High impact information on KRT34

• These data suggest that tyrosine phosphorylation of pp120/HA4 may regulate Ca2+/Mg(2+)-dependent ecto-ATPase activity [1].
• Insulin binding to the alpha-subunit of its receptor stimulates the receptor tyrosine kinase to phosphorylate the beta-subunit and several endogenous protein substrates, including pp120/HA4, a liver-specific plasma membrane glycoprotein of M(r) 20,000 [1].
• In NIH 3T3 cells co-expressing the insulin receptor and pp120/HA4, insulin caused a 2-fold increase in ecto-ATPase activity [1].
• The current investigation reports on the synthesis of four types of phase-pure hydroxyapatite with varying levels of porosity (HA1-HA4), and with defined levels of macro- and microporosities [2].
• 2. Seven compounds were isolated of which four were identified as follows: Ha-1, 5-hydroxytryptamine; Ha-3, GSPYFVamide; Ha-4, pQPPLPRYamide; Ha-5, SGYLAFPRMamide [3].

Biological context of KRT34

• Insulin-stimulated phosphorylation of recombinant pp120/HA4, an endogenous substrate of the insulin receptor tyrosine kinase [1].

Anatomical context of KRT34

• 3. Ha-4, pQPPLPRYamide, was found to excite the heart of H. aspersa, relax the esophagus and both excite (mainly) and inhibit central neurons [3].

Analytical, diagnostic and therapeutic context of KRT34

• All were well polarized, as shown by the formation of spherical and even tubular BC-like structures and by the restricted localization at the BC, visualized by immunofluorescence, of the apical membrane marker HA4, a possible bile acid carrier [4].

References