Syndecan 1

Syndecan 1

Syndecan 1
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols  ; CD138; SDC; SYND1; syndecan
External IDs GeneCards:
RNA expression pattern
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Syndecan 1 is a protein which in humans is encoded by the SDC1 gene.[1][2]


  • Function 1
  • Application 2
  • References 3
  • Further reading 4
  • External links 5


The protein encoded by this gene is a transmembrane (type I) HIV-1 tat protein. The syndecan-1 protein functions as an integral membrane protein and participates in cell proliferation, cell migration and cell-matrix interactions via its receptor for extracellular matrix proteins. Syndecan-1 is a sponge for growth factors, with binding largely via heparan sulfate chains.

An exception is the prosecretory mitogen lacritin that binds syndecan-1 only after heparanase modification.[3][4] Binding utilizes an enzyme-regulated 'off-on' switch in which active epithelial heparanase (HPSE) cleaves off heparan sulfate to expose a binding site in the N-terminal region of syndecan-1's core protein.[3]Three SDC1 elements are required. (1) The heparanase-exposed hydrophobic sequence GAGAL that promotes the alpha helicity of lacritin's C-terminal amphipathic alpha helix form and likely binds to the hydrophobic face. (2) Heparanase-cleaved heparan sulfate that is 3-O sulfated.[4] This likely interacts with the cationic face of lacritin's C-terminal amphipathic alpha helix. (3) An N-terminal chondroitin sulfate chain that also likely binds to the cationic face. Point mutagenesis of lacritin has narrowed the ligation site.[4] Altered syndecan-1 expression has been detected in several different tumor types. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. These two represent the major variants of this gene and encode the same protein.[5]


It is a useful marker for plasma cells,[6] but only if the cells tested are already known to be derived from blood.[7]


  1. ^ Mali M, Jaakkola P, Arvilommi AM, Jalkanen M (April 1990). "Sequence of human syndecan indicates a novel gene family of integral membrane proteoglycans". J. Biol. Chem. 265 (12): 6884–9.  
  2. ^ Ala-Kapee M, Nevanlinna H, Mali M, Jalkanen M, Schröder J (September 1990). "Localization of gene for human syndecan, an integral membrane proteoglycan and a matrix receptor, to chromosome 2". Somat. Cell Mol. Genet. 16 (5): 501–5.  
  3. ^ a b Ma P, Beck SL, Raab RW, McKown RL, Coffman GL, Utani A, Chirico WJ, Rapraeger AC, Laurie GW (September 2006). "Heparanase deglycanation of syndecan-1 is required for binding of the epithelial-restricted prosecretory mitogen lacritin". The Journal of Cell Biology 174 (7): 1097–106.  
  4. ^ a b c Zhang Y, Wang N, Raab RW, McKown RL, Irwin JA, Kwon I, van Kuppevelt TH, Laurie GW (March 2013). "Targeting of heparanase-modified syndecan-1 by prosecretory mitogen lacritin requires conserved core GAGAL plus heparan and chondroitin sulfate as a novel hybrid binding site that enhances selectivity". The Journal of Biological Chemistry 288 (17): 12090–101.  
  5. ^ "Entrez Gene: SDC1 syndecan 1". 
  6. ^ Rawstron AC (May 2006). "Immunophenotyping of plasma cells". Curr Protoc Cytom. Chapter 6: Unit6.23.  
  7. ^ O'Connell FP, Pinkus JL, Pinkus GS (February 2004). "CD138 (syndecan-1), a plasma cell marker immunohistochemical profile in hematopoietic and nonhematopoietic neoplasms". Am. J. Clin. Pathol. 121 (2): 254–63.  

Further reading

  • David G (1992). "Structural and functional diversity of the heparan sulfate proteoglycans". Adv. Exp. Med. Biol. 313: 69–78.  
  • Jaakkola P, Jalkanen M (1999). "Transcriptional regulation of Syndecan-1 expression by growth factors". Prog. Nucleic Acid Res. Mol. Biol. Progress in Nucleic Acid Research and Molecular Biology 63: 109–38.  
  • Wijdenes J, Dore JM, Clement C, Vermot-Desroches C (2003). "CD138". J. Biol. Regul. Homeost. Agents 16 (2): 152–5.  
  • Lories V, Cassiman JJ, Van den Berghe H, David G (1992). "Differential expression of cell surface heparan sulfate proteoglycans in human mammary epithelial cells and lung fibroblasts". J. Biol. Chem. 267 (2): 1116–22.  
  • Vainio S, Jalkanen M, Bernfield M, Saxén L (1992). "Transient expression of syndecan in mesenchymal cell aggregates of the embryonic kidney". Dev. Biol. 152 (2): 221–32.  
  • Kiefer MC, Ishihara M, Swiedler SJ et al. (1992). "The molecular biology of heparan sulfate fibroblast growth factor receptors". Ann. N. Y. Acad. Sci. 638: 167–76.  
  • Ala-Kapee M, Nevanlinna H, Mali M et al. (1990). "Localization of gene for human syndecan, an integral membrane proteoglycan and a matrix receptor, to chromosome 2". Somat. Cell Mol. Genet. 16 (5): 501–5.  
  • Mali M, Jaakkola P, Arvilommi AM, Jalkanen M (1990). "Sequence of human syndecan indicates a novel gene family of integral membrane proteoglycans". J. Biol. Chem. 265 (12): 6884–9.  
  • Sanderson RD, Lalor P, Bernfield M (1992). "B lymphocytes express and lose syndecan at specific stages of differentiation". Cell Regul. 1 (1): 27–35.  
  • Asundi VK, Carey DJ (1995). "Self-association of N-syndecan (syndecan-3) core protein is mediated by a novel structural motif in the transmembrane domain and ectodomain flanking region". J. Biol. Chem. 270 (44): 26404–10.  
  • Zhang L, David G, Esko JD (1995). "Repetitive Ser-Gly sequences enhance heparan sulfate assembly in proteoglycans". J. Biol. Chem. 270 (45): 27127–35.  
  • Barillari G, Gendelman R, Gallo RC, Ensoli B (1993). "The Tat protein of human immunodeficiency virus type 1, a growth factor for AIDS Kaposi sarcoma and cytokine-activated vascular cells, induces adhesion of the same cell types by using integrin receptors recognizing the RGD amino acid sequence". Proc. Natl. Acad. Sci. U.S.A. 90 (17): 7941–5.  
  • Spring J, Goldberger OA, Jenkins NA et al. (1994). "Mapping of the syndecan genes in the mouse: linkage with members of the myc gene family". Genomics 21 (3): 597–601.  
  • Sneed TB, Stanley DJ, Young LA, Sanderson RD (1994). "Interleukin-6 regulates expression of the syndecan-1 proteoglycan on B lymphoid cells". Cell. Immunol. 153 (2): 456–67.  
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4.  
  • Kokenyesi R, Bernfield M (1994). "Core protein structure and sequence determine the site and presence of heparan sulfate and chondroitin sulfate on syndecan-1". J. Biol. Chem. 269 (16): 12304–9.  
  • Albini A, Benelli R, Presta M et al. (1996). "HIV-tat protein is a heparin-binding angiogenic growth factor". Oncogene 12 (2): 289–97.  
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806.  
  • Kaukonen J, Alanen-Kurki L, Jalkanen M, Palotie A (1997). "The mapping and visual ordering of the human syndecan-1 and N-myc genes near the telomeric region of chromosome 2p". Hum. Genet. 99 (3): 295–7.  

External links