High impact information on mas

• We propose that mas acts via its modified serine protease motif, either as a novel adhesion molecule and/or as a competitive antagonist of serine proteases, to stabilize muscle attachment [1].
• During embryonic development, the mas amino- and carboxy-terminal polypeptides are differentially localized [1].
• This mutant phenotype suggests that mas normally acts to stabilize cell-matrix interaction and represents a novel functional and limiting component in the adhesion process. mas encodes a 1047-amino-acid preproprotein that is further processed by proteolytic cleavage to generate two polypeptides [1].
• The evolutionary tree obtained shows that the visual pigment genes and mas oncogene form one cluster and that the receptor genes form another [2].
• Total loss of mas function is lethal and results in aberrations in the embryonic central and peripheral nervous systems, consistent with a role in axonal guidance [3].

Biological context of mas

• This Tenebrio masquerade-like serine proteinase homologue (Tm-mas) contains a trypsin-like serine proteinase domain in the C-terminal region, except for the substitution of Ser to Gly at the active site triad, and a disulfide-knotted domain at the amino-terminal region [4].

Anatomical context of mas

• The55-kDa zymogen form of Tm-mas was detected in the hemolymph when PO activity was not evident [4].

Regulatory relationships of mas

• This suggests that the purified 45-kDa Tm-mas is an activated form of pro-PO activating factor [4].

Other interactions of mas

• Furthermore, when Tenebrio hemolymph was incubated with Ca2+ and beta-1,3-glucan, the conversion of pro-PO to PO and the 55-kDa zymogen Tm-mas to the 45-kDa protein, was faster than in the presence of Ca2+ only [4].

References