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Gene Review

LSP1  -  lymphocyte-specific protein 1

Homo sapiens

Synonyms: 47 kDa actin-binding protein, 52 kDa phosphoprotein, Lymphocyte-specific antigen WP34, Lymphocyte-specific protein 1, WP34, ...
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Disease relevance of LSP1


High impact information on LSP1

  • The protein p56lck (Lck) is a Src-like, lymphocyte-specific tyrosine kinase [5].
  • Cross-linking of this lymphocyte-specific protein, designated TACI (transmembrane activator and CAML-interactor), on the surface of transfected Jurkat cells with TACI-specific antibodies led to activation of the transcription factors NF-AT, AP-1, and NFkappaB [6].
  • A new technique of direct binding of radioactive DNA was used to screen a complementary DNA expression library from the BJAB cell line in lambda gt11 phage to derive molecular cDNA clones representing a putative B lymphocyte-specific octamer binding protein [7].
  • Lymphoid enhancer-binding factor 1 (LEF-1) is a pre-B and T lymphocyte-specific nuclear protein that participates in the regulation of the T-cell antigen receptor (TCR) alpha enhancer by binding to the nucleotide sequence 5'-CCTTTGAA [8].
  • CARMA1 is a lymphocyte-specific member of the membrane-associated guanylate kinase (MAGUK) family of scaffolding proteins, which coordinate signaling pathways emanating from the plasma membrane [9].

Biological context of LSP1


Anatomical context of LSP1

  • LSP1 modulates leukocyte populations in resting and inflamed peritoneum [10].
  • Since its overexpression is implicated in the functional pathogenesis of a novel human neutrophil motile dysfunction and microfilamentous cytoskeletal abnormality (NAD 47/89), finding LSP1 in all human leukocytes suggests that it plays a role in regulating microfilamentous cytoskeleton structure and motile function in all leukocytes [13].
  • This suggests that regulation of LSP1 expression in myeloid cells may be a functionally important event [13].
  • By immunoblot, LSP1 is strongly expressed in PMN, less expressed in lymphocytes and monocytes (30-40% and 55-65% of the PMN level, respectively) [13].
  • The presence of LSP1 protein in medullary thymocytes, but only in scattered cortical thymocytes, provided additional evidence for heterogeneity of expression in T cells [1].

Associations of LSP1 with chemical compounds

  • LSP1(-) neutrophils demonstrate an enhanced chemotactic response in vitro to N-formyl methionyl-leucyl-phenylalanine (FMLP) and to the C-X-C chemokine, KC, indicating that their enhanced influx into the peritoneum may be a result of increased motility [10].
  • As the anti-LSP1 reagent used in the present study recognizes a formalin-resistant epitope it should be of considerable value in the diagnosis of routinely fixed material [1].
  • Mouse LSP1 protein contains 330 amino acids and contains an NH2-terminal acidic domain of approximately 177 amino acids [12].
  • Mock transfectants without LSP1 (U937(-)) and cell lines with LSP1 levels similar to those of monocytes (U937(+)) or 4-fold those of monocytes (U937(+)) express LSP1 as indicated and express other actin-binding proteins at normal levels before or after monocytic induction (MI) with dibutyryl cyclic adenosine monophosphate [14].
  • The C-terminal domains of the mouse and human LSP1 proteins are highly conserved and include several conserved, putative serine/threonine phosphorylation sites [15].

Physical interactions of LSP1


Regulatory relationships of LSP1


Other interactions of LSP1


Analytical, diagnostic and therapeutic context of LSP1

  • By immunoblot and Northern blot, LSP1 is minimally expressed in U-PLB985 and U-HL60 (< 10% of the PMN level) and is weakly expressed in the B lymphoid cell line Daudi, but is not expressed in the pro-B, pre-B, T lymphoid cell lines tested, U-U937 or MI-U937 [13].
  • Immunohistochemistry and three-color flow cytometry analysis of fetal or postnatal thymocytes revealed that LSP1 was increasingly expressed during intrathymic human T-cell maturation [11].
  • Site-directed mutagenesis of the basic amino acids in the KRYK (VI) or KYEK (VII) sequences to acidic amino acids create mutants that bind F-actin with lower affinity than full-length wild-type LSP1 [18].
  • Immunoprecipitation of LSP1 protein from 32P-orthophosphate-loaded cells show that both the mouse and human LSP1 proteins are phosphoproteins [15].
  • To define the hair-forming domains of LSP1, the relationship to the known F-actin binding domains, and binding domain interactions, LSP1 truncates, which include or exclude the different F-actin binding domains, were created by PCR [4].


