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Gene Review:

LOC390387 - similar to Striatin

Homo sapiens

This record was replaced with 100133284.

Jongstra-Bilen, J. et al., Franco, S. et al., Espert, L. et al., Terranova, R. et al., Sinkora, M. et al., et al.

Tedder, Sato, Poe, Fujimoto,

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Disease relevance of LOC390387

This study examines LSP1-deficient (Lsp1(-/-)) mice for the development of myeloid and lymphocytic cell populations and their response to the development of peritonitis induced by thioglycollate (TG) and to a T-dependent antigen [1].

High impact information on LOC390387

The same phenomena occurred in a T cell line and in transfected HEK.293 cells that expressed both wild-type CXCR4 and a truncated form of CD4 that is unable to bind the lymphocyte-specific protein kinase Lck [2].
Our data demonstrate that LSP1 is a negative regulator of neutrophil chemotaxis [1].
The level of peritoneal lymphocytes is decreased in Lsp1(-/-) mice without affecting a particular lymphocytic subset [1].
LSP1 modulates leukocyte populations in resting and inflamed peritoneum [1].
Lsp1(-/-) mice exhibit significantly higher levels of resident macrophages in the peritoneum compared to wild-type (wt) mice, whereas the development of myeloid cells is normal [1].

Biological context of LOC390387

Errors in the repair of both general and lymphocyte-specific DSBs can lead to oncogenic chromosomal translocations . Here, we review recent advances in understanding factors and protein complexes involved in the response to DNA DSBs with a focus on the B lymphocyte specific process of CSR [3].
On injection of TG, the Lsp1(-/-) mice exhibit an accelerated kinetics of changes in peritoneal macrophage and neutrophil numbers as compared to wt including increased influx of these cells [1].
Lymphocyte-specific protein 1, recently renamed leukocyte-specific protein 1 (LSP1), is an F-actin binding protein expressed in lymphocytes, macrophages, and neutrophils in mice and humans [1].
In this study, we have analyzed gammadelta thymocyte subsets with respect to behavior during cultivation, cell cycle status, and lymphocyte-specific transcripts [4].
Inhibition of HDAC activity during reprogramming selectively blocks the silencing of lymphocyte-specific genes but does not prevent the establishment of muscle-specific gene expression [5].

Associations of LOC390387 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 [1].
B-lymphocyte signal transduction in response to anti-immunoglobulin and bacterial lipopolysaccharide [6].
Development of N-4,6-pyrimidine-N-alkyl-N'-phenyl ureas as orally active inhibitors of lymphocyte specific tyrosine kinase [7].

Regulatory relationships of LOC390387

CD19 regulates intrinsic B lymphocyte signal transduction and activation through a novel mechanism of processive amplification [8].
CD19 and CD22 regulate a B lymphocyte signal transduction pathway that contributes to autoimmunity [9].

Other interactions of LOC390387

Complementary roles for CD19 and Bruton's tyrosine kinase in B lymphocyte signal transduction [10].

References

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]
Autophagy is involved in T cell death after binding of HIV-1 envelope proteins to CXCR4. Espert, L., Denizot, M., Grimaldi, M., Robert-Hebmann, V., Gay, B., Varbanov, M., Codogno, P., Biard-Piechaczyk, M. J. Clin. Invest. (2006) [Pubmed]
Pathways that suppress programmed DNA breaks from progressing to chromosomal breaks and translocations. Franco, S., Alt, F.W., Manis, J.P. DNA Repair (Amst.) (2006) [Pubmed]
Two Groups of Porcine TCR{gamma}{delta}+ Thymocytes Behave and Diverge Differently. Sinkora, M., Sinkorov??, J., Cimburek, Z., Holtmeier, W. J. Immunol. (2007) [Pubmed]
Acquisition and extinction of gene expression programs are separable events in heterokaryon reprogramming. Terranova, R., Pereira, C.F., Du Roure, C., Merkenschlager, M., Fisher, A.G. J. Cell. Sci. (2006) [Pubmed]
B-lymphocyte signal transduction in response to anti-immunoglobulin and bacterial lipopolysaccharide. DeFranco, A.L., Gold, M.R., Jakway, J.P. Immunol. Rev. (1987) [Pubmed]
Development of N-4,6-pyrimidine-N-alkyl-N'-phenyl ureas as orally active inhibitors of lymphocyte specific tyrosine kinase. Maier, J.A., Brugel, T.A., Sabat, M., Golebiowski, A., Laufersweiler, M.J., VanRens, J.C., Hopkins, C.R., De, B., Hsieh, L.C., Brown, K.K., Easwaran, V., Janusz, M.J. Bioorg. Med. Chem. Lett. (2006) [Pubmed]
CD19 regulates intrinsic B lymphocyte signal transduction and activation through a novel mechanism of processive amplification. Fujimoto, M., Poe, J.C., Hasegawa, M., Tedder, T.F. Immunol. Res. (2000) [Pubmed]
CD19 and CD22 regulate a B lymphocyte signal transduction pathway that contributes to autoimmunity. Tedder, T.F., Sato, S., Poe, J.C., Fujimoto, M. The Keio journal of medicine. (2000) [Pubmed]
Complementary roles for CD19 and Bruton's tyrosine kinase in B lymphocyte signal transduction. Fujimoto, M., Poe, J.C., Satterthwaite, A.B., Wahl, M.I., Witte, O.N., Tedder, T.F. J. Immunol. (2002) [Pubmed]

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