Overexpression in colorectal carcinoma of two lysosomal enzymes, CLN2 and CLN1, involved in neuronal ceroid lipofuscinosis

Abstract

The volume change, ΔVh,, accompanying the hydrophobic hydration associated with the volume phase transition in Poly(N‐isopropylacrylamide) gels was measured by a simple method. The hydration accompanies a negative ΔVh′−2.5 cm3/mol. The P‐T phase diagram, the coexistence curve, for the gels was determined from the swelling ratio‐pressure curves up to 350 MPa for various constant temperatures. The contour of the coexistence curve is shaped like an ellipsoid on the P‐T plain, which is a feature peculiar to the reversible pressure‐temperature denaturation of a protein. The thermodynamic analysis of the Clausius–Clapeyron relation for the measured ΔVh elucidates that the obtained coexistence curve represents the phase boundary between thermodynamic different phases like the two phases, native and denatured, of a protein and gives the transition enthalpy, ΔH, 5.2kJ/mol by estimate, which well coincides with the transition heat measured by a calorimetric method. Considering the volume‐dependent free energy, Δvmi · P, for the mixing free energy of the gel, we can fit the calculated curve to the measured swelling ratio‐pressure curve of PNIPA gels. The value of Δvmi changes the sign from negative to positive above around 100MPa. © 2005 Wiley Periodicals, Inc. J Appl Polym Sci 97: 405–412, 2005

Cathepsin D, a Lysosomal Protease, Regulates ABCA1-mediated Lipid Efflux

“…CTSD is involved in intracellular catabolism in lysosomal compartments but also functions in hormone and antigen processing (24 -26). CTSD has been implicated in mitogenic activity in certain cancers (27,28), which may be related to the secretion of its pro-form (24), lysosomal membrane permeabilization, and apoptosis (29). In addition, genetic variants in CTSD have been identified as a risk factor for Alzheimer disease (30) and are the causative gene of neuronal ceroid lipofuscinosis (31,32).…”

Effect of acute hypoxic shock on the rat brain morphology and tripeptidyl peptidase I activity

“…Cells over-expressing TPPI have been shown to release the enzyme in the extracellular matrix, where it can act as a matrix protease. By hydrolyzing proteins in the extracellular matrix it opens free spaces for metastasizing tumor cells and probably for newly forming blood vessels in the process of neovascularization (Tsukamato et al, 2006). We also observed a diffuse reaction of the enzyme around some blood vessels.…”

“…However, the increase of TPPI activity 12 h to a day post-treatment is clear evidence that the enzyme activity is needed in the rat brain exactly in that period. Over-expression of TPPI is reported in the invasive front of some metastatic tumors (Altorjay et al, 2005;Tsukamato et al, 2006) which are well known to be characterized by hypoxic microenvironment (Vaupel and Harrison, 2004;Melillo, 2014). Cells over-expressing TPPI have been shown to release the enzyme in the extracellular matrix, where it can act as a matrix protease.…”

Revealing ETC-1922159 Affected Unknown 3<em>^rd</em> order WNT10B-X-X Combinations, in Silico

“…Defects in these genes have been implicated in infantile neuronal ceroid lipofuscinosis 148 & 149 . Tsukamoto et al 150 observe overexpression of CLN1 in colorectal cancer which encodes PPT for removal of fatty acids from fattyacylated cysteineresidues in proteins 148 . Consistent with these, ETC-1922159 treatment of colorectal cancer cells lead to the the down regulation of PPT1 and the pipeline indicates this with a low rank of 91.…”