  1. Lymphocyte-specific protein 1: a specific marker of human leucocytes. Pulford, K., Jones, M., Banham, A.H., Haralambieva, E., Mason, D.Y. Immunology (1999) [Pubmed]
  2. Lymphocyte-specific protein 1 expression in eukaryotic cells reproduces the morphologic and motile abnormality of NAD 47/89 neutrophils. Howard, T.H., Hartwig, J., Cunningham, C. Blood (1998) [Pubmed]
  3. Leucocyte-specific protein (LSP1) in malignant lymphoma and Hodgkin's disease. Marafioti, T., Jabri, L., Pulford, K., Brousset, P., Mason, D.Y., Delsol, G. Br. J. Haematol. (2003) [Pubmed]
  4. Hair-forming activity of human lymphocyte specific protein 1 requires cooperation between its caldesmon-like domains and the villin headpiece-like domains. Zhang, Q., Li, Y., Howard, T.H. Cell Motil. Cytoskeleton (2001) [Pubmed]
  5. Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck. Eck, M.J., Shoelson, S.E., Harrison, S.C. Nature (1993) [Pubmed]
  6. NF-AT activation induced by a CAML-interacting member of the tumor necrosis factor receptor superfamily. von Bülow, G.U., Bram, R.J. Science (1997) [Pubmed]
  7. Cloning of a lymphoid-specific cDNA encoding a protein binding the regulatory octamer DNA motif. Staudt, L.M., Clerc, R.G., Singh, H., LeBowitz, J.H., Sharp, P.A., Baltimore, D. Science (1988) [Pubmed]
  8. DNA-binding properties of the HMG domain of the lymphoid-specific transcriptional regulator LEF-1. Giese, K., Amsterdam, A., Grosschedl, R. Genes Dev. (1991) [Pubmed]
  9. CARMA1 is a critical lipid raft-associated regulator of TCR-induced NF-kappa B activation. Gaide, O., Favier, B., Legler, D.F., Bonnet, D., Brissoni, B., Valitutti, S., Bron, C., Tschopp, J., Thome, M. Nat. Immunol. (2002) [Pubmed]
  10. LSP1 modulates leukocyte populations in resting and inflamed peritoneum. Jongstra-Bilen, J., Misener, V.L., Wang, C., Ginzberg, H., Auerbach, A., Joyner, A.L., Downey, G.P., Jongstra, J. Blood (2000) [Pubmed]
  11. Developmental regulation of lymphocyte-specific protein 1 (LSP1) expression in thymus during human T-cell maturation. Palker, T.J., Fong, A.M., Scearce, R.M., Patel, D.D., Haynes, B.F. Hybridoma (1998) [Pubmed]
  12. The lymphocyte-specific protein LSP1 binds to F-actin and to the cytoskeleton through its COOH-terminal basic domain. Jongstra-Bilen, J., Janmey, P.A., Hartwig, J.H., Galea, S., Jongstra, J. J. Cell Biol. (1992) [Pubmed]
  13. The actin-binding protein, lymphocyte-specific protein 1, is expressed in human leukocytes and human myeloid and lymphoid cell lines. Li, Y., Guerrero, A., Howard, T.H. J. Immunol. (1995) [Pubmed]
  14. LSP1 modulates the locomotion of monocyte-differentiated U937 cells. Li, Y., Zhang, Q., Aaron, R., Hilliard, L., Howard, T.H. Blood (2000) [Pubmed]
  15. Human and mouse LSP1 genes code for highly conserved phosphoproteins. Jongstra-Bilen, J., Young, A.J., Chong, R., Jongstra, J. J. Immunol. (1990) [Pubmed]
  16. Lymphocyte-specific Ca2+-binding protein LSP1 is associated with the cytoplasmic face of the plasma membrane. Klein, D.P., Jongstra-Bilen, J., Ogryzlo, K., Chong, R., Jongstra, J. Mol. Cell. Biol. (1989) [Pubmed]
  17. The lymphocyte-specific tyrosine protein kinase p56lck is endocytosed in Jurkat cells stimulated via CD2. Marie-Cardine, A., Maridonneau-Parini, I., Ferrer, M., Danielian, S., Rothhut, B., Fagard, R., Dautry-Varsat, A., Fischer, S. J. Immunol. (1992) [Pubmed]
  18. Human lymphocyte-specific protein 1, the protein overexpressed in neutrophil actin dysfunction with 47-kDa and 89-kDa protein abnormalities (NAD 47/89), has multiple F-actin binding domains. Zhang, Q., Li, Y., Howard, T.H. J. Immunol. (2000) [Pubmed]
  19. Expression of lymphocyte-specific chemokines in human malignant glioma: Essential role of LARC in cellular immunity of malignant glioma. Kimura, T., Takeshima, H., Nomiyama, N., Nishi, T., Kino, T., Kochi, M., Kuratsu, J.I., Ushio, Y. Int. J. Oncol. (2002) [Pubmed]
  20. Calcium-dependent cyclosporin A-sensitive activation of the interleukin-2 promoter by p56lck. Baldari, C.T., Heguy, A., Telford, J.L. J. Biol. Chem. (1993) [Pubmed]
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