Cochin University of Science and Technology

About: Cochin University of Science and Technology is a education organization based out in Kochi, Kerala, India. It is known for research contribution in the topics: Thin film & Natural rubber. The organization has 5382 authors who have published 7690 publications receiving 103827 citations. The organization is also known as: CUSAT & Cochin University.

Chipless RFID Tag Using Multiple Microstrip Open Stub Resonators

Abstract: A novel compact RFID tag employing open stubs in a microstrip transmission line is proposed. The prototype of the tag is fabricated on a substrate of dielectric constant 4.4 and loss tangent 0.0018. The tag consists of microstrip open stub resonators and cross polarized transmitting and receiving disc monopole antennas. A prototype of 8 bit data encoded tag is demonstrated in this communication. Method for enhancing the performance of the RFID tag is also proposed. Magnitude or group delay response can be used to decode the tag informations.

Plasma membrane targeting of podocin through the classical exocytic pathway: effect of NPHS2 mutations.

Abstract: Podocytes are specialized epithelial cells of the glomerulus in the kidney, which interconnect at the top of the glomerular basement membrane through the slit diaphragm, an adherens-like junction that plays a crucial role in the glomerular filtration process. Podocin, a plasma membrane anchored stomatin-like protein, is expressed in lipid rafts at the insertion of the slit diaphragm in podocytes. Mutations in NPHS2, the gene encoding podocin, are associated with inherited and sporadic cases of steroid-resistant nephrotic syndrome. Here, we show that brefeldin A induces accumulation of newly synthesized podocin in the endoplasmic reticulum, suggesting that podocin biosynthesis follows the classical secretory pathway, and we study the effect of 12 NPHS2 mutations associated with steroid-resistant nephrotic syndrome on the trafficking of the protein. We found that 9 podocin mutants were not targeted to the plasma membrane, 8 being retained in the endoplasmic reticulum and one being localized in late endosomes. Furthermore, by screening our database of patients with NPHS2 mutations, we found that podocin mutants retained in the endoplasmic reticulum are associated with earlier onset of the disease than those correctly targeted to the cell membrane. Our data suggest that most of NPHS2 mutations lead to retention of podocin in the endoplasmic reticulum and therefore provide a rationale for devising therapeutic approaches aimed at correcting the protein processing defect.