Disease relevance of SNIP

• Analysis of another event-related potential, P140 (a measure of the sensory processes), showed no change in response to hypoglycemia [1].
• The fractionation behavior of NCP98 is, however, similar to that of the P140 encoded by a temperature-sensitive strain of Fujinami sarcoma virus in infected cells grown at the nonpermissive temperature [2].
• In this study, for the first time in the context of infectious HIV-1 particles, we analyzed the contribution of amino acid residues (S134, I135, N136, N137, T139 and P140) in the beta7-beta8 loop for RT heterodimerization, enzymatic activity, and virus infectivity [3].
• Stability of cytadherence-related proteins P140/P110 in Mycoplasma genitalium requires MG218 and unidentified factors [4].

High impact information on SNIP

• Its tyrosine phosphorylation by integrin-mediated adhesion and EGF stimulation and its involvement in cell spreading on matrix proteins suggest that p140Cap plays a role in controlling actin cytoskeleton organization in response to adhesive and growth factor signaling [5].
• In addition p140Cap codistributes with cortical actin and actin stress fibers but not with focal adhesions [5].
• By immunofluorescence analysis, we demonstrated that in ECV304 cells plated on fibronectin, the endogenous p140Cap colocalizes with p130Cas in the perinuclear region as well as in lamellipodia [5].
• P140, an event-related potential reflecting sensory processes, was not altered [6].
• We compared the intracellular location of the product of the c-fps proto-oncogene, NCP98, with that of its viral homolog P140, the transforming protein of Fujinami sarcoma virus [2].

Biological context of SNIP

• Loss of either P140 or P110 yields a hemadsorption-negative phenotype and correlates with decreased or increased levels of cytoskeleton-related proteins MG386 and DnaK, respectively [7].
• We have deleted by homologous recombination the mg191 and mg192 genes from the MgPa operon encoding the P140 and P110 cytadhesins [7].
• Amino acids N137 and P140 in the p51 subunit of HIV-1 reverse transcriptase (RT) are part of the beta7-beta8-loop that contributes to the formation of the base of the non-nucleoside RT inhibitor (NNRTI)-binding pocket and makes up a substantial part of the dimerization interface [8].
• Preincubation of platelets with the tyrosine phosphatase inhibitor orthovanadate prevented the tyrosine dephosphorylation of P38 and P140, and reduced platelet aggregation induced by thrombin receptor activation [9].

Anatomical context of SNIP

• SIP30 is expressed abundantly in brain and slightly in testis and kidney [10].
• This fractionation behavior differs from that of P140, which is found predominantly in the particulate fraction, both in Fujinami sarcoma virus-infected chicken embryo fibroblasts and in Fujinami sarcoma virus-infected myeloblasts [2].
• Scanning electron microscopy analysis reveals the absolute requirement of P140 and P110 for the proper development of the attachment organelle [7].
• Using crossed immunoelectrophoresis with an antiserum raised against immature rat cerebellar plasma membrane preparations (anti-BPM serum) that primarily recognizes one neuronal surface antigen (D2)33, it was established that the P140 comprises the D2 protein [11].
• RESULTS: The endothelial cell count showed significant (P < .001) reduction by approximately 10% after the "Reversed Tip and Snip" technique and by approximately 15% (P < .001) after the "Divide and Conquer" technique [12].

Associations of SNIP with chemical compounds

• Activation of human platelets by thrombin or a thrombin receptor-activating peptide (TRAP) resulted in a decrease in tyrosine phosphorylation of two proteins, P38 and P140 [9].
• When platelets were stimulated under conditions that precluded the activation of glycoprotein IIb/IIIa (dissociation of the complex by EGTA at 37 degrees C) or the binding of fibrinogen (preincubation of platelets with RGDS), tyrosine dephosphorylation of P38 and P140 was not observed [9].
• Laboratory tests also proved that moistening the fly prolonged the efficacy period of the three tested products from 3 to 6 weeks in case of Alfacron SB, from 4 to 7 weeks for Snip IRB and from 7 to 9 weeks in case of Alfacron 10 WP [13].

Analytical, diagnostic and therapeutic context of SNIP

• GST-pull-down and immunoprecipitation assays showed direct binding of SIP30 to SNAP25 [10].
• CONCLUSIONS: The "Reversed Tip and Snip" phacoemulsification technique produces less endothelial cell loss than the "Divide and Conquer" technique [12].

References