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HAPLN1


Official Full Name
hyaluronan and proteoglycan link protein 1
Organism
Homo sapiens
Gene ID
1404
Background
Predicted to enable hyaluronic acid binding activity. Predicted to be an extracellular matrix structural constituent conferring compression resistance. Predicted to be involved in nervous system development; positive regulation of neuroblast proliferation; and skeletal system development. Located in collagen-containing extracellular matrix. [provided by Alliance of Genome Resources, Feb 2025]
Synonyms
CRT1; CRTL1

Cat.No. Product Name Price
SHH113933 shRNA set against Mouse Hapln1(NM_013500.4) Inquiry
SHH113937 shRNA set against Rat Hapln1(NM_019189.2) Inquiry
SHH310289 shRNA set against Human HAPLN1 (NM_001884.3) Inquiry
SHH310293 shRNA set against Mouse HAPLN1 (NM_013500.4) Inquiry
SHH310297 shRNA set against Rat HAPLN1 (NM_019189.2) Inquiry
SHW005974 shRNA set against Chicken HAPLN1 (NM_205482) Inquiry
Cat.No. Product Name Price
CDFR011487 Rat Hapln1 cDNA Clone(NM_019189.2) Inquiry
MiUTR1M-05538 HAPLN1 miRNA 3'UTR clone Inquiry
MiUTR1R-02379 HAPLN1 miRNA 3'UTR clone Inquiry
MiUTR4H-TG11399 HAPLN1 miRNA 3'UTR clone Inquiry
CDCB167449 Chicken HAPLN1 ORF Clone (NM_205482) Inquiry
CDCB184401 Rabbit HAPLN1 ORF clone (XM_008261911.1) Inquiry
CDCL151092 Mouse Hapln1 ORF clone (NM_013500.4) Inquiry
CDCL184546 Human HAPLN1 ORF clone(NM_001884.3) Inquiry
CDCR378520 Rat Hapln1 ORF Clone(NM_019189.2) Inquiry
CDCS410495 Human HAPLN1 ORF Clone (BC057808) Inquiry

Detailed Information

Recent Research Progress

HAPLN1, Hyaluronan And Proteoglycan Link Protein 1, is an acid glycoprotein with 354-amino. It belongs the link protein gene family which consists of four HAPLN members. Similar to the other three link proteins, structure of HAPLN1 has NH2-terminal signal sequence followed by immunoglobulin-like domain and two link modules or proteoglycan tandem repeats. Interestingly, proteoglycan tandem repeats mentioned above, or link modules, is the main site for mediating binding to hyaluronic acid (HA). All structures of HAPLN1 above indicate that it has some pathological activity in some field as the recent studies.

Some researches proved that serving as a major component of cartilage extracellular matrix (ECM), HAPLN1 stabilizes aggregates of aggrecan and HA. In the absence of HAPLN1, aggregates are smaller and less stable. HAPLN1 binds to aggrecan on the HA chain in a 1:1 ratio. The obtained aggregates are captured within the mesh-like network of type II collagen fibrils producing a large stable macromolecular structures, which contributes to resist compression and shock absorption in the joint. Although HAPLN1 is a major component of cartilage ECM, it is also highly expressed in noncartilaginous tissues such as small intestine and placenta, embryonic and adult heart tissues, and, to a lower extent, many other tissues.

HAPLN1 and tumorigenesis

Some progress of expression of HAPLN1 in cancers and its significance for tumorigenesis has been made. Sihem Mebarki et al. showed that there are two tight gene networks associating cell surface Wnt signaling, stem/progenitor markers and mesenchymal commitment in hepatocellular carcinomas (HCCs). Both networks were linked by Hyaluronan And Proteoglycan Link Protein 1 (HAPLN1), which appeared de novo in aggressive HCCs expressing cytoplasmic β-catenin and stem cell markers. HAPLN1 was independently associated with bad overall and disease-free outcome. So they has come to a conclusion that HAPLN1 reflects a signaling network leading to stemness, mesenchymal commitment and hepatocellular carcinomas progression. ZENGZENG WANG et al. indicated that HAPLN1 may be involved in the pathogenesis of clear cell renal cell carcinoma as HAPLN1 was lowly expressed and highly methylated in clear cell renal cell carcinoma tissues. Interestingly, a related research has showed that HAPLN1 is a novel pathogenic factor in multiple myeloma (MM) that induces the activation of an atypical NF-κB, a family of transcription factors that play a key role in cell survival and proliferation in MM, and thereby promotes the resistance of bortezomib which is a proteasome inhibitor used in the management of MM, inhibiting both canonical and noncanonical activation of NF-κB in MM cells.

HAPLN1 and other diseases

According to rencent researches, HAPLN1 also has an impact on other diseases. As some research reported, by upregulating HAPLN1 and downregulating Versican at the terminal stage, human bone marrow mesenchymal stromal cells (MSCs) can ameliorate progression of amyotrophic lateral sclerosis (ALS) which is a progressive neurodegenerative disorder resulting in a lethal outcome, significantly improve motor activity, and prolong survival. What’s more, there has been a research showed that as some extracellular matrix proteins including HAPLN1 are highly expressed in human cartilage and human articular chondrocytes, a low oxygen microenvironment may act to modulate cell proliferation and chondrogenic differentiation of both AMSCs and chondrocytes.

References:

  1. Mebarki, et al. De novo HAPLN1 expression hallmarks wnt-induced stem cell and fibrogenic networks leading to aggressive human hepatocellular carcinomas. Oncotarget, 2016, 7(26): 39026-39043.
  2. ZENGZENG WANG, et alIdentification of potential pathogenic biomarkers in clear cell renal cell carcinoma. Oncology Letters, 2018, 15(6):8491-8499.
  3. Forostyak S, et al. Intrathecal Delivery of Mesenchymal Stromal Cells Protects the Structure of Altered Perineuronal Nets in SOD1 Rats and Amends the Course of ALS. Stem Cells, 2014, 32(12):3163-72.
  4. Huynh M, et al. Hyaluronan and proteoglycan link protein 1 (HAPLN1) activates bortezomib-resistant NF-κB activity and increases drug resistance in multiple myeloma. Journal of Biological Chemistry, 2017, 293(7):jbc.RA117.000667.
  5. Galeano-Garces, et al. Molecular Validation of Chondrogenic Differentiation and Hypoxia Responsiveness of Platelet-Lysate Expanded Adipose Tissue–Derived Human Mesenchymal Stromal Cells. CARTILAGE, 2017, 8(3):283-299.
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