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SPCS3  -  signal peptidase complex subunit 3 homolog...

Homo sapiens

Synonyms: FLJ22649, Microsomal signal peptidase 22/23 kDa subunit, PRO3567, SPC22, SPC22/23, ...
 
 
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Disease relevance of SPCS3

  • SPC3, a synthetic peptide derived from the V3 domain of human immunodeficiency virus type 1 (HIV-1) gp120, inhibits HIV-1 entry into CD4+ and CD4- cells by two distinct mechanisms [1].
  • In agreement with this hypothesis, SPC3 treatment after HIV-1 exposure dramatically reduced the number of infected cells without altering gp120-CD4 interaction or viral gene expression [1].
  • V3 loop-derived peptide SPC3 inhibits infection of CD4- and galactosylceramide- cells by LAV-2/B [2].
 

High impact information on SPCS3

  • In the present study, we investigated the mechanisms of action of SPC3 in these cell types--i.e., CD4+ lymphocytes and CD4- epithelial cells expressing galactosylceramide (GalCer), an alternative receptor for HIV-1 gp120 [1].
  • Recently, we reported that a synthetic multibranched peptide (SPC3) containing eight V3-loop consensus motifs (GPGRAF) inhibited HIV-1 infection in both CD4+ and CD4- susceptible cells [1].
  • Accordingly, SPC3 was found to inhibit the binding of gp120 to the GalCer receptor [1].
  • In contrast, SPC3 blocked HIV-1 entry into CD4-/GalCer+ human colon epithelial cells when present in competition with HIV-1 but had no effect when added after infection [1].
  • Liposome-associated SPC3 were tested for both inhibition of cell-cell fusion and infection with HIV-1 clones [3].
 

Chemical compound and disease context of SPCS3

  • Thus, the data suggest that SPC3 affects HIV-1 infection by two distinct mechanisms: (i) prevention of GalCer-mediated HIV-1 attachment to the surface of CD4-/GalCer+ cells and (ii) post-binding inhibition of HIV-1 entry into CD4+ lymphocytes [1].
 

Biological context of SPCS3

 

Anatomical context of SPCS3

  • These data suggested that SPC3 did not inhibit the binding of HIV-1 to CD4+ lymphocytes but interfered with a post-binding step necessary for virus entry [1].
  • SPC3 was found to interact with CD4+ cell membrane with a K0.5 value in the range of 500 nM [5].
  • Syncytium formation was impaired when human CD4+ cells expressed recombinant HIV Env in the presence of SPC3 [4].
  • SPC3 inhibited the LAV-2/B-mediated infection of B-cell line which does not express the CD4 and the galactosylceramide molecules on their cell surface, suggesting an SPC3-sensitive CD4/galactosylceramide-independent pathway of viral infection in HIV susceptible cells [2].
  • Budding of secretory granules causes the lumen to acidify to <pH 6.0, which is both necessary and sufficient to trigger SPC3-mediated proteolytic conversion of proopiomelanocortin to ACTH [6].
 

Associations of SPCS3 with chemical compounds

  • These data suggest that the liposome approach may be used to improve SPC3 antiviral efficacy [3].
  • Moreover, only some of these anti-HIV active analogs inhibited the binding of [3H]suramin (a polysulfonyl compound which displays a high affinity for the V3 loop) to SPC3, a synthetic peptide which contains the conserved GPGRAF region of the V3 loop [7].
  • SPC3 was entrapped in various liposomal formulations, either different in size (mean diameter of 100 and 250 nm), SPC3 concentration or cholesterol content [3].
 

Analytical, diagnostic and therapeutic context of SPCS3

  • Changes in mRNA from the SpC3 gene (Sp064) were also followed by RT-PCR [8].
  • Properties of HIV envelope expressed in the presence of SPC3, an Env-derived peptide drug under phase II clinical trials [4].

References

  1. SPC3, a synthetic peptide derived from the V3 domain of human immunodeficiency virus type 1 (HIV-1) gp120, inhibits HIV-1 entry into CD4+ and CD4- cells by two distinct mechanisms. Yahi, N., Fantini, J., Baghdiguian, S., Mabrouk, K., Tamalet, C., Rochat, H., Van Rietschoten, J., Sabatier, J.M. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  2. V3 loop-derived peptide SPC3 inhibits infection of CD4- and galactosylceramide- cells by LAV-2/B. Moulard, M., Mabrouk, K., Martin, I., Van Rietschoten, J., Rochat, H., Sabatier, J.M. J. Pept. Res. (1999) [Pubmed]
  3. Liposomal encapsulation enhances antiviral efficacy of SPC3 against human immunodeficiency virus type-1 infection in human lymphocytes. de Mareuil, J., Mabrouk, K., Doria, E., Moulard, M., de Chasteigner, S., Oughideni, R., van Rietschoten, J., Rochat, H., De Waard, M., Sabatier, J.M. Antiviral Res. (2002) [Pubmed]
  4. Properties of HIV envelope expressed in the presence of SPC3, an Env-derived peptide drug under phase II clinical trials. Barbouche, R., Fenouillet, E., Papandréou, M.J., Kiény, M.P., Sabatier, J.M. J. Pept. Res. (1998) [Pubmed]
  5. SPC3, an anti-HIV peptide construct derived from the viral envelope, binds and enters HIV target cells. Barbouche, R., Miquelis, R., Sabatier, J.M., Fenouillet, E. J. Pept. Sci. (1998) [Pubmed]
  6. Biosynthesis and secretion of pituitary hormones: dynamics and regulation. Moore, H.P., Andresen, J.M., Eaton, B.A., Grabe, M., Haugwitz, M., Wu, M.M., Machen, T.E. Arch. Physiol. Biochem. (2002) [Pubmed]
  7. Synthesis of single- and double-chain fluorocarbon and hydrocarbon galactosyl amphiphiles and their anti-HIV-1 activity. Faroux-Corlay, B., Clary, L., Gadras, C., Hammache, D., Greiner, J., Santaella, C., Aubertin, A.M., Vierling, P., Fantini, J. Carbohydr. Res. (2000) [Pubmed]
  8. Expression of SpC3, the sea urchin complement component, in response to lipopolysaccharide. Clow, L.A., Gross, P.S., Shih, C.S., Smith, L.C. Immunogenetics (2000) [Pubmed]
 
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