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Gene Review

Lphn2  -  latrophilin 2

Mus musculus

Synonyms: AI450192, CIRL-2, Calcium-independent alpha-latrotoxin receptor 2, Gm619, Kiaa0786, ...
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High impact information on Lphn2

  • To study the effects of altered carbohydrate structure on Ab effector function, we have used gene transfection techniques to produce mouse-human chimeric IgG1 Abs in the Chinese hamster ovary (CHO) cell line Lec 1, which is incapable of processing the high-mannose intermediate through the terminal glycosylation steps [1].
  • The altered carbohydrates expressed at the surface of Lec9 cells appeared to be responsible for their loss of tumorigenicity, because revertants for lectin resistance were able to form tumors, and a double mutant (Lec9.Lec1) that expressed a Lec1 glycosylation phenotype also formed tumors [2].
  • We had previously shown that IgG1 Abs produced in the cell line Lec 1, which attaches a high-mannose intermediate carbohydrate, were severely deficient in complement activation, showed a slightly reduced affinity for Fc gammaRI, and had a reduced in vivo half-life [3].
  • Comparison of GnTI sequences detected three mutations within the luminal domain of Lec1 GnTI, each resulting in an amino acid substitution [4].
  • Glycosylation defect in Lec1 Chinese hamster ovary mutant is due to a point mutation in N-acetylglucosaminyltransferase I gene [4].

Anatomical context of Lphn2

  • We also produced IgG1 Abs in Pro-5, the wild-type CHO cell line that is the parent of Lec 1 [1].
  • Both Lec1 GnTI and the GnTI mutant (Cys123 --> Arg123) are correctly localized to the Golgi apparatus, indicating that the inactive GnTI molecules are sufficiently well folded for efficient transport from the endoplasmic reticulum [4].

Associations of Lphn2 with chemical compounds

  • Analysis of the attached carbohydrates shows those present on IgG1-Lec 1 were mannose terminated [5].

Other interactions of Lphn2


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