction between perlecan protein core and progranulin: potential effects on tumor growth.51
215967512011Endorepellin, the angiostatic module of perlecan, interacts with both the α2β1 integrin and vascular endothelial growth factor receptor 2 (VEGFR2): a dual receptor antagonism.45
180244322008Integrin alpha2beta1 is the required receptor for endorepellin angiostatic activity.42
128118192003CTGF/Hcs24, hypertrophic chondrocyte-specific gene product, interacts with perlecan in regulating the proliferation and differentiation of chondrocytes.37
206738682010A genetic association study of maternal and fetal candidate genes that predispose to preterm prelabor rupture of membranes (PROM).36
276135012017A current view of perlecan in physiology and pathology: A mosaic of functions.36


Mary C Farach-Carson ; Brian Grindel

HSPG2 (heparan sulfate proteoglycan 2)

Atlas Genet Cytogenet Oncol Haematol. 2008-10-01

Online version: http://atlasgeneticsoncology.org/gene/40890/hspg2-(heparan-sulfate-proteoglycan-2)